From Structure to Phenotype: Impact of Collagen Alterations on Human Health

Arseni, Lavinia; Lombardi, Anita; Orioli, Donata

doi:10.3390/ijms19051407

Cited by 186Connective tissue disorders researchCollagen: Extraction and CharacterizationCellular Mechanics and Interactions

From Structure to Phenotype: Impact of Collagen Alterations on Human Health

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Arseni, Lavinia, Lombardi, Anita, Orioli, Donata·2018·International Journal of Molecular Sciences

DOI 10.3390/ijms19051407PMC PMC5983607

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Abstract

The extracellular matrix (ECM) is a highly dynamic and heterogeneous structure that plays multiple roles in living organisms. Its integrity and homeostasis are crucial for normal tissue development and organ physiology. Loss or alteration of ECM components turns towards a disease outcome. In this review, we provide a general overview of ECM components with a special focus on collagens, the most abundant and diverse ECM molecules. We discuss the different functions of the ECM including its impact on cell proliferation, migration and differentiation by highlighting the relevance of the bidirectional cross-talk between the matrix and surrounding cells. By systematically reviewing all the hereditary disorders associated to altered collagen structure or resulting in excessive collagen degradation, we point to the functional relevance of the collagen and therefore of the ECM elements for human health. Moreover, the large overlapping spectrum of clinical features of the collagen-related disorders makes in some cases the patient clinical diagnosis very difficult. A better understanding of ECM complexity and molecular mechanisms regulating the expression and functions of the various ECM elements will be fundamental to fully recognize the different clinical entities.

