Cloning and comparative sequence analysis of the gene encoding canine intercellular adhesion molecule-1 (ICAM-1)

Canine intercellular adhesion molecule-1 (ICAM-1) plays a primary role in the adherence of canine neutrophils to endothelial cells and in the cytotoxicity of canine neutrophils for adult cardiac myocytes. We have cloned the canine ICAM-1 gene and have analyzed the conservation of ICAM-1 amino acid (...

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Veröffentlicht in:Gene 1995-04, Vol.156 (2), p.291-295
Hauptverfasser: Manning, Anthony M., Lu, Hui-Fang, Kukielka, Gilbert L., Oliver, Mary G., Ty, Theresa, Toman, Carol A., Drong, Roger F., Slightom, Jerry L., Ballantyne, Christie M., Entman, Mark L., Smith, C.Wayne, Anderson, Donald C.
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Sprache:eng
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Zusammenfassung:Canine intercellular adhesion molecule-1 (ICAM-1) plays a primary role in the adherence of canine neutrophils to endothelial cells and in the cytotoxicity of canine neutrophils for adult cardiac myocytes. We have cloned the canine ICAM-1 gene and have analyzed the conservation of ICAM-1 amino acid (aa) sequences in man, chimpanzee, mouse, rat and dog. Canine ICAM-1 displays 61% identity with human ICAM-1. Cys residues critical to the immunoglobulin (Ig) fold structure and four sites of N-linked glycosylation are absolutely conserved in ICAM-1 from all species. Residues in the cytoplasmic tail associated with cytoskeletal α-actinin binding are highly conserved, supporting the hypothesis that intracellular attachment is indeed important for ICAM-1 function. Residues critical for human ICAM-1 binding to the β 2-integrin leukocyte-function-associated antigen 1 (LFA-1) are highly conserved between all species, whereas those residues demonstrated to play an important role in interaction of human ICAM-1 with macrophage activation complex 1 (Mac-1) are not highly conserved. Residues critical for ICAM-1 binding to rhinovirus and malaria-infected red blood cells (IRBC) are not highly conserved.
ISSN:0378-1119
1879-0038
DOI:10.1016/0378-1119(95)00045-8