The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins

If one of the keys to biology is protein structure, then nature is an efficient operator, because it adopts a number of structurally related proteins to perform functions as diverse as maintaining the mineralized matrix of bones and teeth, the transparency of the cornea, the tensile strength of the...

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Bibliographic Details
Published in:The Journal of biological chemistry 1999-07, Vol.274 (27), p.18843-18846
Main Author: Iozzo, R V
Format: Article
Language:English
Subjects:
Animals
Cell Division
Extracellular Matrix - physiology
Humans
Leucine
Models, Molecular
Proteoglycans - chemistry
Proteoglycans - genetics
Proteoglycans - physiology
Receptor Protein-Tyrosine Kinases - metabolism
Structure-Activity Relationship
Transforming Growth Factor beta - antagonists & inhibitors
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Summary:If one of the keys to biology is protein structure, then nature is an efficient operator, because it adopts a number of structurally related proteins to perform functions as diverse as maintaining the mineralized matrix of bones and teeth, the transparency of the cornea, the tensile strength of the skin and tendon, and the viscoelasticity of blood vessels. Proteoglycans play key roles in all of these fundamental biological processes and behave as potent effectors of cellular pathways. The past decade has witnessed an explosion of knowledge in the proteoglycan world, with significant advances in the genetics and cell biology of these complex macromolecules. This minireview describes recent advances in the biology of the small leucine-rich proteoglycan (SLRP) super(1) gene family with special emphasis on the biology of the archetype proteoglycan decorin. The focus is on the "functional network" created by these molecules in tissues, on genetic evidence for their functional roles during ontogeny, and on their activities as modulators of complex pathological processes such as fibrosis and cancer growth. Other more extensive reviews may serve to fill the gaps in this one.
ISSN:0021-9258
DOI:10.1074/jbc.274.27.18843