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In child cohorts, the most robust relationship with joint hypermobility is for ADHD.
“With regard to psychiatry, the most robust relationship with joint hypermobility in child cohorts is for ADHD. 18–21”
From No association between joint hypermobility, musculoskeletal pain and neurodevelopmental problems in a school-based sample of 11-year-old children (2025) · cites this paper as [19]
Section 5, “Collagen Alterations in Pathological Events” (page unavailable), mentions hypermobile joints in patients with Ehlers–Danlos syndrome but discusses motor development, not psychiatric conditions. Searches for ADHD, attention-deficit/hyperactivity disorder, and joint hypermobility in child cohorts found no passage assessing the claimed relationship or comparing it with other psychiatric relationships. (LLM, conf=0.76)
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Background
Matricryptins and matrikines: biologically active fragments of the extracellular matrix
Ricard‐Blum, S., & Salza, R. (2014) · Experimental Dermatology · doi:10.1111/exd.12435 · Cited by 224 · cited 2× · see citing works
“The ectodomains of syndecans 1–4 are also matricryptins, whereas fragments derived from hyaluronan degradation regulate inflammation and wound healing ([28] and references therein).”
Background
Inheritance of a novel COL8A2 mutation defines a distinct early-onset subtype of fuchs corneal dystrophy.
Gottsch, J., Sundin, O., Liu, S. H., Jun, A. S., Broman, K., Stark, W., Vito, E. C. L., Narang, A., Thompson, J. M., & Magovern, M. (2005) · Investigative Ophthalmology and Visual Science · doi:10.1167/iovs.04-0937 · Cited by 223 · cited 1× · see citing works
“Another family with one PPCD2 patient and few FECD cases, due to heterozygous missense mutation in COL8A2, has been described [139].”
Background
COL4A3/COL4A4 mutations: from familial hematuria to autosomal-dominant or recessive Alport syndrome.
Longo, I., Porcedda, P., Mari, F., Giachino, D., Meloni, I., Deplano, C., Brusco, A., Bosio, M., Massella, L., Lavoratti, G., et al. (2002) · Kidney International · doi:10.1046/j.1523-1755.2002.00379.x · Cited by 223 · cited 1× · see citing works
“Autosomal recessive Alport syndrome presents as gross proteinuria in childhood and progression to end-stage kidney disease often before the fourth decade [120].”
Background
Variants in a Novel Epidermal Collagen Gene (COL29A1) Are Associated with Atopic Dermatitis
Söderhäll, C., Marenholz, I., Kerscher, T., Rüschendorf, F., Esparza-Gordillo, J., Worm, M., Grüber, C., Gabriele Mayr, B., Albrecht, M., Rohde, K., et al. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050242 · Cited by 223 · cited 1× · see citing works
“Lack of COL29A1 expression in the outer layers of the epidermis of ATOD patients points to a role of collagen XXIX in epidermal integrity, whose breakdown is a clinical hallmark of AD [160].”
Background
Collectins
van de Wetering, J. K., GOLDE, L. M. G. V., & Batenburg, J. J. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04040.x · Cited by 221 · cited 1× · see citing works
“Notably, collagen-like triple helical domains are found in several other proteins that do not have structural function and therefore are not considered as real collagens [65].”
Background
Extracellular microfibrils: contextual platforms for TGFβ and BMP signaling
Ramirez, F., & Rifkin, D. B. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.05.005 · Cited by 207 · see citing works
Hyaluronan synthesis and degradation in cartilage and bone
Bastow, E. R., Byers, S., Golub, S. B., Clarkin, C. E., Pitsillides, A. A., & Fosang, A. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7360-z · Cited by 201 · cited 1× · see citing works
“Hyaluronidases are a family of enzymes capable of degrading HA [51].”
Background
Cell-Matrix Interactions in Mammary Gland Development and Breast CancerPreprint
Muschler, J. L., & Streuli, C. H. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003202 · Cited by 200 · cited 1× · see citing works
“Alterations of ECM remodelling can also influence the course and progression of several other pathological conditions, including fibrosis, skin disorders and cancer [74].”
Background
A mutation in COL9A1 causes multiple epiphyseal dysplasia: further evidence for locus heterogeneity.
Czarny‐Ratajczak, M., Lohiniva, J., Rogala, P., Kozłowski, K., Perälä, M., Carter, L., Spector, T., Kołodziej, L., Seppänen, U., Glazar, R., et al. (2001) · American Journal of Human Genetics · doi:10.1086/324023 · Cited by 198 · cited 1× · see citing works
“The mother had the same mutation but she did not reveal any symptom before age 45 years [143]”
Background
Mutations in FKBP10 Cause Recessive Osteogenesis Imperfecta and Bruck Syndrome
Kelley, B., Malfait, F., Bonafė, L., Baldridge, D., Homan, E. P., Symoens, S., Willaert, A., Elcioglu, N., Maldergem, L. V., Verellen-Dumoulin, C., et al. (2010) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.250 · Cited by 186 · cited 1× · see citing works
“All the others clinical data on the 29 patients with OI type XI (mutations in FKBP10) are limited and heterogeneous regarding the age of onset, the number of fractures, the type of affected bones and the severity of the disorder [88].”
Background
Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2
Leuchter, R. H., Alanay, Y., Bank, R. A., Campos‐Xavier, B., Zankl, A., Superti‐Furga, A., & Bonafé, L. (2004) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.30231 · Cited by 185 · cited 1× · see citing works
“Mutations in this gene affect the instalment and secretion of collagen fibres from osteoblasts [163].”
Background
Interactions of the Amino-terminal Noncollagenous (NC1) Domain of Type VII Collagen with Extracellular Matrix Components
Chen, M., Marinkovich, M., Veis, A., Cai, X.-Y., Rao, C. N., O'Toole, E., & Woodley, D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.23.14516 · Cited by 173 · cited 1×
“The anchoring filaments are assembled in an antiparallel manner, tail to tail with some C-terminal overlap [62,64].”
Background
Genetic linkage of a polymorphism in the type II procollagen gene (COL2A1) to primary osteoarthritis associated with mild chondrodysplasia.
Knowlton, R., Katzenstein, P., Moskowitz, R., Weaver, E. J., Malemud, C., Pathria, M., Jimenez, S., & Prockop, D. (1990) · New England Journal of Medicine · doi:10.1056/nejm199002223220807 · Cited by 169 · cited 1× · see citing works
“Several cases have been reported, included family members over various generations [95,100,101].”
Background
Collagenase: a key enzyme in collagen turnover
Shingleton, W. D., Cawston, T. E., Hodges, D. J., & Brick, P. (1996) · Biochemistry and Cell Biology · doi:10.1139/o96-083 · Cited by 166 · cited 1× · see citing works
“Finally, lysosomes fuse together to generate large structures containing collagen and ECM fragments that undergo enzymatic digestion by cysteine cathepsins [72,73].”
Background
Plasmin activates pro‐matrix metalloproteinase‐2 with a membrane‐type 1 matrix metalloproteinase‐dependent mechanism
Monea, S., Lehti, K., Keski-oja, J., & Mignatti, P. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10126 · Cited by 165 · cited 1×
“Upon activation, MMP-2 can degrade several collagen types, fibronectin, elastin as well as gelatin, the denatured form of collagen [69].”
Background
Mutations in FKBP14 cause a variant of Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss
Baumann, M., Giunta, C., Krabichler, B., Rüschendorf, F., Zoppi, N., Colombi, M., Bittner, R. E., Quijano-Roy, S., Muntoni, F., Cirak, S., et al. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.12.004 · Cited by 162 · cited 1× · see citing works
“It catalyses the folding of COL3 and interacts with COL3, COL4 and COLX [165].”
Background
Novel hepatocyte growth factor (HGF) binding domains on fibronectin and vitronectin coordinate a distinct and amplified Met-integrin induced signalling pathway in endothelial cells
Rahman, S., Patel, Y. M., Murray, J., Patel, K., Sumathipala, R. N., Sobel, M., & Wijelath, E. (2005) · BMC Cell Biology · doi:10.1186/1471-2121-6-8 · Cited by 162 · cited 1× · see citing works
“Hepatocyte growth factor (HGF) binds to the 70 kDa N-terminal and the 40 kDa C-terminal fragments of fibronectin [15], whereas platelet-derived growth factor (PDGF) binds the type III and the variable domains of fibronectin [16].”
Background
Phenotypic Spectrum of COL4A1 Mutations: Porencephaly to Schizencephaly
Yoneda, Y., Haginoya, K., Kato, M., Osaka, H., Yokochi, K., Arai, H., Kakita, A., Yamamoto, T., Otsuki, Y., Shimizu, S.-I., et al. (2013) · Annals of Neurology · doi:10.1002/ana.23736 · Cited by 161 · cited 1× · see citing works
“Affected individuals have delayed growth and development, hypotonia, spastic hemiplegia, seizures, migraine headaches, speech problems and intellectual disability with variable severity [126].”
Background
Inherited epidermolysis bullosa: new diagnostic criteria and classification.
Intong, L., & Murrell, D. (2012) · Clinical Dermatology · doi:10.1016/j.clindermatol.2011.03.012 · Cited by 159 · cited 1×
“Patients usually do not survive more than 30 years due to severe renal complications or aggressive squamous cell carcinoma arising in the areas of repeated scarring [154].”
Background
Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase.
Bonnefoy, A., & Legrand, C. (2000) · Thrombosis Research · doi:10.1016/s0049-3848(99)00242-x · Cited by 158 · cited 1× · see citing works
“Plasmin and elastase are serine proteinases, the first degrades fibrin, fibronectin and laminin [47], whereas the latter degrades fibronectin and elastin [48].”
Background
Mutation Update for COL2A1 Gene Variants Associated with Type II Collagenopathies
Barat-Houari, M., Sarrabay, G., Gatinois, V., Fabre, A., Dumont, B., Geneviève, D., & Touitou, I. (2016) · Human Mutation · doi:10.1002/humu.22915 · Cited by 152 · cited 2×
“The cartilage appears as abnormal gelatinous texture and translucent [75].”
Background
Autosomal recessive cutis laxa syndrome revisited
Morava, E., Guillard, M., Lefeber, D., & Wevers, R. (2009) · European Journal of Human Genetics · doi:10.1038/ejhg.2009.22 · Cited by 146 · cited 2× · see citing works
“Cutis laxa is a rare skin disorder characterized by wrinkled, redundant, inelastic and sagging skin due to defective synthesis of elastic fibres and other proteins of the ECM [167].”
Background
Recessive Osteogenesis Imperfecta Caused by Missense Mutations in SPARC
Mendoza‐Londono, R., Fahiminiya, S., Majewski, J., Tétreault, M., Nadaf, J., Kannus, P., Sochett, E. B., Howard, A., Stimec, J., Dupuis, L., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2015.04.021 · Cited by 139 · cited 1× · see citing works
