Laminin peptides stimulate human neutrophil motility

摘要: Laminin, isolated from Engelbreth-Holm-Swarm tumor, and 10 chemically synthesized peptides, corresponding to various regions of the laminin A B1 chains, were compared for their abilities stimulate human peripheral blood polymorphonuclear leukocyte (PMN) chemotaxis chemokinesis through polycarbonate membrane filters in a 48-well microchemotaxis assay. Peptides F-9, F-11, F-12, F-13 derived chain at intersection cross, six peptides chain: peptide TG-1 amino-terminal top globule; GD-1, GD-3, GD-6, GD-7 carboxyl-terminal globular domain; AG-1 above domain. Laminin evaluated over concentration range 1 200 micrograms/ml motility assays. Six TG-1, stimulated PMN migration absence gradient (chemokinesis). fluorescein conjugate most active peptide, exhibited nonspecific, nonsaturable binding PMN. Intact other failed migration. In contrast, intact rabbit chemokinesis. These results demonstrate that PMNs have divergent migratory responses laminin. findings suggest basement does not directly vivo, but selected sequences, which may be generated during proteolytic digestion laminin, can activate