Search PubMed⌕ Search

Biomedical subjects

D N Misra

Publications and source records attributed to D N Misra.

84 records · Page 5Linked to original sources
PubMedDate not supplied

Major histocompatibility complex class I antigens expressed on rat trophoblast cells.

There is controversy about the size of the major histocompatibility complex antigens of trophoblast cells from placenta. There are some reports that the heavy chains of these molecules are smaller (39-43 kd) than those of the classical class I antigens (45-46 kd), while there are others which show that both the light and the heavy forms of class I antigens occur in the trophoblast cells. In order to investigate this problem, we studied the classical class I antigen (RT1.Aa) and the pregnancy-associated class I antigen (Pa) of the rat from 125I-labeled basal trophoblast cells, isolated from the placenta of WF females pregnant by DA males, using very mild conditions. These antigens were compared with those of the syngeneic (DA x DA) trophoblast cells or paternal (DA) lymphocytes by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both the Aa and Pa antigens, precipitated from the two trophoblast preparations, showed a heavy chain of 46 kd associated with a 12 kd beta 2-microglobulin component, as did the same molecules precipitated from the lymphocytes. Heavy chains in the range of 39-43 kd could not be detected in any of the samples. The results suggest that the smaller molecular weight heavy chains are methodological artifacts and could arise from loss of a glycan(s) during isolation.

Animals↗
PubMedDate not supplied

Biochemical analysis of the rat MHC class I antigens RT1.Aa, RT1.Fa and Pa.

In DA strain rats, there are two other MHC class I loci (Pa and RT1.Fa) in the vicinity of the classical class I locus RT1.Aa. The Pa antigen is the pregnancy-associated antigen, and it was detected by antibodies elicited in WF females pregnant by DA males without any other immunization. The Fa antigen was detected by a monoclonal antibody raised by alloimmunization. In the present work, the Aa, Fa and the Pa antigens have been compared by HPLC peptide mapping and by isoelectric focusing after their isolation by appropriate monoclonal antibodies. All the three antigens are identical in primary structure with respect to lysine, methionine, asparagine and the aromatic amino acid residues, but they differ from one another with respect to glutamic acid and/or aspartic acid residues. The pI values of the antigens differ slightly. All three antigens have two identical N-linked glycans, but the Fa antigen has an additional N-linked glycan. Based on the available amino acid sequence of the Pa antigen, it can be concluded that both Aa and Pa antigens are devoid of glycosylation in the second domain. This lack of glycosylation of the classical antigen Aa is unique for the rat, since classical class I antigens of the mouse show glycosylation in the first and second, and sometimes in the third domain, and those in the human, in the first domain only. The high degree of similarity among the Aa, Fa, and Pa molecules that this study indicates is also unique for the rat, since antigens encoded by different class I genes of the same haplotype are quite disparate in the mouse and human.

Animals↗