“Other features are decreased calf muscle mass, joint hyperlaxity and soft skin [89].”
Background
Extracellular Matrix in Development: Insights from Mechanisms Conserved between Invertebrates and VertebratesPreprint
Brown, N. H. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005082 · Cited by 127 · cited 1× · see citing works
“An example of coexistence is observed during muscle differentiation, where a sticky ECM is required to bind the extremities of the cells, whereas a slippery matrix coats the lateral sides [38].”
Background
Autosomal recessive myosclerosis myopathy is a collagen VI disorder
Merlini, L., Martoni, E., Grumati, P., Sabatelli, P., Squarzoni, S., Urciuolo, A., Ferlini, A., Gualandi, F., & Bonaldo, P. (2008) · Neurology · doi:10.1212/01.wnl.0000327611.01687.5e · Cited by 125 · cited 1× · see citing works
“Increased serum creatine kinase was also found [133].”
Background
Matricryptins derived from collagens and proteoglycans
Ricard‐Blum, S. (2010) · Frontiers in bioscience · doi:10.2741/3712 · Cited by 124 · cited 5× · see citing works
“More severe vision defects can be observed in patients with the Knobloch syndrome-1 due to alterations of the type XVIII collagen.”
BackgroundInfluential
Trichothiodystrophy: From basic mechanisms to clinical implications
Stefanini, M., Botta, E., Lanzafame, M., & Orioli, D. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.10.005 · Cited by 120 · cited 1× · see citing works
“TTD patients present a 20-fold higher mortality compared to the US general population [158,159].”
BackgroundSelf-citation
Structural basis of homo- and heterotrimerization of collagen I
Sharma, U., Carrique, L., Goff, S. V., Mariano, N., Georges, R.-N., Delolme, F., Koivunen, P., Myllyharju, J., Moali, C., Aghajari, N., et al. (2017) · Nature Communications · doi:10.1038/ncomms14671 · Cited by 119 · cited 1× · see citing works
“The most abundant collagen of the human body, the interstitial type I collagen, is made by two identical α1 and one α2 chain, which shows high sequence homology with α1 [57].”
Background
The Non-phagocytic Route of Collagen Uptake
Madsen, D. H., Ingvarsen, S. Z., Jürgensen, H. J., Melander, M. C., Kjøller, L., Moyer, A., Honoré, C., Madsen, C. A., Garred, P., Burgdorf, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.208033 · Cited by 113 · cited 1× · see citing works
“Finally, lysosomes fuse together to generate large structures containing collagen and ECM fragments that undergo enzymatic digestion by cysteine cathepsins [72,73].”
Background
Structure of Homo- and Hetero-oligomeric Meprin Metalloproteases
Bertenshaw, G. P., Norcum, M. T., & Bond, J. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208808200 · Cited by 113 · cited 6× · see citing works
“ADAMs are involved in cytokines processing and growth factor receptor shedding [43] while ADAMTS play a role in degradation of ECM components, particularly collagens and proteoglycans [44].”
BackgroundInfluential
Novel COL4A1 mutations associated with HANAC syndrome: A role for the triple helical CB3[IV] domain
Plaisier, E., Chen, Z.-Y., Gekeler, F., Benhassine, S., Dahan, K., Marro, B., Alamowitch, S., Pâques, M., & Ronco, P. (2010) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.33659 · Cited by 104 · cited 1×
“In addition, patients may manifest eye problems, like arterial retinal tortuosity, cataract and abnormality called Axenfeld-Rieger anomaly [124].”
Background
Genetic risk factors for spontaneous intracerebral haemorrhage
Carpenter, A., Singh, I. P., Gandhi, C. D., & Prestigiacomo, C. J. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.226 · Cited by 103 · cited 1× · see citing works
“The mutated vascular collagen diminishes the tensile strength of vessels and increases their fragility, which can lead to haemorrhage [128].”
Background
Loss of dermatan sulfate epimerase (DSE) function results in musculocontractural Ehlers–Danlos syndrome
Müller, T., Mizumoto, S., Suresh, I., Komatsu, Y., Vodopiutz, J., Dündar, M., Straub, V. W., Lingenhel, A., Melmer, A., Lechner, S., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt227 · Cited by 103 · cited 2× · see citing works
“EDSMC1 and 2 share most of the clinical features, even though the majority of cases (31) refer to the EDSMC1 and only three cases are reported for the EDSMC2 type [78].”
Background
A frequent functional SNP in theMMP1promoter is associated with higher disease severity in recessive dystrophic epidermolysis bullosa
Titeux, M., Pendaries, V., Tonasso‐Calvière, L., Décha, A., Bodemer, C., & Hovnanian, A. (2007) · Human Mutation · doi:10.1002/humu.20647 · Cited by 101 · cited 2× · see citing works
“An association between disease severity and specific SNP in MMP1 gene (*120353) was found in three affected members of one family and in a cohort of 31 unrelated French RDEB patients [136].”
Background
Collagenous transmembrane proteins: collagen XVII as a prototype
Franzke, C.-W., Tasanen, K., Schumann, H., & Bruckner‐Tuderman, L. (2003) · Matrix Biology · doi:10.1016/s0945-053x(03)00051-9 · Cited by 101 · cited 1× · see citing works
“Collagen types XIII and XVII are included in this group [61].”
Background
A loss of function mutation in the COL9A2 gene causes autosomal recessive Stickler syndrome
Baker, S., Booth, C., Fillman, C., Shapiro, M., Blair, M., Hyland, J., & Ala-kokko, L. (2011) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.34071 · Cited by 101 · cited 2× · see citing works
“None of the family members was known to have cleft palate and, although there was short stature in childhood, normal height was found in adults [108].”
Background
Novel and emerging therapies in the treatment of recessive dystrophic epidermolysis bullosa.
Rashidghamat, E., & McGrath, J. (2017) · Intractable & Rare Diseases Research · doi:10.5582/irdr.2017.01005 · Cited by 99 · cited 1×
“DDEB and RDEB are also known as Cockayne-Touraine disease and Hallopeau-Siemens disease, respectively [135].”
Background
Dominant mutations in the type II collagen gene, COL2A1, produce spondyloepimetaphyseal dysplasia, Strudwick type
Tiller, G. E., Polumbo, P. A., Weis, M. A., Bogaert, R., Lachman, R. S., Cohn, D. H., Rimoin, D. L., & Eyre, D. R. (1995) · Nature Genetics · doi:10.1038/ng0995-87 · Cited by 93 · cited 1× · see citing works
“The disorder is a skeletal dysplasia with platyspondyly and brachydactyly E-like changes (short meta-carpals and metatarsals, short distal phalanges in the hand and feet) [107].”
Background
Topical Review: Schizencephaly: Clinical Spectrum, Epilepsy, and Pathogenesis
Granata, T., Freri, E., Caccia, C., Setola, V., Taroni, F., & Battaglia, G. (2004) · Journal of Child Neurology · doi:10.1177/08830738040190030801 · Cited by 92 · cited 1×
“Type II is associated with mental retardation, seizures, hypotonia, spasticity, inability to walk or speak and blindness [127].”
Background
Recurrent De Novo Mutations Affecting Residue Arg138 of Pyrroline-5-Carboxylate Synthase Cause a Progeroid Form of Autosomal-Dominant Cutis Laxa
Fischer‐Zirnsak, B., Escande‐Beillard, N., Ganesh, J., Tan, Y. X., Al-Bughaili, M., Lin, A. E., Sahai, I., Bahena, P., Reichert, S. L., Loh, A., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2015.08.001 · Cited by 89 · cited 1× · see citing works
“Patients also exhibit a combination of muscular hypotonia with brisk muscle reflexes [170].”
Background
A report on 10 new patients with heterozygous mutations in the COL11A1 gene and a review of genotype–phenotype correlations in type XI collagenopathies
Majava, M., Hoornaert, K. P., Bartholdi, D., Bouma, M., Bouman, K., Carrera, M., Devriendt, K., Hurst, J., Kitsos, G., Niedrist, D., et al. (2007) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.31586 · Cited by 88 · cited 1×
“Moreover, COL11A1 mutations are associated by early-onset hearing loss [110].”
Background
Collagen type VI and related disorders: Bethlem myopathy and Ullrich scleroatonic muscular dystrophy.
Bertini, E., & Pepe, G. (2002) · European journal of paediatric neurology · doi:10.1053/ejpn.2002.0593 · Cited by 88 · cited 1× · see citing works
“The mild form may also reveal skin abnormalities, including follicular hyperkeratosis on the arms and legs; soft, velvety skin on the hand palms and feet soles; abnormal wound healing resulting in shallow scars [131].”
Background
The natural history, including orofacial features of three patients with Ehlers–Danlos syndrome, dermatosparaxis type (EDS type VIIC)
Malfait, F., Coster, P. D., Haußer, I., van Essen, A. J., Franck, P., Colige, A., Nusgens, B., MARTENS, L. C., & Paepe, A. D. (2004) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.30299 · Cited by 85 · cited 1× · see citing works
“Extra (redundant) folds of skin may be present as affected children get older [81].”
Background
Congenital Myasthenic Syndrome Type 19 Is Caused by Mutations in COL13A1, Encoding the Atypical Non-fibrillar Collagen Type XIII α1 Chain
Logan, C. V., Cossins, J., Cruz, P. M. R., Parry, D. A., Maxwell, S., Martínez‐Martínez, P., Riepsaame, J., Abdelhamed, Z. A., Lake, A. V. R., Moran, M., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2015.10.017 · Cited by 82 · cited 1× · see citing works
“The severity of the weakness and disease course is variable [149].”
Background
Régulation de l’activité cellulaire par la matrice extracelulaire : le concept de matrikines
Maquart, F., Siméon, A., Pasco, S., & Monboisse, J. (1999) · Journal de la Société de Biologie · doi:10.1051/jbio/1999193040423 · Cited by 81 · see citing works
Fibronectin Growth Factor-Binding Domains Are Required for Fibroblast Survival
Lin, F., Ren, X.-D., Pan, Z., Macri, L. K., Zong, W., Tonnesen, M. G., Rafailovich, M. H., Bar‐Sagi, D., & Clark, R. A. F. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2010.253 · Cited by 77 · cited 1× · see citing works
“Hepatocyte growth factor (HGF) binds to the 70 kDa N-terminal and the 40 kDa C-terminal fragments of fibronectin [15], whereas platelet-derived growth factor (PDGF) binds the type III and the variable domains of fibronectin [16].”
Background
Infantile Cortical Hyperostosis (Caffey Disease): A Review
Kamoun-Goldrat, A. S., & Merrer, M. F. L. (2008) · Journal of Oral and Maxillofacial Surgery · doi:10.1016/j.joms.2007.09.007 · Cited by 73 · cited 1× · see citing works
“Rare cases of recurrence have also been described [90].”
Background
Ullrich congenital muscular dystrophy: clinicopathological features, natural history and pathomechanism(s)
Yonekawa, T., & Nishino, I. (2014) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2013-307052 · Cited by 71 · cited 1× · see citing works
“As in BTHLM1, some people with UCMD1 have follicular hyperkeratosis [132].”
Background
Osteogenesis Imperfecta: A Translational Approach to Brittle Bone Disease
