Lund University, Department of Experimental Medical Science, BMC B12, Lund, Sweden.
Matrix Biol. 2010 May;29(4):248-53. doi: 10.1016/j.matbio.2010.01.001. Epub 2010 Jan 18.
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.
小富含亮氨酸的蛋白聚糖/蛋白 (SLRPs) 与胶原纤维形成有关，因此对细胞外基质的正常形成非常重要。SLRPs 在组织和病理条件下表达不同，有助于结缔组织特性的发展。最近对 SLRPs 与胶原蛋白的结合进行了表征，这可能为这些相互作用的意义提供了一些线索。在这个迷你综述中，我们总结了该领域的已发表工作，并提出了 SLRPs 如何控制胶原基质结构和功能的几种机制。SLRPs 似乎会影响胶原的交联模式。我们还提出，SLRP-胶原蛋白相互作用可以通过空间位阻或在纤维生长过程中直接连接两个胶原蛋白单体来协助将胶原蛋白单体并置。
