Identification of swine and primate cellular adhesion molecules (CAM) using mouse anti‐human monoclonal antibodies
1995; Wiley; Volume: 2; Issue: 2 Linguagem: Inglês
10.1111/j.1399-3089.1995.tb00071.x
ISSN1399-3089
AutoresMakiko Kumagai‐Braesch, Bernioe Schacter, Zengmin Yan, James Michaelson, Scott Arn, Mary D. Smith, Mary E. White‐Scharf, Rodney L. Monroy, David H. Sachs, James T. Kurnick,
Tópico(s)T-cell and B-cell Immunology
ResumoAbstract: A series of adhesion molecules of swine and Cynomolgus monkeys were identified by screening for cross‐reactivity with a panel of monoclonal murine anti‐human adhesion molecule antibodies obtained from the 5th International Workshop and Conference on Human Leukocyte Differentiation Antigens (Boston, MA, USA, 1993). Of 162 antibodies tested, 25 were found that cross‐react significantly with swine cells, while 67 were found to react strongly with cells of Cynomolgus monkeys. Cross reactivities to swine were found with antibodies to CD 18 (β2 integrin), CD29 (β1 integrin), β7 integrin, CD49d (α4 integrin) CD49b(α2 integrin), and to a lesser extent to CD62p(P‐selectin), CD62L(L‐selectin), CD102(ICAM‐2), CD11b, and CD49c (α3 integrin). Cross‐reactivities to primate cells also included CD18, CD29, CD49d, and CD49b. In addition, reactivities to Cynomolgus monkey cells were detected with antibodies to CD11 (a, b, and c), CD31, CD44, CD49e, CD49f, CD50, CD54, CD56, CD62p, CD 102 and CD56. The tissue distribution and molecular weight of the swine antigens are similar to their human counterparts. These findings provide a spectrum of monoclonal antibodies that react with shared epitopes on homologous adhesion molecules of human, swine, and monkey cells, thus facilitating study of the role of these molecules in the immunobiology of monkeys and swine. These reagents may be useful to dissect the role of adhesion molecules in both alio‐ and xenoreactivity.
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