Cited by 378Proteoglycans and glycosaminoglycans researchBone and Dental Protein StudiesConnective tissue disorders research

The regulatory roles of small leucine‐rich proteoglycans in extracellular matrix assembly

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Chen, Shoujun, Birk, David E.·2013·The FEBS Journal

Abstract

Small leucine‐rich proteoglycans ( SLRP s) are involved in a variety of biological and pathological processes. This review focuses on their regulatory roles in matrix assembly. SLRP s have protein cores and hypervariable glycosylation with multivalent binding abilities. During development, differential interactions of SLRP s with other molecules result in tissue‐specific spatial and temporal distributions. The changing expression patterns play a critical role in the regulation of tissue‐specific matrix assembly and therefore tissue function. SLRP s play significant structural roles within extracellular matrices. In addition, they play regulatory roles in collagen fibril growth, fibril organization and extracellular matrix assembly. Moreover, they are involved in mediating cell–matrix interactions. Abnormal SLRP expression and/or structures result in dysfunctional extracellular matrices and pathophysiology. Altered expression of SLRP s has been found in many disease models, and structural deficiency also causes altered matrix assembly. SLRP s regulate assembly of the extracellular matrix, which defines the microenvironment, modulating both the extracellular matrix and cellular functions, with an impact on tissue function.

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Crossref · 10.1111/febs.12136

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  • The surface gaps are a primary binding site for dermatan sulphate-containing proteoglycans, which are necessary for preventing adjacent fibrils from fusing together.

    “They are also a primary binding site for dermatan sulphate-containing proteoglycans (Scott and Haigh, 1988), which, as we will also see later, are necessary for preventing adjacent fibrils from fusing together (Chen and Birk, 2013).”

    From Corneal structure and transparency (2015) · cites this paper as Chen and Birk, 2013

    The section “Instructive roles in collagen fibrillogenesis” (page unavailable) says that proteoglycan glycosaminoglycans extend into the space between fibrils and can influence their spacing and organization. It does not say that dermatan sulphate-containing proteoglycans are necessary to prevent adjacent fibrils from fusing. The surface-binding-site clause is cited to Scott and Haigh, not Chen and Birk, and is not judged here. (LLM, conf=0.84)

    Experimental — accuracy not yet measured
  • In the mammalian cornea, the most likely corneal crystallin candidates are aldehyde dehydrogenases, particularly ALDH3A1, first detected in bovine cornea and later confirmed by others.

    “In the mammalian cornea, the most likely candidates are aldehyde dehydrogenases, particularly ALDH3A1, that was first detected in the bovine cornea by Holt and Kinoshita (1973) and later confirmed by others (Alexander et al., 1981, Silverman et al., 1981, Chen et al., 2013).”

    From Corneal structure and transparency (2015) · cites this paper as Chen et al., 2013

    The sections on corneal SLRPs and matrix integrity discuss proteoglycans, collagen organization, and transparency, but not corneal crystallins or aldehyde dehydrogenases. Searches for ALDH3A1, corneal crystallins, and Holt and Kinoshita found no passage addressing the claimed identification or its history. (LLM, conf=0.76)

    Experimental — accuracy not yet measured
  • Corneal crystallins change the refractive index of the cell cytoplasm to better match the extracellular matrix and thus eliminate scattering.

    “they have a dual role in that they change the refractive index of the cell cytoplasm to better match the extracellular matrix and thus eliminate scattering (Chen et al., 2013).”

    From Corneal structure and transparency (2015) · cites this paper as Chen et al., 2013

    The sections on SLRP expression and disrupted matrix integrity discuss corneal transparency and light scattering in relation to stromal collagen organization. Searches for corneal crystallins and refractive-index matching found no passage in our copy addressing the claimed cytoplasmic mechanism. No page numbers were available for these passages. (LLM, conf=0.75)

    Experimental — accuracy not yet measured

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Cited by

Sorted by citations

Authors
Chen, S., & Birk, D. E.
Affiliations
University of South Florida (US)
Corresponding author
Birk, David E.
Venue
The FEBS Journal
Publisher
Wiley
Published
2013-02-14
Volume
280
Issue
10
Pages
2120-2137
ISSN
  • 1742-464X (ISSN-L)
  • 1742-4658
OpenAlex
W2009298572
Cited by
378
References
0
Citations by year
2026: 25 · 2025: 33 · 2024: 15 · 2023: 29 · 2022: 30 · 2021: 34 · 2020: 45 · 2019: 25 · 2018: 36 · 2017: 26 · 2016: 20 · 2015: 23 · 2014: 24 · 2013: 12
FWCI
2.88
Type
journal article
Language
en
Open access
Locations
  • FEBS Journal (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
Funders
  • National Institutes of Health
  • National Eye Institute (R01EY005129, EY05129)
  • National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR44745, R01AR044745)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
  • Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Connective tissue disorders research
Keywords
small leucine-rich proteoglycans, extracellular matrix assembly, collagen fibril organization, cell-matrix interactions, multivalent binding
MeSH terms
Lumican, Animals, Collagen, Cornea, Corneal Dystrophies, Hereditary, Extracellular Matrix, Humans, Keratan Sulfate, Leucine, Protein Binding, Chondroitin Sulfate Proteoglycans, Proteoglycans, Tendons, Protein Transport, Protein Interaction Mapping

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