| Literature DB >> 3817909 |
Abstract
The RT1.A (H-2K,D type) class I major histocompatibility complex (MHC) antigens of the rat are well recognized as membrane-bound glycoproteins. In this report, we demonstrate that liver and kidney in the DA rat strain contain large amounts of a water-soluble RT1.A class I molecule with a discrete heavy chain approximately 5 kd smaller than the membrane-bound form. An identical molecule could be identified in DA rat serum. This small class I molecule carries all of the polymorphic antigenic determinants of the RT1.A av1 class I molecule. The water-soluble molecule is readily denatured in its pure form when frozen and thawed, but this does not occur when it is mixed with serum, presumably because of a stabilizing interaction with one or more carrier proteins. The half-life of the class I molecule in serum was measured to be approximately 1.5 h. The LEW rat strain produced detectable but substantially smaller amounts of water-soluble RT1.A molecules. Our studies indicate that RT1.A class I MHC antigens are synthesized and presumably secreted in a smaller water-soluble form by liver, kidney, and possibly other tissues under physiological conditions, a point of considerable interest in view of the immunoregulatory functions of the membrane-bound forms of these molecules.Entities:
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Year: 1987 PMID: 3817909 DOI: 10.1007/bf00364273
Source DB: PubMed Journal: Immunogenetics ISSN: 0093-7711 Impact factor: 2.846