The effects of bovine serum albumin and the chemotactic peptide formyl-methionyl-leucyl-phenylalanine on the adherence of guinea pig polymorphonuclear leukocytes to nylon fiber columns.

Glycogen-induced guinea pig polymorphonuclear leukocytes were passed over nylon fiber columns and adherent and nonadherent fractions were quantitated by determination of hexosaminidase activity after lysis with Triton. Bovine serum albumin reduced the number of adherent cells at 37 degrees C as well as 4 degrees C, after fixation of the cells with glutaraldehyde, and in the absence and presence of EDTA. The chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine increased the adherent cell fraction at 37 degrees C, but failed to do so at 4 degrees C, after glutaraldehyde fixation and in the presence of 10 mmol/EDTA. Since metabolic inhibitors had no effect on the rate of adherence it is suggested that increased cell deformability is responsible for chemotactic factor-induced increased cell attachment to nylon fibers.