Shapiro, J., Byers, P., Glorieux, F., & Sponsellor, P. (2013) · doi:10.1016/c2011-0-07790-6 · Cited by 68 · cited 1×
“Types X OI is a severe deforming form of the disorder characterized by aberrant collagen crosslinking, folding and chaperoning [87].”
Background
Novel form of X-linked nonsyndromic hearing loss with cochlear malformation caused by a mutation in the type IV collagen gene COL4A6
Rost, S., Bach, E., Neuner, C., Nanda, I., Dysek, S., Bittner, R., Keller, A., Bartsch, O., Mlynski, R., Haaf, T., et al. (2013) · European Journal of Human Genetics · doi:10.1038/ejhg.2013.108 · Cited by 66 · cited 1×
“Female patients develop mild to moderate hearing impairment in the third/fourth decades of life and rarely hearing loss in the first decade of life [129].”
Background
The phenotype of the musculocontractural type of Ehlers‐Danlos syndrome due to <i>CHST14</i> mutations
Janecke, A. R., Li, B., Boehm, M., Krabichler, B., Rohrbach, M., Müller, T., Fuchs, I., Golas, G., Katagiri, Y., Ziegler, S. G., et al. (2016) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.37383 · Cited by 66 · cited 1× · see citing works
“EDSMC neonates show distal arthrogryposis and muscular hypotonia [78,79].”
Background
The presence of a fibrotic focus is an independent predictor of early metastasis in lymph node-negative breast cancer patients.
Colpaert, C., Vermeulen, P., Marck, E. V., & Dirix, L. (2001) · American Journal of Surgical Pathology · doi:10.1097/00000478-200112000-00016 · Cited by 61 · cited 1× · see citing works
“Tissue stiffness can drive malignant transformation via integrin-mediated mechanisms [23] and such fibrotic “stiff” lesions are associated with a poor prognosis [24].”
Background
Type IX collagen gene mutations can result in multiple epiphyseal dysplasia that is associated with osteochondritis dissecans and a mild myopathy
Jackson, G. C., Marcus‐Soekarman, D., Stolte‐Dijkstra, I., Verrips, A., Taylor, J. A., & Briggs, M. D. (2010) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.33240 · Cited by 59 · cited 1× · see citing works
“EDM2 onset is usually in childhood, around 3-4 years of age and clinical variability is observed even within the same family [141].”
Background
Missense and nonsense mutations in the alternatively-spliced exon 2 ofCOL2A1cause the ocular variant of Stickler syndrome
McAlinden, A., Majava, M., Bishop, P. N., Perveen, R., Black, G. C. M., Pierpont, M. E., Ala‐Kokko, L., & Männikkö, M. (2007) · Human Mutation · doi:10.1002/humu.20603 · Cited by 56 · cited 1× · see citing works
“Systemic features of premature osteoarthritis, cleft palate, hearing impairment and craniofacial abnormalities are very mild or absent [113].”
Background
Dominant negative mutations in the C‐propeptide of COL2A1 cause platyspondylic lethal skeletal dysplasia, torrance type, and define a novel subfamily within the type 2 collagenopathies
Zankl, A., Neumann, L., Ignatius, J., Nikkels, P., Schrander-Stumpel, C., Mortier, G., Omran, H., Wright, M., Hilbert, K., Bonafė, L., et al. (2005) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.30531 · Cited by 55 · cited 1×
“The resting cartilage appeared hypercellular with large chondrocytes [102,103].”
Background
Unraveling metalloproteinase function in skeletal biology and disease using genetically altered mice
Aiken, A., & Khokha, R. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.07.002 · Cited by 53 · see citing works
Schmid type of metaphyseal chondrodysplasia and COL10A1 mutations—findings in 10 patients
Mäkitie, O., Susic, M., Ward, L., Barclay, C., Glorieux, F., & Cole, W. (2005) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.30855 · Cited by 53 · cited 1×
“These defects give rise to unusual “waddling” walk (gait) [144].”
Background
Novel recessive BFSP2 and PITX3 mutations: Insights into mutational mechanisms from consanguineous populations
Aldahmesh, M., Khan, A. O., Mohamed, J. Y., & Alkuraya, F. (2011) · Genetics in Medicine · doi:10.1097/gim.0b013e31822623d5 · Cited by 52 · cited 1×
“Skull defects range from occipital encephalocele to occult cutis aplasia [151].”
Background
De Barsy syndrome: a review of the phenotype
Kivuva, E., Parker, M., Cohen, M. C., Wagner, B., & Sobey, G. (2008) · Clinical Dysmorphology · doi:10.1097/mcd.0b013e3282f4a964 · Cited by 52 · cited 1×
“ARCL3A is characterized by cutis laxa (a progeria-like appearance) and ophthalmologic abnormalities [169].”
Background
Molecular Packing in Network-Forming Collagens
Knupp, C., & Squire, J. (2003) · TheScientificWorldJournal · doi:10.1100/tsw.2003.40 · Cited by 52 · cited 2×
“For this reason collagen type VI can also be included among the network-forming collagens [60].”
Background
Alport syndrome with diffuse leiomyomatosis
Anker, M., Arnemann, J., Neumann, K., Ahrens, P., Schmidt, H., & König, R. (2003) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.20019 · Cited by 51 · cited 1× · see citing works
“DL-ATS reveals the Alport syndrome features associated with diffuse leiomyomatosis [119].”
Background
A novel locus for autosomal dominant nonsyndromic hearing loss, DFNA13, maps to chromosome 6p.
Brown, M. R., Tomek, M., Laer, L. V., Smith, S. D., Kenyon, J., Camp, G. V., & Smith, R. J. H. (1997) · American Journal of Human Genetics · doi:10.1086/514892 · Cited by 51 · cited 1× · see citing works
“The affected individuals experienced progressive hearing loss beginning in the second to fourth decades [147].”
Background
Autosomal recessive Stickler syndrome in two families is caused by mutations in the COL9A1 gene.
Nikopoulos, K., Schrauwen, I., Simon, M. E. H., Collin, R. W., Veckeneer, M., Keymolen, K., Camp, G. V., Cremers, F., & van den Born, L. I. (2011) · Investigative Ophthalmology and Visual Science · doi:10.1167/iovs.10-7128 · Cited by 50 · cited 1× · see citing works
“Individuals affected by STL4 have moderate-to-severe sensorineural hearing loss, moderate-to-high myopia with vitreoretinopathy, cataracts and epiphyseal dysplasia [112].”
Background
Recessive mutations in COL25A1 are a cause of congenital cranial dysinnervation disorder.
Shinwari, J. M. A., Khan, A. O., Awad, S., Shinwari, Z., Alaiya, A., Al-anazi, M., Tahir, A. I., Poizat, C., & Tassan, N. A. (2015) · American Journal of Human Genetics · doi:10.1016/j.ajhg.2014.11.006 · Cited by 49 · cited 1×
“The third sib had no ptosis but showed bilateral Duane retraction syndrome, exotropic in the right eye and esotropic in the left [152].”
Background
Comparison of the impact of open and endovascular abdominal aortic aneurysm repair on renal function.
Saratzis, A., Sarafidis, P., Melas, N., & Khaira, H. (2014) · Journal of Vascular Surgery · doi:10.1016/j.jvs.2014.03.282 · Cited by 48 · cited 1×
“The main symptoms of this condition are dysphasia, frontotemporal cerebral atrophy and frontotemporal dementia, speech disorder, memory impairment [155].”
Background
The shed ectodomain of type XIII collagen affects cell behaviour in a matrix-dependent manner
Väisänen, M., Väisänen, T., & Pihlajaniemi, T. A. (2004) · Biochemical Journal · doi:10.1042/bj20031974 · Cited by 47 · cited 1× · see citing works
“The ectodomains of membrane collagens XIII, XVII, XXIII and XXV [33] are matricryptins involved in cell adhesion, migration or proliferation [34].”
Background
Spondylometepiphyseal dysplasia, Strudwick type.
Anderson, C., Sillence, D., Lachman, R., Toomey, K., Bull, M., Dorst, J., Rimoin, D., & Opitz, J. M. (1982) · American journal of medical genetics · doi:10.1002/ajmg.1320130304 · Cited by 46 · cited 1×
“Distinctive radiographic feature is irregular sclerotic changes, described as “dappled” in the metaphyses of the long bones that are caused by alternating zones of osteopenia and osteosclerosis [106].”
Background
Czech dysplasia metatarsal type: another type II collagen disorder
Hoornaert, K., Mařík, I. A., Kozlowski, K. S., Cole, T. R. P., Merrer, M. F. L., Leroy, J. G., Coucke, P. J., Sillence, D. O., & Mortier, G. R. (2007) · European Journal of Human Genetics · doi:10.1038/sj.ejhg.5201913 · Cited by 46 · cited 1× · see citing works
“Only five affected families from the Czech Republic have been so far reported [98].”
Background
A COL17A1 Splice-Altering Mutation Is Prevalent in Inherited Recurrent Corneal Erosions.
Oliver, V. F., van Bysterveldt, K. V., Cadzow, M., Steger, B., Romano, V., Markie, D., Hewitt, A., Mackey, D., Willoughby, C., Sherwin, T., et al. (2016) · Ophthalmology (Rochester, Minn.) · doi:10.1016/j.ophtha.2015.12.008 · Cited by 45 · cited 4×
“Epithelial recurrent erosion dystrophy (ERED) COL17 ERED (#122400) is caused by heterozygous mutation in COL17A1 gene (*113811) on chromosome 10q24.”
BackgroundInfluential
Target-Derived Matricryptins Organize Cerebellar Synapse Formation Through α3β1 Integrins
Su, J., Stenbjorn, R. S., Gorse, K., Su, K., Hauser, K., Ricard-Blum, S., Pihlajaniemi, T., & Fox, M. A. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.07.001 · Cited by 45 · cited 1× · see citing works
“Matrikines from collagens IV are involved in angiogenesis [35] and synapse formation [36].”
Background
Extracellular Matrix Degradation
Murphy, G., & Reynolds, J. J. (2003) · Definitions · doi:10.1002/0471221929.ch7 · Cited by 43 · cited 1×
“Cathepsin S was shown to target and degrade collagens [68].”
Background
Autosomal dominant avascular necrosis of femoral head in two Taiwanese pedigrees and linkage to chromosome 12q13.
Chen, W.-M., Liu, Y.-F., Lin, M.-W., Chen, I.-C., Lin, P.-Y., Lin, G.-L., Jou, Y., Lin, Y., Fann, C., Wu, J.-Y., et al. (2004) · American Journal of Human Genetics · doi:10.1086/422702 · Cited by 41 · cited 1×
“LCPD affects more often boys who are usually shorter than their peers [99].”
Background
Non-Lethal Type VIII Osteogenesis Imperfecta Has Elevated Bone Matrix Mineralization
Fratzl‐Zelman, N., Barnes, A. M., Weis, M., Carter, E. M., Hefferan, T. E., Perino, G., Chang, W., Smith, P. A., Roschger, P., Klaus Klaushofer, A., et al. (2016) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-1334 · Cited by 41 · cited 1× · see citing works
“The type VIII form of OI (mutations in P3H1) includes severe growth defects, skeletal demineralization, scoliosis, round face and proptosis [85].”
Background
Next generation sequencing uncovers a missense mutation in COL4A1 as the cause of familial retinal arteriolar tortuosity
Zenteno, J. C., Crespí, J., Buentello‐Volante, B., Buil, J. A., Bassaganyas, F., Vela, J. I., Díaz‐Cascajosa, J., & Marieges, M. T. (2014) · Graefe s Archive for Clinical and Experimental Ophthalmology · doi:10.1007/s00417-014-2800-6 · Cited by 40 · cited 1× · see citing works
“Involvement of non-ocular vascular beds has not been demonstrated in most cases but occasionally other associated vascular abnormalities have been recorded, including malformations in the Kieselbach nasal septum, spinal cord vascular mass, telangiectasis of bulbar conjunctiva and internal carotid artery aneurysm [123].”
