Fluid shear stress induces actin polymerization in human neutrophils

✍ Scribed by Masaki Okuyama; Yoshihiko Ohta; Jun-ichi Kambayashi; Morito Monden

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 866 KB
• Volume: 63
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/(sici)1097-4644(19961215)63:4<432::aid-jcb5>3.0.co;2-u

✦ Synopsis

We have previously reported that a physiological range of shear stress induces neutrophil homotypic aggregation mediated by lymphocyte function-associated antigen-I (LFA-1) and intercellular adhesion rnolecule-3 (ICAM-3) interactions. To further characterize the homotypic aggregation, actin polymerization was investigated in neutrophils stimulated by shear stress in comparison with formyl-methionyl-leucyl-phenylalanine (fMLP). In fhlLPstimulated neutrophils, actin polymerization was localized in the pseudopods, and this reaction was not mediated by a cytosolic level of Ca2+. in contrast to fMLP stimulation, the actin polymerization induced by shear stress in a cone-plate viscometer was localized in cell-cell contact regions, and this polymerization required the increase of intracellular Ca2+. This shear stress-induced actin polymerization was not observed when neutrophils were pretreated with anti-LFA-I or anti-ICAM-3 antibody. in conclusion, LFA-1 and ICAM-3 interaction mediated by the increase of [Ca2+]i generated the intercellular signal in order to accumulate F-actin in the cell-cell contact regions.