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By Dina Beverly

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Sample text

Another perplexing aspect of the /32-microglobulin association of CD1 proteins has recently been demonstrated by a report of P2microglobulin-independent expression of the human C D l d protein by intestinal epithelial cells. Immunoprecipitations from lysates of ‘=I-labeled normal colonic epithelial cells performed with these mAbs, or with a mAb raised against a bacterial fusion protein constructed from the human C D l d cDNA sequence (Bilsland and Milstein, 1991), revealed a 100-kDa band under nonreducing conditions and a single 37-kDa band after reduction.

1987a). In similar fashion, two separate epitopes have been defined on the C D l b molecule, whereas the four anti-CDlc mAbs so far examined in this fashion appear to bind to the same or overlapping epitopes (Amiot et al. 1986, 1987b; Favaloro et al. 1987a). The relationship of these serologic epitopes to the protein structure of CD1 is currently unknown. , 1989). This variable reactivity with trypsin-cleaved CDla further underscores the heterogeneity of anti-CDla mAbs and may be of practical significance when these antibodies are used to examine cells isolated from trypsin-treated tissues or cell monolayers.

ASSOCIATIONOF CD1 HEAVYCHAINS WITH P2-MICROGLOBULIN The association of CD1 heavy chains with P2-microglobulin is a distinctive structural feature of these proteins. The ability of cellular proteins to associate with P2-microglobulin is apparently limited to a relatively small group of proteins, all of which appear to have functions related to the immune system. Initially, P2-microglobulin binding was believed to be restricted only to MHC class I proteins. However, CD1 and two other proteins are now known to be exceptions to this rule.

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