Background
Mitochondrial oxidative phosphorylation in autosomal dominant optic atrophy
Mayorov, V., Lowrey, A. J., Biousse, V., Newman, N. J., Cline, S. D., & Brown, M. D. (2008) · BMC Biochemistry · doi:10.1186/1471-2091-9-22 · Cited by 39 · cited 1× · see citing works
“They affect the ability of heparin sulphate to bind several growth factors such as VEGF, PDGF and FGF, thus altering the downstream signalling events [50].”
Background
A constitutional disorder of connective tissue suggesting a defect in collagen biosynthesis
Meigel, W., M�ller, P. K., Pontz, B. F., S�rensen, N., & Spranger, J. W. (1974) · Journal of Molecular Medicine · doi:10.1007/bf01468935 · Cited by 37 · cited 1× · see citing works
“Alpha-2-Deficient Collagen Disease COL1 In 1974 Meigel and co-authors [91] described a 10-year-old son of consanguineous parents, with an apparently ‘new’ connective tissue disorder.”
Background
Expanding the clinical and mutational spectrum of B4GALT7-spondylodysplastic Ehlers-Danlos syndrome
Ritelli, M., Dordoni, C., Cinquina, V., Venturini, M., Calzavara‐Pinton, P., & Colombi, M. (2017) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-017-0704-3 · Cited by 36 · see citing works
Common interruptions in the repeating tripeptide sequence of non-fibrillar collagens: sequence analysis and structural studies on triple-helix peptide models.
Thiagarajan, G., Li, Y., Mohs, A., Strafaci, C., Popiel, M., Baum, J., & Brodsky, B. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.11.075 · Cited by 35 · cited 1×
“Non-collagenous (NC) regions may also have structural function as shown by the transmembrane collagens [58].”
Background
A novel mutation in PYCR1 causes an autosomal recessive cutis laxa with premature aging features in a family
Lin, D., Yeung, C.-Y., Liu, H.-L., Ho, C.-S., Shu, C.-H., Chuang, C.-K., Huang, Y.-W., Wu, T.-Y., Huang, Z.-G., Jian, Y.-R., et al. (2011) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.33963 · Cited by 33 · cited 1×
“ARCL3B is a rare autosomal recessive disorder characterized by a progeria-like appearance with distinctive facial features, sparse hair, ophthalmologic abnormalities and intrauterine growth retardation [168].”
Background
TFIIH-dependent MMP-1 overexpression in trichothiodystrophy leads to extracellular matrix alterations in patient skin
Arseni, L., Lanzafame, M., Compe, E., Fortugno, P., Afonso-Barroso, A., Peverali, F. A., Lehmann, A. R., Zambruno, G., Egly, J., Stefanini, M., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1416181112 · Cited by 30 · cited 1× · see citing works
“This event leads to hyper-secretion of active MMP1 enzyme and degradation of collagen type I in the dermis of TTD patient skin [157].”
BackgroundSelf-citation
Collagen remodeling by phagocytosis is determined by collagen substrate topology and calcium-dependent interactions of gelsolin with nonmuscle myosin IIA in cell adhesions
Arora, P. D., Wang, Y., Bresnick, A., Dawson, J. F., Janmey, P., & McCulloch, C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0754 · Cited by 30 · cited 1× · see citing works
“The extracellular collagen fragments are then recruited through phagocytosis from the neighbouring cells, mainly fibroblasts and macrophages, which send them to degradation via the lysosomal pathway [70].”
Background
XPD mutations in trichothiodystrophy hamper collagen VI expression and reveal a role of TFIIH in transcription derepression
Orioli, D., Compe, E., Nardò, T., Mura, M., Giraudon, C., Botta, E., Arrigoni, L., Peverali, F. A., Egly, J., & Stefanini, M. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds508 · Cited by 26 · cited 1× · see citing works
“A reduced expression of COL6A1 (*120220), an abundant collagen of skin and connective tissue, has been shown in the skin of TTD patients with mutations in the ERCC2/XPD gene [156].”
BackgroundSelf-citation
Bruck syndrome - a rare syndrome of bone fragility and joint contracture and novel homozygous FKBP10 mutation.
Moravej, H., Karamifar, H., Karamizadeh, Z., Amirhakimi, G., Atashi, S., & Nasirabadi, S. (2015) · Endokrynologia Polska · doi:10.5603/ep.2015.0024 · Cited by 24 · see citing works
Radiological and histological variants of thanatophoric dysplasia are associated with common mutations in FGFR-3
Nerlich, A. G., Freisinger, P., & Bonaventure, J. (1996) · American Journal of Medical Genetics · doi:10.1002/(sici)1096-8628(19960503)63:1 · Cited by 23 · see citing works
Czech Dysplasia Metatarsal Type
Marik, I., Marikova, O., Zemková, D., Kuklik, M., & Kozlowski, K. (2004) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.30132 · Cited by 23 · cited 1×
“Czech dysplasia is a skeletal dysplasia characterized by early and progressive onset, shortening of the third and fourth toes caused by metatarsal hypoplasia [97].”
Background
Mutations in COL8A2, the Gene Encoding the α2 Chain of Type VIII Collagen, Cause Two Forms of Corneal Endothelial Dystrophy
Black, G., Biswas, S., Munier, F., Stone, E., Bonshek, R., & McLeod, D. (2002) · doi:10.1042/cs103069pb · Cited by 23 · cited 1×
“The authors suggested that the underlying pathogenesis of FECD and PPCD2 may be related to disturbance of the role of COL8 in influencing the terminal differentiation of the neural crest-derived corneal endothelial cell [140].”
Background
Dominant and Recessive Forms of Fibrochondrogenesis Resulting from Mutations at a Second Locus, COL11A2
Tompson, S. W., Faqeih, E., Ala-kokko, L., Hecht, J. T., Miki, R., Funari, T. L., Funari, V., Nevarez, L., Krakow, D., & Cohn, D. H. (2012) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.34406 · Cited by 22 · cited 1×
“Affected individuals who survive the neonatal period have high myopia, mild to moderate hearing loss and severe skeletal dysplasia [146].”
Background
Recurrence of achondrogenesis type 2 in sibs: Additional evidence for germline mosaicism
Comstock, J., Putnam, A., Sangle, N., Lowichik, A., Rose, N., & Opitz, J. M. (2010) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.33463 · Cited by 21 · cited 1×
“The inheritance is autosomal dominant but somatic and germline mosaicism have also been reported [96].”
Background
Steel Syndrome: Dislocated Hips and Radial Heads, Carpal Coalition, Scoliosis, Short Stature, and Characteristic Facial Features
Flynn, J., Ramírez, N., Betz, R., Mulcahey, M., Pino, F., Herrera-soto, J. A., Carlo, S., & Cornier, A. (2010) · Journal of pediatric orthopedics · doi:10.1097/bpo.0b013e3181d3e464 · Cited by 21 · cited 1× · see citing works
“The dislocated hips are resistant to surgical intervention [153].”
Background
Brittle Cornea Syndrome: Case Report with Novel Mutation in thePRDM5Gene and Review of the Literature
Avgitidou, G., Siebelmann, S., Bachmann, B. O., Kohlhase, J., Heindl, L. M., & Cursiefen, C. (2015) · Case Reports in Ophthalmological Medicine · doi:10.1155/2015/637084 · Cited by 20 · cited 1× · see citing works
“Systemic abnormalities included increased skin laxity, pectus excavatum, scoliosis, congenital hip dislocation, recurrent shoulder dislocation, high-frequency hearing loss, high-arched palate and mitral valve prolapse [166].”
Background
Pregnancy in women with Alport syndrome
Crovetto, F., Moroni, G., Zaina, B., Acaia, B., Ossola, M., & Fedele, L. (2013) · International Urology and Nephrology · doi:10.1007/s11255-012-0154-8 · Cited by 20
Dominant inheritance of multiple epiphyseal dysplasia, myopia and deafness
Beighton, P., Goldberg, L., & Hof, J. (1978) · Clinical Genetics · doi:10.1111/j.1399-0004.1978.tb02125.x · Cited by 20 · cited 2×
“Several cases have been reported, included family members over various generations [95,100,101].”
Background
Survival to adulthood and dominant inheritance of platyspondylic skeletal dysplasia, Torrance-Luton type
Neumann, L., Kunze, J., Uhl, M., Stöver, B., Zabel, B., & Spranger, J. (2003) · Pediatric Radiology · doi:10.1007/s00247-003-1055-x · Cited by 18 · cited 1×
“Though generally lethal in the perinatal period, a few long-term survivors with PLSD-T have been reported [104].”
Background
Modulating Collagen Triple-Helix Stability with 4-Chloro, 4-Fluoro, and 4-Methylprolines
Shoulders, M., & Raines, R. T. (2009) · Advances in Experimental Medicine and Biology · doi:10.1007/978-0-387-73657-0_115 · Cited by 16 · cited 2×
“Finally, fibrils assemble into fibres of larger diameter [52].”
Background
Familial translocation t(Y;15)(q12;p11) and de novo deletion of the Prader-Willi syndrome (PWS) critical region on 15q11-q13
D, S. E. M., Morris, M. A., Dahoun, S. P., DeLozier-Blanchet, C. D., Gos, A., Sizonenko, P. C., & Antonarakis, S. E. (1997) · American Journal of Medical Genetics · doi:10.1002/(sici)1096-8628(19970613)70:3 · Cited by 15 · see citing works
A case of Marshall's syndrome and review of the literature
Çalışkan, E., Açıkgöz, G., Yeniay, Y., Özmen, I., Gamsızkan, M., & Akar, A. (2015) · International Journal of Dermatology · doi:10.1111/ijd.12471 · Cited by 7
Spondyloepiphyseal dysplasia with accumulation of glycoprotein in the chondrocytes: spondyloepiphyseal dysplasia, Stanescu type
Nishimura, G., Saitoh, Y., Okuzumi, S., Imaizumi, K., Hayasaka, K., & Hashimoto, M. (1998) · Skeletal Radiology · doi:10.1007/s002560050363 · Cited by 7 · cited 1×
“Other clinical characteristics are generalized platyspondyly, hypoplastic pelvis, epiphyseal flattening with metaphyseal splaying of the long bones and enlarged phalangeal epimetaphyses of the hands [93,94].”
Background
Ectodermal dysplasia with tetramelic deficiencies and no mutation in p63: Odontotrichomelic syndrome or a new entity?
Zankl, A., Scheffer, H., & Schinzel, A. (2004) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.20646 · Cited by 6 · cited 1× · see citing works
“Some patients also present shortening of long bones, degenerative changes in the proximal femora, limited elbow extension, midface hypoplasia, myopia, deafness and mental retardation [105].”
Background
Namaqualand hip dysplasia. Orthopedic implications.
Learmonth, I., Christy, G., & Beighton, P. (1987) · Clinical Orthopaedics and Related Research · doi:10.1097/00003086-198705000-00020 · Cited by 5
Pathogenenic variant in the COL2A1 gene is associated with Spondyloepiphyseal dysplasia type Stanescu
Hammarsjö, A., Nordgren, A., Lagerstedt-Robinson, K., Malmgren, H., Nilsson, D., Wedrén, S., Nordenskjöld, M., Nishimura, G., & Grigelioniene, G. (2016) · American Journal of Medical Genetics. Part A · doi:10.1002/ajmg.a.37387 · Cited by 3 · cited 1×
“Other clinical characteristics are generalized platyspondyly, hypoplastic pelvis, epiphyseal flattening with metaphyseal splaying of the long bones and enlarged phalangeal epimetaphyses of the hands [93,94].”
Background

