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• W1972601352 abstract "The previously demonstrated role of H-2 gene products in nonimmune cell interactions was further analyzed. As model of such interactions served the erythropoietic performance (in terms of 59Fe uptake) of bone marrow cell (BMC) inocula in the cellular environment of the spleen of massively irradiated hosts. When the performance in syngeneic hosts is taken as standard, the performance of cells from the same pool in H-2 disparate (congenic) hosts is subnormal. The inhibition was also observed in two congenic strain combinations where the H-2 disparity did not involve the I region. The capacity of BMC to distinguish H-2 -identical and H-2 -disparate hosts could be greatly reduced or virtually abolished by enzymatic digestion of certain cell surface carbohydrates. An essential effect of neuraminidase was further increased by emulsin. When the digested cells were left for 6 h in an enzyme-free medium, their capacity to dinstinguish H-2 disparities recovered. A pretreatment with papain, which cleaves a large fragment of the H-2 protein carrying both the antigenic site and the carbohydrate chain, had an effect comparable with but no greater than the sugar-removing enzymes. The enzymatic effect was largely due to the impairment of the performance of BMC in H-2 -identical hosts rather than to an improvement in H-2 -disparate ones. The neuraminidase- and emulsin-sensitive groupings thus seem to be essential for the cells to recognize “self” rather than “non-self” and to interact with H-2 -identical cells in physiological processes. A hypothesis is proposed that in H-2 glycoproteins, the antigenically and physiologically active sites are distinct, being located in the protein and carbohydrate parts of the molecules, respectively. It is further suggested that the normal function of the H-2 products might consist in providing the cell surface with structures which are complementary to similar structures on other cells; the carbohydrate moiety seems to be essential for this type of physiological interaction in contrast to the key and lock-type of complementarity in immune interactions which is based on protein structures." @default.
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• W1972601352 date "1977-02-01" @default.
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• W1972601352 title "Search for the physiological function of H-2 gene products" @default.
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• W1972601352 doi "https://doi.org/10.1002/eji.1830070203" @default.
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