Interaction of casein with human polymorphonuclear cells.
Attachment of 125I-casein to PMN cells was investigated. Iodination did not decrease the chemotactic effect of casein. 125I-casein binding was increasing toward a maximum reached at about 45 min at 24, and 37 degrees C. At 4 degrees C the binding was proportional to time for 45 min. No saturation was achieved even at 15 mg/ml casein. About 40% of casein remained attached to PMN in a casein-free medium after 60 min, at 37 degrees C. Pretreatment of the cells with trypsin or butanol, or the presence of indomethacin, azide, and PMSF did not affect the binding of casein. The hydrophobic amino acid, leucin counteracted the attachment of casein. Our data show that at chemotactic doses casein is bound specifically to cell membranes by hydrophobic forces. The induction of chemotaxis may be due to micellar casein-membrane lipid complexes.
D000328:Adult; D001667:Binding, Competitive; D002364:Caseins / Q000097:blood*; D002462:Cell Membrane / Q000378:metabolism; D006801:Humans; D007457:Iodine Radioisotopes; D007700:Kinetics; D009504:Neutrophils / Q000378:metabolism*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000494:pharmacology
D002364:Caseins; D007457:Iodine Radioisotopes; D012710:Serum Albumin, Bovine