Flagged first, then by citations

13 of the 172 references couldn’t be matched to a known paper.

Research works printed but not linked: 13

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Regulation of Collagen I and Collagen III in Tissue Injury and Regeneration
Singh, D., Rai, V., & Agrawal, D. K. (2023) · Cardiology and Cardiovascular Medicine · doi:10.26502/fccm.92920302 · Cited by 469 · see citing works
“Alterations in the morphology and function of heart ventricles can occur from disruptions in collagen metabolism, which in turn cause anomalies in the remodeling of the collagen network [76].”
Background
The extracellular matrix in development
Walma, D. A. C., & Yamada, K. M. (2020) · Development · doi:10.1242/dev.175596 · Cited by 398 · see citing works
“Human genetic disorders can result from perturbed ECM structure, dynamics, components and/or interactions (Arseni et al., 2018; Bateman et al., 2009; Lamande and Bateman, 2019; Pozzi et al., 2017).”
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Collagen: quantification, biomechanics and role of minor subtypes in cartilage
Bielajew, B. J., Hu, J. C. Y., & Athanasiou, K. A. (2020) · Nature Reviews Materials · doi:10.1038/s41578-020-0213-1 · Cited by 318 · see citing works
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“epidermis, which is the connective tissue composed of fibroblasts, responsible for the synthesis and secretion of collagen and other matrix proteins (such as fibronectin, elastin, and glycans) to the extracellular environment, giving the skin elasticity, strength, and ability to resist external interference [6,7].”
Background
From mechanical resilience to active material properties in biopolymer networks
Burla, F., Mulla, Y., Vos, B. E., Aufderhorst-Roberts, A., & Koenderink, G. H. (2019) · Nature Reviews Physics · doi:10.1038/s42254-019-0036-4 · Cited by 224 · see citing works
The Role of Extracellular Matrix in Skin Wound Healing
Potekaev, N., Borzykh, O., Medvedev, G. V., Pushkin, D., Petrova, M., Petrov, A. V., Dmitrenko, D., Karpova, E. I., Demina, O., & Shnayder, N. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10245947 · Cited by 189 · see citing works
“The large, branched hyaluronic acid molecule traps TGF-β1 molecules near the fibroblast.”
BackgroundInfluential
A Collagen Supplement Improves Skin Hydration, Elasticity, Roughness, and Density: Results of a Randomized, Placebo-Controlled, Blind Study
Bolke, L., Schlippe, G., Gerß, J., & Voss, W. (2019) · Nutrients · doi:10.3390/nu11102494 · Cited by 200 · see citing works
Main and Minor Types of Collagens in the Articular Cartilage: The Role of Collagens in Repair Tissue Evaluation in Chondral Defects
Alcaide-Ruggiero, L., Molina-Hernández, V., Granados, M., & Domínguez, J. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413329 · Cited by 152 · see citing works
“In the Golgi, three of these α chains are assembled one around the other, along a central axis, to generate a procollagen molecule in the form of right-handed triple-helix (Figure 2-3) [32,33].”
BackgroundInfluential
Epigenetic Regulation of Skin Cells in Natural Aging and Premature Aging Diseases
Orioli, D., & Dellambra, E. (2018) · Cells · doi:10.3390/cells7120268 · Cited by 144 · see citing works
“Matrix components maintain the skin architecture and confer elasticity as well as resistance and strength to tissue [1,6].”
BackgroundSelf-citation
Collagen Biosynthesis, Processing, and Maturation in Lung Ageing
Onursal, C., Dick, E., Angelidis, I., Schiller, H. B., & Staab-Weijnitz, C. A. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.593874 · Cited by 122 · see citing works
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“The extracellular matrix (ECM) is a complex, non-cellular network produced primarily by fibroblasts, including proteoglycans, hyaluronic acid, adhesion glycoproteins (fibronectin and laminin), and fibrin (collagen and elastin), as well as growth factors and cytokines [84].”
Background
Cellular and Molecular Mechanisms in the Pathogenesis of Classical, Vascular, and Hypermobile Ehlers‒Danlos Syndromes
Chiarelli, N., Ritelli, M., Zoppi, N., & Colombi, M. (2019) · Genes · doi:10.3390/genes10080609 · Cited by 82 · see citing works
“Collagens are also involved in cell adhesion, chemotaxis, and migration [1,2].”
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Avian Coloration Genetics: Recent Advances and Emerging Questions
Price-Waldman, R., & Stoddard, M. C. (2021) · Journal of Heredity · doi:10.1093/jhered/esab015 · Cited by 118 · see citing works
“However, the molecular and genetic basis of collagen has been extensively studied in other systems (Kadler et al. 2008; Arseni et al. 2018; Holmes et al. 2018; Haq et al. 2019); insights into the regulation of collagen fiber diameter and spacing suggest promising avenues for research into the genetics of structurally…”
Background
Novel scaffold platforms for simultaneous induction osteogenesis and angiogenesis in bone tissue engineering: a cutting-edge approach
Saberi, A., Kouhjani, M., Mohammadi, M., & Hosta‐Rigau, L. (2023) · Journal of Nanobiotechnology · doi:10.1186/s12951-023-02115-7 · Cited by 82 · see citing works
“Collagen, for instance, has been identified in at least 28 different types [171].”
Background
A natural strategy for astaxanthin stabilization and color regulation: Interaction with proteins.
Yao, Q., Ma, J., Chen, X., Zhao, G., & Zang, J. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.134343 · Cited by 71 · see citing works
Polydeoxyribonucleotide: A promising skin anti-aging agent
Khan, A., Wang, G., Zhou, F., Gong, L., Zhang, J., Qi, L., & Cui, H. (2022) · Chinese Journal of Plastic and Reconstructive Surgery · doi:10.1016/j.cjprs.2022.09.015 · Cited by 60 · see citing works
Overview of the molecular determinants contributing to the expression of Psoriasis and Psoriatic Arthritis phenotypes
Caputo, V., Strafella, C., Termine, A., Dattola, A., Mazzilli, S., Lanna, C., Cosio, T., Campione, E., Novelli, G., Giardina, E., et al. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15742 · Cited by 61 · see citing works
An Update on the Clinical Efficacy and Safety of Collagen Injectables for Aesthetic and Regenerative Medicine Applications
Salvatore, L., Natali, M. L., Brunetti, C., Sannino, A., & Gallo, N. (2023) · Polymers · doi:10.3390/polym15041020 · Cited by 61 · see citing works
Biodegradable Materials for Tissue Engineering: Development, Classification and Current Applications
Modrák, M., Trebuňová, M., Balogová, A. F., Hudák, R., & Živčák, J. (2023) · Journal of Functional Biomaterials · doi:10.3390/jfb14030159 · Cited by 71 · see citing works
“At least 28 different types of collagens are currently recognized [60].”
Background
Characterization of recombinant humanized collagen type III and its influence on cell behavior and phenotype
Wang, J., Hu, H., Wang, J., Qiu, H., Gao, Y., Xu, Y., Liu, Z., Tang, Y., Song, L., Ramshaw, J. A. M., et al. (2022) · Journal of Leather Science and Engineering · doi:10.1186/s42825-022-00103-5 · Cited by 47 · see citing works
Senolytic therapeutics: An emerging treatment modality for osteoarthritis
Ansari, M. M., Ghosh, M., Lee, D., & Son, Y. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102275 · Cited by 48 · see citing works
Glycosylation Modulates the Structure and Functions of Collagen: A Review
Tvaroška, I. (2024) · Molecules · doi:10.3390/molecules29071417 · Cited by 55 · see citing works
“See, for example, references [14,15,31,194,212–216].”
Background
Cardiac ECM: Its Epigenetic Regulation and Role in Heart Development and Repair
Song, R., & Zhang, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228610 · Cited by 47 · see citing works
SOD3 Suppresses the Expression of MMP-1 and Increases the Integrity of Extracellular Matrix in Fibroblasts
Kim, J. H., Jeong, H. D., Song, M. J., Lee, D. H., Chung, J. H., & Lee, S. (2022) · Antioxidants · doi:10.3390/antiox11050928 · Cited by 36 · see citing works
“The dermal ECM comprises fibrillar collagen, including the most abundant type I collagen, elastin, and proteoglycan [7,8].”
Background
Doxycycline Hyclate Modulates Antioxidant Defenses, Matrix Metalloproteinases, and COX-2 Activity Accelerating Skin Wound Healing by Secondary Intention in Rats
Altoé, L. S., Alves, R. S., Miranda, L. L., Sarandy, M. M., Bastos, D. S., Gonçalves-Santos, E., Novaes, R., & Gonçalves, R. V. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/4681041 · Cited by 33
Extraction and Purification of Biopolymers from Marine Origin Sources Envisaging Their Use for Biotechnological Applications
Carvalho, D. N., Gonçalves, C., Sousa, R. O., Reis, R. L., Oliveira, J. M., & Silva, T. H. (2024) · Marine Biotechnology · doi:10.1007/s10126-024-10361-5 · Cited by 42 · see citing works
Wound Healing Activities and Potential of Selected African Medicinal Plants and Their Synthesized Biogenic Nanoparticles
Tyavambiza, C., Dube, P., Goboza, M., Meyer, S., Madiehe, A. M., & Meyer, M. (2021) · Plants · doi:10.3390/plants10122635 · Cited by 44 · see citing works
“The level of vascularity decreases as the scar matures [30,31].”
Background
Collagens and elastin genetic variations and their potential role in aging-related diseases and longevity in humans
Romero‐Ortuño, R., Kenny, R. A., & McManus, R. (2019) · Experimental Gerontology · doi:10.1016/j.exger.2019.110781 · Cited by 29 · see citing works
Advances of three-dimensional (3D) culture systems for in vitro spermatogenesis
Salem, M., Khadivi, F., Javanbakht, P., Mojaverrostami, S., Abbasi, M., Feizollahi, N., Abbasi, Y., Heidarian, E., & Yazdi, F. R. (2023) · Stem Cell Research & Therapy · doi:10.1186/s13287-023-03466-6 · Cited by 39 · see citing works
“It plays a critical role in maintenance of organ structure, tissue integrity and normal functioning [110, 111].”
Background
Identification of the collagen family as prognostic biomarkers and immune-associated targets in gastric cancer
Chen, Y., Chen, W., Dai, X., Zhang, C., Zhang, Q., & Lu, J. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.106798 · Cited by 29 · see citing works
Morphological signs of connective tissue dysplasia as predictors of frequent post-exercise musculoskeletal disorders
Nikolenko, V. N., Oganesyan, M. V., Vovkogon, A. D., Cao, Y., Churganova, A. A., Золотарева, М. А., Ачкасов, Е. Е., Sankova, M. V., Rizaeva, N. A., & Sinelnikov, M. Y. (2020) · BMC Musculoskeletal Disorders · doi:10.1186/s12891-020-03698-0 · Cited by 26 · see citing works
