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

Shoujun Chen, +1 more
- 01 May 2013 - 
- Vol. 280, Iss: 10, pp 2120-2137
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TLDR
Small leucine‐rich proteoglycans regulate assembly of the extracellular matrix, which defines the microenvironment, modulating both the extracllular matrix and cellular functions, with an impact on tissue function.
Abstract
Small leucine-rich proteoglycans (SLRPs) are involved in a variety of biological and pathological processes. This review focuses on their regulatory roles in matrix assembly. SLRPs have protein cores and hypervariable glycosylation with multivalent binding abilities. During development, differential interactions of SLRPs 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. SLRPs 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 SLRPs has been found in many disease models, and structural deficiency also causes altered matrix assembly. SLRPs 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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Myocardial Extracellular Matrix An Ever-Changing and Diverse Entity

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References
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Journal ArticleDOI

Collagen fibril formation

TL;DR: Preliminary evidence from invertebrates is included which suggests that the principles for bipolar fibril assembly were established at least 500 million years ago, and how mature fibrils are assembled from early fibrILS is reviewed.
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Targeted Disruption of Decorin Leads to Abnormal Collagen Fibril Morphology and Skin Fragility

TL;DR: A fundamental role is demonstrated for decorin in regulating collagen fiber formation in vivo in mice harboring a targeted disruption of the decorin gene, which provides an explanation for the reduced tensile strength of the skin.
Journal ArticleDOI

Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators.

TL;DR: A working hypothesis is put forward for how fibronectin and integrins determine the site of fibril assembly, and collagens V and XI (the nucleators) initiate collagen fibrillogenesis.
Journal ArticleDOI

Targeted disruption of the biglycan gene leads to an osteoporosis-like phenotype in mice

TL;DR: This is the first report in which deficiency of a non-collagenous ECM protein leads to a skeletal phenotype that is marked by low bone mass that becomes more obvious with age and may serve as an animal model to study the role of ECM proteins in osteoporosis.
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