Macrophage receptors for lumican. A corneal keratan sulfate proteoglycan.

摘要: Purpose. Keratan sulfate proteoglycans (KSPCs) of the cornea exhibit a characteristic change in glycosylation resulting from stromal inflammation and scarring. To examine potential roles for these molecules pathobiology cornea, authors investigated interaction inflammatory macrophages with KSPCs vitro. Methods. Attachment spreading mouse peritoneal were examined on surfaces coated corneal proteoglycans, intact or modified glycosylation. Solution-phase interactions demonstrated using soluble labeled 125 l-Iodine fluorescein. The affinity specificity determined by competitive inhibition unlabeled proteoglycans. Results. Macrophages did not adhere to KSPGs but attach spread rapidly lumican core protein after removal keratan chains. Arterial lumican, nonsulfated form this proteoglycan, also stimulated macrophage attachment. Labeled arterial specifically bound high affinity. Flow cytometry proportion binding lumican. Lumican was inhibited divalent cation-chelators polyanions. Inhibition kinetics distinct maleated bovine serum albumin, collagen, laminin, fibronectin. Conclusions. highly sulfated do promote adhesion; however, low-sulfate present pathologic corneas may act localize regions inflammation, receptor differs scavenger receptors several other extracellular matrix molecules.