-transparent.png){kind=logo}
Gangliotriaosylceramide (Gg3Cer) was previously described as a tumor-associated antigen in murine L5178Y lymphoma [Young, W. W., Jr., and Hakomori, S., Science (Wash. D.C.), 211: 487-489, 1981]. This paper describes the major factors affecting the expression of Gg3Cer at the surface of various clones of L5178Y lymphoma. Of 26 sublines that were recloned, six cell lines showing different degrees of Gg3Cer expression at the cell surface were used for analysis of the glycolipid composition as related to its cell surface antigenicity. Three remarkable correlations between glycolipid composition and the antigenicity of Gg3Cer have been found: (a) high-expressor sublines were characterized by a large proportion of a unique molecular species of Gg3Cer having alpha-hydroxypalmitic acid in its ceramide moiety in striking contrast to low expressors which did not contain this molecular species; (b) low expressors contained a large quantity of ganglio-N-tetraosylceramide (Gg4Cer) and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc beta 1 leads to 4Gal beta 1 leads to 4Glc beta 1 leads to 1 Cer (GM1b) gangliosides, whereas these glycolipids were almost absent in high-expressor clones; and (c) nonexpressors, which were converted from the high expressors in vivo through immunotherapy with the monoclonal antibodies to Gg3Cer, contained a large quantity of ganglio-N-tetraosylceramide and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc beta 1 leads to 4Gal beta 1 leads to 4Glc beta 1 leads to 1Cer. The nonexpressors should have an induced enzyme system to metabolize Gg3Cer to ganglio-N-tetraosylceramide and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc beta 1 leads to 4Gal beta 1 leads to 4Glc beta 1 leads to 1Cer. Three factors, i.e., ceramide composition, coexisting glycolipids, and an antibody-dependent glycolipid change, are therefore important in determination of glycolipid antigenicity and antigen modulation by antibodies. The ceramide composition may affect glycolipid organization in membranes, and the coexisting glycolipid having a longer carbohydrate chain may mask the accessibility of antibody to the antigenic glycolipid. The antigenic modulation by the action of the antibody in vivo may be based on activation of a new glycosyltransferase.
R Kannagi, and
R Stroup, and
N A Cochran, and
D L Urdal, and
W W Young, and
S Hakomori
June 1991,
Ceskoslovenska patologie,
R Kannagi, and
R Stroup, and
N A Cochran, and
D L Urdal, and
W W Young, and
S Hakomori
November 1986,
Biochemistry,
R Kannagi, and
R Stroup, and
N A Cochran, and
D L Urdal, and
W W Young, and
S Hakomori
January 1979,
Journal of immunology (Baltimore, Md. : 1950),
R Kannagi, and
R Stroup, and
N A Cochran, and
D L Urdal, and
W W Young, and
S Hakomori
March 1970,
Journal of lipid research,
R Kannagi, and
R Stroup, and
N A Cochran, and
D L Urdal, and
W W Young, and
S Hakomori
September 1993,
The Histochemical journal,
R Kannagi, and
R Stroup, and
N A Cochran, and
D L Urdal, and
W W Young, and
S Hakomori
October 1961,
Cancer research,
R Kannagi, and
R Stroup, and
N A Cochran, and
D L Urdal, and
W W Young, and
S Hakomori
January 1971,
Immunology,
R Kannagi, and
R Stroup, and
N A Cochran, and
D L Urdal, and
W W Young, and
S Hakomori
June 1985,
Cancer research,
R Kannagi, and
R Stroup, and
N A Cochran, and
D L Urdal, and
W W Young, and
S Hakomori
October 1967,
Journal of bacteriology,
R Kannagi, and
R Stroup, and
N A Cochran, and
D L Urdal, and
W W Young, and
S Hakomori
January 1980,
Archivos de investigacion medica,
