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

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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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Figure 1 Schematic representation of the complex meshwork of proteins forming the extracellular matrix (ECM). The main ECM components, namely collagens, proteoglycans, hyaluronan, fibronectin, laminin and elastin, as well as the integrin ECM receptors, are depicted. The ECM provides mechanical support and anchoring for cells and tissues but it also acts as a reservoir of growth factors and cytokines and regulator of normal tissue development and homeostasis. Alterations in any of these functions result in a pathological status characterized by various tissue abnormalities.CC BY · PubMed Central

Figure 2 Schematic representation of collagen biosynthesis steps. The main biosynthesis steps of various collagen types are indicated. Green arrows highlight the contiguous processing steps whereas red arrows indicate the final step of collagen assembly into the different structural conformations. Coloured boxes on the right indicate potential alterations occurring during collagen processing at different steps, thus causing abnormalities in the structure and/or assembly. Abbreviations: NC, non-collagenous domain.CC BY · PubMed Central

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Unique ligand and kinase-independent roles of the insulin receptor in regulation of cell cycle, senescence and apoptosis
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Hypusinated eIF5A is required for the translation of collagen
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Atopic Eczema: Genetic Analysis of COL6A5, COL8A1, and COL10A1 in Mediterranean Populations
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Oral Collagen Oligopeptides as a Modulator of Skin Health: A Comprehensive Evaluation of Clinical and Molecular Effects
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Magnesium deficiency and its interaction with the musculoskeletal system, exercise, and connective tissue: an evidence synthesis
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The correlation between total protein content and antioxidant activity of collagen isolated from a marine sponge Stylissa flabelliformis collected from North Lombok Indonesia coast
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Curcumin alleviates TGF-β1-induced fibrosis in NRK-49F cells via suppression of miR-21 expression, and regulation of the TGF-β1/smad3 signaling pathway
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“as ( ) ( ) ( ) ( ) 1 1 2 1 1 cos 2 1 F F a b φ θ   = − − −   , and then the amplitude of the photoacoustic signal at the second layer can be expressed as ( ) ( ) ( ) ( ) 1 1 1, 1 cos 2 1 PA F a b φ φ θ   ∝ + −   [5]”

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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