Hyaluronate binding proteins also bind to fibronectin, laminin and collagen.
Small molecular weight proteins, isolated from the culture medium of embryonic chick heart fibroblasts and 3T3 cell lines by hyaluronate affinity chromatography, bind in order of apparent affinity, to hyaluronate, fibronectin, collagen and laminin. Such proteins isolated from the MSV-transformed 3T3 cell line bind in greater amounts to the nectins and hyaluronate than do similar proteins isolated from heart fibroblasts or 3T3 cells. These small hyaluronate binding proteins are immunologically distinct from other well characterized proteins such as laminin, fibronectin, bovine serum albumin and actin. Their relationship to other small, extracellular proteins and their possible role in structuring of extracellular matrix are discussed.
D000818:Animals; D001667:Binding, Competitive; D001704:Biopolymers; D002352:Carrier Proteins / Q000378:metabolism*; D002460:Cell Line; D002645:Chickens; D002846:Chromatography, Affinity; D003094:Collagen / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D005347:Fibroblasts / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism*; D018960:Hyaluronan Receptors; D007797:Laminin / Q000378:metabolism*; D051379:Mice; D009206:Myocardium / Q000378:metabolism; D011485:Protein Binding
D001704:Biopolymers; D002352:Carrier Proteins; D005353:Fibronectins; D018960:Hyaluronan Receptors; D007797:Laminin; D003094:Collagen