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Am J Physiol Heart Circ Physiol 275: H145-H150, 1998;
0363-6135/98 $5.00
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Vol. 275, Issue 1, H145-H150, July 1998

Three noncontiguous peptides comprise binding sites on high-molecular-weight kininogen to neutrophils

Mohammad M. H. Khan1,2, Satya P. Kunapuli1,3, Yingzhang Lin1, Abraham Majluf-Cruz1, Raul A. Dela Cadena1,4, Stuart L. Cooper2, and Robert W. Colman1,5

1 The Sol Sherry Thrombosis Research Center and Departments of 3 Physiology, 4 Pathology, and 5 Medicine, Temple University School of Medicine, Philadelphia, Pennsylvania 19140; and 2 Department of Chemical Engineering, University of Delaware, Newark, Delaware 19716

The binding of high-molecular-weight kininogen (HK) to neutrophils (polymorphonuclear leukocytes, PMN) is required for the stimulation of aggregation and degranulation by human plasma kallikrein as well as the displacement of fibrinogen from this cell surface. The putative receptor for HK is the leukocyte integrin alpha Mbeta 2, and domains 3 (D3) and 5 (D5) of HK form its binding site. To further map the binding sites on HK for PMN, we used D3 recombinant exon products and designed peptides from D3 and D5. In D3, a heptapeptide, Leu271-Ala277, from exon 7 product, and a peptide, Cys333-Cys352, from exon 9 product can inhibit binding of kininogen to PMN. Two contiguous peptides from D5 in the histidine-glycine-rich region, Gly442-Lys458 and Phe459-Lys478, each inhibit the binding of HK to PMN. This study has thus delineated three noncontiguous surface-oriented sequences on HK, which together comprise all or most of the binding site for human PMN.

kininogen; Mac-1 (alpha Mbeta 2); polymorphonuclear leukocytes; binding sites


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