Modulation of Stiffness-Dependent Macrophage Inflammatory Responses by Collagen Deposition
Meli, V. S., Rowley, A. T., Veerasubramanian, P. K., Heedy, S., Liu, W. F., & Wang, S. (2024) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.3c01892 · Cited by 23 · see citing works
Genetic and Epigenetic Aspects of Skin Collagen Fiber Turnover and Functioning
Потекаев, Н. Н., Borzykh, O. B., Medvedev, G. V., Петрова, М. М., Gavrilyuk, O. A., Karpova, E. I., Trefilova, V. V., Demina, O. M., Popova, T. E., & Shnayder, N. A. (2021) · Cosmetics · doi:10.3390/cosmetics8040092 · Cited by 26 · see citing works
Employing Extracellular Matrix-Based Tissue Engineering Strategies for Age-Dependent Tissue Degenerations
Jo, Y., Hwang, S. H., & Jang, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179367 · Cited by 23 · see citing works
“As the strict regulation of ECM synthesis and remodeling is directly associated with healthy tissue conditions, alterations in ECM remodeling can affect the course and progression of several other pathological conditions, including fibrosis, disorders, and cancers [2].”
Background
Extracellular Matrix in Development and Disease
Oxford, J., Reeck, J., & Hardy, M. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20010205 · Cited by 24 · see citing works
“The link between ECM molecules and phenotypic characteristics of specific hereditary diseases is reviewed by Arseni and colleagues [3], with an emphasis on the most prevalent of all ECM proteins, collagens, and mutations that result in bone fragility, muscle weakness, and skin defects.”
Background
Effect of electroacupuncture on the degradation of collagen in pelvic floor supporting tissue of stress urinary incontinence rats
Li, C.-N., Yang, M., Qu, Z., Ruan, S., Chen, B., Ran, J., Shu, W., Chen, Y.-L., & Hou, W.-G. (2022) · International Urogynecology Journal · doi:10.1007/s00192-022-05106-8 · Cited by 22
“Fiber-forming collagen is stabilized by nonreducible covalent cross-links between specific triplehelix domains and telopeptides, such as interstitial collagen (collagen I, collagen II, and collagen III), collagen V, and collagen XI [22].”
Background
Glycosaminoglycan Modification of Decorin Depends on MMP14 Activity and Regulates Collagen Assembly
Daquinag, A. C., Gao, Z., Fussell, C., Sun, K., & Kolonin, M. G. (2020) · Cells · doi:10.3390/cells9122646 · Cited by 28 · see citing works
Comparison of Biological Activities and Protective Effects on PAH-Induced Oxidative Damage of Different Coffee Cherry Pulp Extracts
Preedalikit, W., Chittasupho, C., Leelapornpisid, P., Potprommanee, S., & Kiattisin, K. (2023) · Foods · doi:10.3390/foods12234292 · Cited by 21 · see citing works
“The inhibitory effects of this speciﬁc enzyme can help to delay the process of collagen breakdown and the subsequent development of wrinkles [67].”
Background
Potential of Atlantic Codfish (Gadus morhua) Skin Collagen for Skincare Biomaterials
Rodrigues, C. V., Sousa, R. O., Carvalho, A. C., Alves, A. L. D. S., Marques, C. F., Cerqueira, M. T., Reis, R. L., & Silva, T. H. (2023) · Molecules · doi:10.3390/molecules28083394 · Cited by 23 · see citing works
“To date, 28 types of collagen were identified and characterized, presenting a triple helix structure [6,7].”
Background
The role of selected flavonoids from bajakah tampala (Spatholobus littoralis Hassk.) stem on cosmetic properties: A review
Sianipar, R. N. R., Suryanegara, L., Fatriasari, W., Tangkearung, E., Kusuma, I. W., Achmadi, S. S., Azelee, N. I. W., & Hamid, Z. A. A. (2023) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2023.01.006 · Cited by 21 · see citing works
“…(MACITs) or transmembrane networks; collagen types XV and XVIII form multiple triple-helix domains and interruptions (MULTIPLEXINs); and the two unclassi-ﬁed collagen types, the type XXVI and XXVIII (Andriotis et al., 2023; Arseni et al., 2018; Mak and Mei, 2017; Sun et al., 2019; Uitto, 2019).”
Rare functional genetic variants in COL7A1, COL6A5, COL1A2 and COL5A2 frequently occur in Chiari Malformation Type 1
Urbizu, A., Garrett, M., Soldano, K., Drechsel, O., Loth, D., Marcé-Grau, A., Soler, O., Poca, M., Ossowski, S., Macaya, A., et al. (2021) · PLoS ONE · doi:10.1371/journal.pone.0251289 · Cited by 21 · see citing works
“Since each collagen is generally expressed in several different tissues, and is tightly associated with other ECM components, alterations in the collagen genes can result in widely overlapping clinical features [38].”
Background
The roles of collagen in chronic kidney disease and vascular calcification
Huang, A., Guo, G., Yu, Y., & Yao, L. (2020) · Journal of Molecular Medicine · doi:10.1007/s00109-020-02014-6 · Cited by 28 · see citing works
“participates in endothelial cell migration and tumor growth [13].”
BackgroundInfluential
RNAseq-Based Prioritization Revealed COL6A5, COL8A1, COL10A1 and MIR146A as Common and Differential Susceptibility Biomarkers for Psoriasis and Psoriatic Arthritis: Confirmation from Genotyping Analysis of 1417 Italian Subjects
Caputo, V., Strafella, C., Termine, A., Campione, E., Bianchi, L., Novelli, G., Giardina, E., & Cascella, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082740 · Cited by 20 · see citing works
“The most abundant components of the ECM are collagens, the fibrous proteins that are involved in the formation and maintenance of structural components and provide mechanical strength and elasticity to connective tissues (such as cartilage, bone, epidermis, cornea and blood vessels) [10,11].”
Background
Apical cell expansion maintained by Dusky-like establishes a scaffold for corneal lens morphogenesis
Ghosh, N., & Treisman, J. (2024) · Science Advances · doi:10.1126/sciadv.ado4167 · Cited by 18
Bioactive extracellular matrix fragments in tendon repair
Mohindra, R., Mohindra, R., Agrawal, D. K., & Thankam, F. G. (2022) · Cell and Tissue Research · doi:10.1007/s00441-022-03684-z · Cited by 17 · see citing works
“Proteinases, such as MMPs, cathepsins, and plasmins, are the main mediators of collagen fragmentation (Arseni et al. 2018).”
Background
MiR-29b-3p Inhibits Migration and Invasion of Papillary Thyroid Carcinoma by Downregulating COL1A1 and COL5A1
Wang, C., Wang, Y., Fu, Z., Huang, W.-J., Yu, Z., Wang, J.-C., Zheng, K., Zhang, S.-W., Li, S., & Chen, J.-Q. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.837581 · Cited by 18
“Collagens, the main protein component of ECM, exhibit a variety of effects, demonstrating proliferative, migratory, and differentiative cellular activities in vivo (19).”
A new ex vivo model of the bone tissue response to the hyperglycemic environment – The embryonic chicken femur organotypic culture in high glucose conditions
Araújo, R., Martín, V., Ferreira, R. M., Fernandes, M. H., & Gomes, P. S. (2022) · Bone · doi:10.1016/j.bone.2022.116355 · Cited by 19 · see citing works
Stromal Protein-Mediated Immune Regulation in Digestive Cancers
Gamradt, P., de la Fouchardière, C., & Hennino, A. (2021) · Cancers · doi:10.3390/cancers13010146 · Cited by 25 · see citing works
“Collagen is the most abundant ECM protein that self-assembles into fibrils, provides tissue support for cell growth, and contributes to mechanical resilience of connective tissue [49].”
Background
Unique ligand and kinase-independent roles of the insulin receptor in regulation of cell cycle, senescence and apoptosis
Nagao, H., Jayavelu, A. K., Cai, W., Pan, H., Dreyfuss, J. M., Batista, T. M., Brandão, B. B., Mann, M., & Kahn, C. R. (2023) · Nature Communications · doi:10.1038/s41467-022-35693-5 · Cited by 21 · see citing works
Protective Effects and Molecular Mechanism of Total Flavonoids from Lycium Barbarum Leaves on Photoaged Human Dermal Fibroblasts
Song, F., Wang, L., Mu, J., & Ma, H. (2022) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2022/4156330 · Cited by 17 · see citing works
“e ECM provides significant conditions for the survival and activity of cells, which can affect the shape, function, metabolism, migration, proliferation, and differentiation of cells through signal transduction systems [4].”
Background
Retracted
Promoting collagen synthesis: a viable strategy to combat skin ageing
Wang, S., Li, F., Feng, X., Feng, M., Niu, X., Jiang, X., Chen, W., & Bai, R. (2025) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2025.2488821 · Cited by 18 · see citing works
A Comprehensive Review on the Beneficial Roles of Vitamin D in Skin Health as a Bio-Functional Ingredient in Nutricosmetic, Cosmeceutical, and Cosmetic Applications
Papadopoulou, S. N. A., Anastasiou, E. A., Adamantidi, T., Ofrydopoulou, A., Letsiou, S., & Τσούπρας, Α. (2025) · Applied Sciences · doi:10.3390/app15020796 · Cited by 22 · see citing works
“Normally, young skin contains more than 75% of collagen [178,179].”
HTRA1-driven detachment of type I collagen from endoplasmic reticulum contributes to myocardial fibrosis in dilated cardiomyopathy
Shi, H., Yuan, M., Cai, J., Lan, L., Wang, Y., Wang, W., Zhou, J., Wang, B., Yu, W., Dong, Z., et al. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05098-7 · Cited by 18 · see citing works
“It plays a critical role in various cellular processes such as cell proliferation, differentiation, and migration [55, 56].”
Background
Hypusinated eIF5A is required for the translation of collagen
Barba-Aliaga, M., Mena, A., Espinoza, V., Apostolova, N., Costell, M., & Alepúz, P. (2021) · bioRxiv · doi:10.1101/2021.02.23.432471 · Cited by 16
Quantitative nanohistology of aging dermal collagen
Huang, S., Strange, A. P., Maeva, A. R., Siddiqui, S., Bastien, P., Aguayo, S. D., Vaez, M., Pollock, H. M., Ghibaudo, M., Potter, A., et al. (2023) · Frontiers in Aging · doi:10.3389/fragi.2023.1178566 · Cited by 14 · see citing works
“By implementing Convolutional Neural Network (CNN) approaches37 to identify pathologyrelated morphological collagen fingerprints, it will be possible to create CNN models to predict either early signs or the severity of collagen-based conditions (Arseni et al., 2018).”
BackgroundMethod
Infiltration of laponite: An effective approach to improve the mechanical properties and thermostability of collagen hydrogel
Li, J., Tian, Z.-H., Yang, H., Duan, L., & Liu, Y. (2022) · Journal of Applied Polymer Science · doi:10.1002/app.53366 · Cited by 14
2‐kDa hyaluronan ameliorates human facial wrinkles through increased dermal collagen density related to promotion of collagen remodeling
Abe, Y., Seino, S., Kurihara, H., Kage, M., & Tokudome, Y. (2022) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.15097 · Cited by 14
