Expression of the 50-kDa integrin-associated protein on myeloid cells and erythrocytes


Por: Rosales C., Gresham H.D., Brown E.J.

Publicada: 1 ene 1992
Resumen:
Integrin-associated protein (IAP) is a 50-kDa intrinsic membrane protein that is involved in signal transduction during neutrophil activation by a variety of Arg-Gly-Asp-containing ligands. However, IAP does not itself directly bind these ligands, which are instead recognized by the leukocyte response integrin (LRI). In fact, IAP is more widely expressed than the LRI and is even on erythrocytes, which express no known integrins. This suggests that IAP may have additional functions besides signal transduction in association with the LRI. In this work we have quantitated IAP expression on several myeloid cells and cell lines, as well as erythrocytes, using a mAb which recognizes this protein. These data show that there are about 10,000 IgG-binding sites on each erythrocyte and 20 times that number on the myeloid cell lines U937 and HL60. Normal PMN and monocytes express about 25,000 IgG-binding sites. There are twice as many Fab'-binding sites on each cell, suggesting that each IgG binds via both Agcombining sites. Binding data using several mAb to IAP suggest that IAP undergoes a temperature-dependent conformational change. Unlike some integrin receptors, IAP is not stored in a regulated secretory compartment in polymorphonuclear leukocytes (PMN). In addition, there is no evidence for internalization or shedding of IAP upon PMN activation. These data show that IAP is expressed at significant levels on myeloid cells and erythrocytes and that its expression is unaffected by the state of PMN activation.

Filiaciones:
Rosales C.:
 Division of Infectious Diseases, Washington Univ. School of Medicine, Campus Box 8051, St. Louis, MO 63110, United States

Gresham H.D.:
 Division of Infectious Diseases, Washington Univ. School of Medicine, Campus Box 8051, St. Louis, MO 63110, United States

Brown E.J.:
 Division of Infectious Diseases, Washington Univ. School of Medicine, Campus Box 8051, St. Louis, MO 63110, United States
ISSN: 00221767
Editorial
AMER ASSOC IMMUNOLOGISTS, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA, Estados Unidos America
Tipo de documento: Article
Volumen: 149 Número: 8
Páginas: 2759-2764
WOS Id: A1992JT98200032
ID de PubMed: 1401911