Centro de Biología Molecular "Severo Ochoa" Consejo Superior de Investigaciones Científicas (C.S.I.C.)/Universidad Autónoma de Madrid (Madrid), Madrid, Spain.
School of Medicine, University of Cardiff, Cardiff, United Kingdom.
Sci Rep. 2016 Nov 23;6:37374. doi: 10.1038/srep37374.
Collagens constitute a large family of extracellular matrix (ECM) proteins that play a fundamental role in supporting the structure of various tissues in multicellular animals. The mechanical strength of fibrillar collagens is highly dependent on the formation of covalent cross-links between individual fibrils, a process initiated by the enzymatic action of members of the lysyl oxidase (LOX) family. Fibrillar collagens are present in a wide variety of animals, therefore often being associated with metazoan evolution, where the emergence of an ancestral collagen chain has been proposed to lead to the formation of different clades. While LOX-generated collagen cross-linking metabolites have been detected in different metazoan families, there is limited information about when and how collagen acquired this particular modification. By analyzing telopeptide and helical sequences, we identified highly conserved, potential cross-linking sites throughout the metazoan tree of life. Based on this analysis, we propose that they have importantly contributed to the formation and further expansion of fibrillar collagens.
胶原蛋白是细胞外基质（ECM）蛋白大家族中的一员，在支撑多细胞动物的各种组织结构方面发挥着基础性作用。纤维状胶原蛋白的机械强度高度依赖于各个纤维之间形成的共价交联，这一过程由赖氨酰氧化酶（LOX）家族成员的酶促作用引发。纤维状胶原蛋白存在于多种动物中，因此通常与后生动物的进化有关，其中提出了祖先胶原蛋白链的出现导致了不同进化枝的形成。虽然在不同的后生动物家族中都检测到了 LOX 生成的胶原蛋白交联代谢物，但关于胶原蛋白何时以及如何获得这种特殊修饰的信息有限。通过分析末端肽和螺旋序列，我们在整个后生动物生命树中鉴定到了高度保守的、潜在的交联位点。基于这一分析，我们提出，这些交联位点对纤维状胶原蛋白的形成和进一步扩展起到了重要作用。
