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The role of small leucine-rich proteoglycans in collagen fibrillogenesis.

Matrix biology : journal of the International Society for Matrix Biology (2010-01-19)
Sebastian Kalamajski, Ake Oldberg
ZUSAMMENFASSUNG

Small leucine-rich proteoglycans/proteins (SLRPs) are associated with collagen fibril formation, and therefore important for the proper formation of extracellular matrices. SLRPs are differentially expressed in tissues and during pathological conditions, contributing to the development of connective tissue properties. The binding of SLRPs to collagens have recently been characterized, and may give some clues to the significance of these interactions. In this mini review, we summarize published work in this field, and propose several mechanisms for how SLRPs can control collagen matrix structure and function. SLRPs appear to influence collagen cross-linking patterns. We also propose that the SLRP-collagen interactions can assist in the process of juxtaposing the collagen monomers by steric hindrance or by directly connecting two collagen monomers during the fibril growth.

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Sigma-Aldrich
L-Leucin, from non-animal source, meets EP, JP, USP testing specifications, suitable for cell culture, 98.5-101.0%
Sigma-Aldrich
L-Leucin, reagent grade, ≥98% (HPLC)
Sigma-Aldrich
L-Leucin, BioUltra, ≥99.5% (NT)
Sigma-Aldrich
L-Leucin, 99%, FG
Supelco
L-Leucin, Pharmaceutical Secondary Standard; Certified Reference Material
Supelco
L-Leucin, certified reference material, TraceCERT®, Manufactured by: Sigma-Aldrich Production GmbH, Switzerland
Leucin, European Pharmacopoeia (EP) Reference Standard