BIOSYNTHESIS AND MATURATION OF THE LYT-2/3 MOLECULAR-COMPLEX IN MOUSE THYMOCYTES

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  • 1 January 1985
    • journal article
    • research article
    • Vol. 135  (3) , 1937-1944
Abstract
The biosynthesis and maturation of the 3 subunits .alpha. (MW = 37,000), .beta. (MW = 32,000), and .gamma. (MW = 27,000) of the mouse Lyt-2/3 antigenic complex have been studied by using 2 monoclonal antibodies directed against a monomorphic determinant of the Lyt-2 antigen. Short time-pulse labeling of thymocytes reveals 3 different high mannose intermediates that give rise upon endo-.beta.-N-acetyl-glucosaminidase H digestion to 3 distinct precursor polypeptides of MW = 22,000 (.alpha.p), MW = 18,000 (.beta.p), and MW = 19,500 (.gamma.p). Pulse-chase analysis indicates rapid posttranslational processing, because mature forms already appear after 10 min of chase. The half-life of the endo-H-sensitive early forms are in the range of 20-30 min. Both the .alpha. and .beta. subunits are suggested to contain 3 N-asparagine-linked oligosaccharides, one of which is of the high mannose type. The .gamma.-chain contains only one such glycan unit of the complex type. The results presented show that all 3 chains undergo additional posttranslational modifications. Finally, the data suggest that the cytoplasmic domains of these chains are of different size.

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