A current viewpoint on structure and evolution of collagens. I. Fibrillar collagens

Abstract

This review summarizes current data of structure of the most representative group of superfamily of collagens-fibrillar collagens. The attention is focused on structural organization of individual domains and their functional role in the hierarchical stacking of collagen α-chains. There are presented characteristics of the main stages of biosynthesis and the supramolecular processing of fibrillar collagens. Also considered are some aspects of evolution of fibrillar collagens. The role of duplication of genome and genes, intergene combination, and translocation of exons in evolution of collagen genes is discussed.

Production of recombinant human procollagen type I C-terminal propeptide and establishment of a sandwich ELISA for quantification

“…Collagens are the major structural proteins of the extracellular matrix that play a crucial role in providing connective tissue structural integrity and homeostasis 1 . Particularly, they are highly associated with bone metabolism, wound healing, and skin recovery, and thus their synthesis is tightly controlled and regulated 2 .…”

“…Particularly, they are highly associated with bone metabolism, wound healing, and skin recovery, and thus their synthesis is tightly controlled and regulated 2 . There are approximately 28 different types of collagens, all of which are composed of three polypeptide chains (α chains) forming either homotrimers with three identical α chains or heterotrimers with two/three different α chains 1 . Type I collagen is the most abundant human body collagen accounting for almost 90% of the organic portion of the bone matrix 2 , 3 .…”

Collagen cross-linking: insights on the evolution of metazoan extracellular matrix

“…Given the modular nature of the collagen molecule, different approaches have been used to study its evolutionary history, including phylogenetic or genomic analyses of the propeptides, the triple helix, or even of the intron-exon organization14151617. Regardess of the approach, all authors agree on the appearance of an ancestral fibrillar collagen in the lineage leading up to the Metazoa, given the fact that the choanoflagellate Monosiga brevicollis , the sister group to Metazoa, encode proteins with triple helical and C-propeptide (COLFI) sequences in different polypeptides, while collagens present in sponges include both in the same protein chain1418.…”

Atomic Force Microscopy for Collagen-Based Nanobiomaterials

“…For instance, a strong correlation between the orientation of Dband and cell elongation has been reported [14]. Collagen type I fibrils are the elementary building blocks in many collagen-rich tissues [16,17] and collagen has a wide range of functions, from tissue mechanical strength and scaffolding to cell migration and tissue repair [1,4,18]. Collagen presents different morphologies in different tissues [1].…”