Characterization of binding properties of the myelin-associated glycoprotein to extracellular matrix constituents.

摘要: The myelin-associated glycoprotein (MAG) can be obtained from adult mouse brain detergent-lysates of a crude membrane fraction as 96-100 kd form (detergent solubilized MAG), and 100,000 g supernatants homogenates 90-96 (soluble MAG). soluble distributes into the Triton X-114-poor aqueous phase, while detergent-solubilized MAG predominantly enters X-114-rich phase. Both molecular forms bind to heparin in hypo- isotonic buffers. Soluble binds several collagens (type G, I, II, III, IV, V, VI, IX) with 5.7 X 10(-8) M for collagen type IX 2.0 10(-7) IV. Binding 125I-labeled G completely inhibited by unlabeled but not heat-denatured collagen. does itself, laminin, fibronectin, or neural cell adhesion molecules L1 N-CAM. is most effectively blocked high weight dextran sulfate, heparan sulfate heparin, chondroitin low being less potent blockers. These findings are agreement previous observations on localization basal lamina interstitial sciatic nerve situ.