The collagen family members as cell adhesion proteins.
The collagen family of extracellular matrix proteins has played a fundamental role in the evolution of multicellular animals. At the present, 28 triple helical proteins have been named as collagens and they can be divided into several subgroups based on their structural and functional properties. In tissues, the cells are anchored to collagenous structures. Often the interaction is indirect and mediated by matrix glycoproteins, but cells also express receptors, which have the ability to directly bind to the triple helical domains in collagens. Some receptors bind to sites that are abundant in all collagens. However, increasing evidence indicates that the coevolution of collagens and cell adhesion mechanisms has given rise to receptors that bind to specific motifs in collagens. These receptors may also recognize the different members of the large collagen family in a selective manner. This review summarizes the present knowledge about the properties of collagen subtypes as cell adhesion proteins.
Heino
Jyrki
J
Department of Biochemistry and Food Chemistry, University of Turku, Arcanum, Vatselankatu 2, FI-20014 Turku, Finland. jyheino@utu.fi
D020816:Amino Acid Motifs; D000818:Animals; D001665:Binding Sites; D002448:Cell Adhesion / Q000502:physiology; D003094:Collagen / Q000737:chemistry / Q000145:classification* / Q000235:genetics / Q000378:metabolism*; D005109:Extracellular Matrix / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D011485:Protein Binding; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D038981:Receptors, Collagen / Q000737:chemistry* / Q000378:metabolism*
D006023:Glycoproteins; D038981:Receptors, Collagen; D003094:Collagen