Collagen synthesis in the skin, its functional and structural features
Borzykh, O. B., Schneider, N. A., Карпова, Е. И., Petrova, M. M., Demina, O. M., & Nasyrova, R. F. (2021) · Medical news of the North Caucasus · doi:10.14300/mnnc.2021.16108 · Cited by 18 · see citing works
“может зависеть от разных факторов, как внешних, так и внутренних [3, 4].”
MALDI imaging combined with two-photon microscopy reveals local differences in the heterogeneity of colorectal cancer
Bharti, A., Ajinkya, K., Markus, M. A., Ramos‐Gomes, F., Bohnenberger, H., Ströbel, P., Alves, F., & Klein, O. (2024) · npj Imaging · doi:10.1038/s44303-024-00041-3 · Cited by 13 · see citing works
“…multimodalapproachintroducedinourstudycouldbeusedtoidentifynoveltargetsnotonlyincancerbutalsoinvariouscollagen-associateddiseases, suchasorgan ﬁ brosisofdifferentorigins,skeletalandcartilageabnormalities, skin alterations, hearing loss and visual defects, as well as muscle weakness 59 .”
Atopic Eczema: Genetic Analysis of COL6A5, COL8A1, and COL10A1 in Mediterranean Populations
Strafella, C., Caputo, V., Minozzi, G., Milano, F., Arcangeli, M., Sobhy, N., Abdelmaksood, R., Hashad, D. I., Vakirlis, E., Novelli, G., et al. (2019) · BioMed Research International · doi:10.1155/2019/3457898 · Cited by 13 · see citing works
A loss of primary cilia by a reduction in mTOR signaling correlates with age-related deteriorations in condylar cartilage
Kitami, M., Kaku, M., Thant, L., & Maeda, T. (2024) · GeroScience · doi:10.1007/s11357-024-01143-x · Cited by 12 · see citing works
“Failure of primary cilia affects various cellular processes, including chondrocyte differentiation [23] and ECM production [20, 24, 25].”
Tolerability and efficacy assessment of an oral collagen supplement for the improvement of biophysical and ultrasonographic parameters of skin in middle eastern consumers
Samadi, A., Movaffaghi, M., Kazemi, F., Yazdanparast, T., Nasrollahi, S. A., & Firooz, A. (2023) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.15700 · Cited by 13 · see citing works
Equol’s efficacy is greater than astaxanthin for antioxidants, extracellular matrix integrity & breakdown, growth factors and inflammatory biomarkers via human skin gene expression analysis
Lephart, E. D. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.03.025 · Cited by 13 · see citing works
Recent Advances in Collagen and Collagen-Based Packaging Materials: A Review
Ezati, P., Khan, A., Bhattacharya, T., Zaitoon, A., Zhang, W.-L., Roy, S., Rhim, J., & Lim, L.-T. (2025) · ACS Food Science & Technology · doi:10.1021/acsfoodscitech.4c00938 · Cited by 11
Multi-organ Transcriptome Atlas of a Mouse Model of Relative Energy Deficiency in Sport (REDs)
van Rosmalen, L., Zhu, J.-Y., Maier, G., Gacasan, E., Lin, T., Zhemchuzhnikova, E., Rothenberg, V., Razu, S. S., Deota, S., Ramasamy, R. K., et al. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.08.001 · Cited by 11 · see citing works
Healthy Aging Metabolomic and Proteomic Signatures Across Multiple Physiological Compartments
Moaddel, R., Candia, J., Ubaida‐Mohien, C., Tanaka, T., Moore, A. Z., Zhu, M., Fantoni, G., Church, S. J., D'Agostino, J., Fan, J., et al. (2025) · Aging Cell · doi:10.1111/acel.70014 · Cited by 14 · see citing works
The Role of Collagens in Atopic Dermatitis
Szalus, K., & Trzeciak, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147647 · Cited by 10 · see citing works
“This process plays a critical role in development, wound healing, and maintaining proper organ homeostasis [24].”
Background
RNA‐Seq reveals distinct transcriptomic differences in rotator cuff tendon based on tear etiology and patient sex
Rai, M. F., Cai, L., Tycksen, E. D., Keener, J., & Chamberlain, A. M. (2022) · Journal of Orthopaedic Research · doi:10.1002/jor.25296 · Cited by 10
“Further immunostaining studies would be needed to demonstrate the association of collagen organization and the functional implication of these collagens in the tendon tissues as changes in collagens have been associated with specific connective tissue diseases.(35) This study also demonstrates the loss in the expressi…”
Background
Paediatric Metabolic Bone Disease: A Lifetime Ahead
Gómez‐Alonso, C. (2020) · Advances in Therapy · doi:10.1007/s12325-019-01174-3 · Cited by 10 · see citing works
Constructing networks for comparison of collagen types
Wesp, V., Scholz, L., Ziermann-Canabarro, J. M., Schuster, S., & Stark, H. (2024) · Journal of Integrative Bioinformatics · doi:10.1515/jib-2024-0020 · Cited by 9 · see citing works
“Theunderstandingofthesequenceandstructureofcollagensiscrucialbecauseofhereditarydiseasesbased on mutations in collagen genes [40], such as osteogenesis imperfecta, Ehlers-Danlos syndrome, and Stickler syndrome.”
Decoding collagen cues: the interplay of integrins and discoidin domain receptors in health and disease
Trono, P., Masi, I., Ottavi, F., & Rosanò, L. (2026) · Journal of Biomedical Science · doi:10.1186/s12929-025-01211-0 · Cited by 13 · see citing works
“…reorganization is central to shaping tissue mechanics in diverse cellular processes driving development, tissue repair, and pathological states [36, 37], DDR2, as major transducer of collagen cues, senses collagen dynamicity and activates intracellular pathways, with a profound impact on cell…”
Proteomic interrogation of the meninges reveals the molecular identities of structural components and regional distinctions along the CNS axis
Santorella, E. M., Balsbaugh, J. L., Ge, S., Saboori, P., Baker, D., & Pachter, J. S. (2023) · Fluids and Barriers of the CNS · doi:10.1186/s12987-023-00473-w · Cited by 8 · see citing works
“Type VI collagen, found in both brain and spinal meninges, consists of monomers that aggregate linearly to form beaded filaments or laterally through their globular domains [9], and might further lend to creating a 3D network in these tissues capable of filtering cellular and soluble elements [56].”
Background
Development of novel hyaluronic acid/human-like collagen bio-composite membranes: A facile "surface modification-assembly" approach.
Luo, X., Liu, Y., Zheng, C., Huo, Q., & Liu, X.-H. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.10.091 · Cited by 9
Characteristics of collagen in ovarian extracellular matrix and its relationship with the development of primordial follicles up to ovulation.
Félix, E. D. S., & Silva, J. (2025) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2025.108029 · Cited by 8
Cell and tissue reprogramming: Unlocking a new era in medical drug discovery
Sen, C. K., Friday, A. J., & Roy, S. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100077 · Cited by 9 · see citing works
Impact of High Glucose on Bone Collagenous Matrix Composition, Structure, and Organization: An Integrative Analysis Using an Ex Vivo Model
Araújo, R., Páscoa, R. N. M. J., Bernardino, R. L., & Gomes, P. S. (2025) · Cells · doi:10.3390/cells14020130 · Cited by 8 · see citing works
“The ECM integrates an array of local and systemic factors, which regulate cellular processes such as growth, differentiation, migration, and survival, through their role in distinct signaling pathways [5,6].”
Unraveling the genetic collagen connection: clinical and therapeutic insights on genetic connective tissue disorders
Neto, N. S. R., Pereira, I. A., Sztajnbok, F., & Azevedo, V. F. (2024) · Revista Brasileira de Reumatologia · doi:10.1186/s42358-024-00373-z · Cited by 11 · see citing works
The CMS19 disease model specifies a pivotal role for collagen XIII in bone homeostasis
Kemppainen, A., Finnilä, M., Heikkinen, A., Härönen, H., Izzi, V., Kauppinen, S., Saarakkala, S. S., Pihlajaniemi, T. A., & Koivunen, J. T. (2022) · Scientific Reports · doi:10.1038/s41598-022-09653-4 · Cited by 9 · see citing works
Contrasting Local and Macroscopic Effects of Collagen Hydroxylation
Varma, S., Orgel, J., & Schieber, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22169068 · Cited by 8
MiR‐1297 attenuates high glucose‐induced injury in HK‐2 cells via targeting COL1A2
Wang, S., Sun, K., Hu, H.-L., Jin, X., Wang, Z., Zhang, H., & Zhao, X. (2021) · Nephrology · doi:10.1111/nep.13881 · Cited by 8
“As the highest content of proteins in mammalian, collagens are the substantial composition of extracellular matrix (ECM), providing scaffolds for tissue formation, remodelling and maintenance.(5) There are at least 28 members of collagen in vertebrates.”
BackgroundInfluential
Oral Collagen Oligopeptides as a Modulator of Skin Health: A Comprehensive Evaluation of Clinical and Molecular Effects
Zague, V., Pinheiro, A. L. T. A., Pinto, J. R., Facchini, G., & Eberlin, S. (2025) · Journal of Medicinal Food · doi:10.1089/jmf.2024.0252 · Cited by 4 · see citing works
A Comprehensive Review on the Role of Collagen in Health and Disease
Pillai, N. S., Khan, S. A., Mehrotra, N., & Jadhav, K. (2024) · Biosciences Biotechnology Research Asia · doi:10.13005/bbra/3307 · Cited by 6 · see citing works
miR–122–5p Promotes Cowshed Particulate Matter2.5-Induced Apoptosis in NR8383 by Targeting COL4A1
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Authors: Arseni, L., Lombardi, A., & Orioli, D.
Affiliations: German Cancer Research Center (DE)
Istituto di Genetica Molecolare (IT)
Corresponding author: Orioli, Donata
ORCID: Arseni, Lavinia
Lombardi, Anita
Orioli, Donata
Venue: International Journal of Molecular Sciences
Publisher: MDPI AG
Published: 2018-05-08
Volume: 19
Issue: 5
Pages: 1407
ISSN: 1422-0067 (ISSN-L)
DOI: 10.3390/ijms19051407
PMC: PMC5983607
OpenAlex: W2800155899
Cited by: 186
References: 172
Citations by year: 2026: 15 · 2025: 31 · 2024: 33 · 2023: 21 · 2022: 23 · 2021: 31 · 2020: 14 · 2019: 12 · 2018: 4
FWCI: 2.13
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: International Journal of Molecular Sciences (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: Deutsches Krebsforschungszentrum
Fondazione Umberto Veronesi
Associazione Italiana per la Ricerca sul Cancro (IG 17710, 17710)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords: collagen, extracellular matrix, collagen degradation, cell proliferation, cell migration, cell differentiation, diagnosis
MeSH terms: Cell Movement, Collagen, Extracellular Matrix, Humans, Phenotype, Structure-Activity Relationship, Extracellular Matrix Proteins, Genetic Diseases, Inborn, Cell Proliferation

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From Structure to Phenotype: Impact of Collagen Alterations on Human Health

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