TY - JOUR
T1 - A peptide derived from neutrophil inhibitory factor (NIF) blocks neutrophil adherence to endothelial cells
AU - Madden, K.
AU - Janczak, J.
AU - McEnroe, G.
AU - Lim, D.
AU - Hartman, T.
AU - Liu, D.
AU - Stanton, L.
PY - 1997
Y1 - 1997
N2 - Objective and Design: Peptides derived from neutrophil inhibitory factor (NIF), a known antagonist of Mac-1, were evaluated as inhibitors of neutrophil adherence. Material: In vitro assays of adherence employed: 1) human polymorphonuclear cells (PMN), 2) human umbilical vein endothelial cells (HUVEC), and 3) CHO cells expressing ICAM-1 (CHO-ICAM cells). Treatment: Cells, pretreated with NIF-derived peptides (0.1-100μM) for 10 minutes, were permitted to adhere for 20 min in the continued presence of peptide. Methods: Cell-based assays: 1) PMN adherence to HUVEC, 2) PMN adhesion to immobilized human serum proteins, and 3) adherence of CHO-ICAM cells to immobilized Mac-1. Results: A NIF-derived peptide of 29 amino acids blocked PMN adherence to HUVEC, but behaved somewhat differently than the parent NIF protein. NIF specifically antagonized Mac-1 dependent adherence, but the peptide blocked neutrophil adherence that was dependent upon both Mac-1 and LFA-1 integrins. CHO-ICAM adherence to Mac-1 was blocked by NIF, but not by the peptide. Binding studies with NIF and the peptide indicate that the molecules bind to different sites. Conclusions: A peptide derived from NIF blocks PMN adherence but, unlike NIF, the mechanism of action is not mediated by direct antagonism Mac-1.
AB - Objective and Design: Peptides derived from neutrophil inhibitory factor (NIF), a known antagonist of Mac-1, were evaluated as inhibitors of neutrophil adherence. Material: In vitro assays of adherence employed: 1) human polymorphonuclear cells (PMN), 2) human umbilical vein endothelial cells (HUVEC), and 3) CHO cells expressing ICAM-1 (CHO-ICAM cells). Treatment: Cells, pretreated with NIF-derived peptides (0.1-100μM) for 10 minutes, were permitted to adhere for 20 min in the continued presence of peptide. Methods: Cell-based assays: 1) PMN adherence to HUVEC, 2) PMN adhesion to immobilized human serum proteins, and 3) adherence of CHO-ICAM cells to immobilized Mac-1. Results: A NIF-derived peptide of 29 amino acids blocked PMN adherence to HUVEC, but behaved somewhat differently than the parent NIF protein. NIF specifically antagonized Mac-1 dependent adherence, but the peptide blocked neutrophil adherence that was dependent upon both Mac-1 and LFA-1 integrins. CHO-ICAM adherence to Mac-1 was blocked by NIF, but not by the peptide. Binding studies with NIF and the peptide indicate that the molecules bind to different sites. Conclusions: A peptide derived from NIF blocks PMN adherence but, unlike NIF, the mechanism of action is not mediated by direct antagonism Mac-1.
KW - Cell adhesion
KW - Mac-1
KW - Neutrophil inhibitory factor (NIF)
KW - Neutrophils
UR - http://www.scopus.com/inward/record.url?scp=0030769469&partnerID=8YFLogxK
U2 - 10.1007/s000110050176
DO - 10.1007/s000110050176
M3 - Article
C2 - 9243305
AN - SCOPUS:0030769469
SN - 1023-3830
VL - 46
SP - 216
EP - 223
JO - Inflammation Research
JF - Inflammation Research
IS - 6
ER -