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.
By Sebastian Kalamajski and Åke Oldberg
Abstract
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.