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

The binding of highmolecular-weight kininogen (HK) to neutrophils (polymorpho-nuclear 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 leu...

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Veröffentlicht in:American journal of physiology. Heart and circulatory physiology 1998-07, Vol.44 (1), p.H145-H150
Hauptverfasser: KHAN, M. M. H, KUNAPULI, S. P, YINGZHANG LIN, MAJLUF-CRUZ, A, DELA CADENA, R. A, COOPER, S. L, COLMAN, R. W
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Sprache:eng
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Zusammenfassung:The binding of highmolecular-weight kininogen (HK) to neutrophils (polymorpho-nuclear 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 alphaMbeta2, and domains 3 (D3) and 5 (D5) of HK form its binding site.
ISSN:0363-6135
1522-1539