Interaction between collagens and glycosaminoglycans investigated using a surface plasmon resonance biosensor.
The interactions of glycosaminoglycans with collagens and other glycoproteins in extracellular matrix play important roles in cell adhesion and extracellular matrix assembly. In order to clarify the chemical bases for these interactions, glycosaminoglycan solutions were injected onto sensor surfaces on which collagens, fibronectin, laminin, and vitronectin were immobilized. Heparin bound to type V collagen, type IX collagen, fibronectin, laminin, and vitronectin; and chondroitin sulfate E bound to type II, type V, and type VII collagen. Heparin showed a higher affinity for type IX collagen than for type V collagen. On the other hand, chondroitin sulfate E showed the highest affinity for type V collagen. The binding of chondroitin sulfate E to type V collagen showed higher affinity than that of heparin to type V collagen. These data suggest that a novel characteristic sequence included in chondroitin sulfate E is involved in binding to type V collagen.
Munakata
H
H
Department of Biochemistry, Hirosaki University School of Medicine, Japan.
Takagaki
K
K
Majima
M
M
Endo
M
M
D000818:Animals; D002809:Chondroitin Sulfates / Q000737:chemistry / Q000378:metabolism; D003094:Collagen / Q000737:chemistry / Q000378:metabolism*; D016326:Extracellular Matrix Proteins / Q000737:chemistry / Q000378:metabolism; D006025:Glycosaminoglycans / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D011485:Protein Binding; D020349:Surface Plasmon Resonance
D016326:Extracellular Matrix Proteins; D006025:Glycosaminoglycans; D002809:Chondroitin Sulfates; D003094:Collagen