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Loss of Sulfoglucuronyl and Other Neolactoglycolipids in Purkinje Cell Abnormality Murine Mutants
Author(s) -
Chou Denise K. H.,
Flores Sally,
Jungalwala Firoze B.
Publication year - 1990
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1990.tb01209.x
Subject(s) - purkinje cell , cerebellum , reeler , mutant , glycolipid , biology , biochemistry , microbiology and biotechnology , neuroscience , gene
A significant reduction in the content of two members of the sulfoglucuronyl‐neolacto series of glycolipids (SGGLs), 3‐sulfoglucuronyl‐lacto‐ N ‐neotetraosylceramide (SGGL‐1) and 3‐sulfoglucuronyl lacto‐ N ‐norhexaosylceramide (SGGL‐2), in the cerebellum of the Purkinje cell abnormality mutants, Purkinje cell degeneration ( pcd/pcd ), lurcher ( Lc /+), and staggerer ( sg/sg ), was also confirmed in the mildly affected nervous ( nr/nr ) mutant. The expression of SGGLs was studied during development of the pcd/pcd mutant cerebellum, and it was shown that the rate of decline in the level of SGGLs practically coincided with the loss of Purkinje cell perikarya. This indicated that SGGLs are primarily localized in Purkinje cells and that initially, at least, there is no genetic defect in the biosynthesis of SGGLs in the mutant. The precursors of SGGLs, viz., lacto‐ N ‐neotetraosylceramide (paragloboside) and lacto‐ N ‐norhexaosylceramide, as well as other glycolipids derived from these precursors, such as X‐determinant fucoglycolipids and disialosyllacto‐ N ‐neotetraosylceramide, were also present in normal cerebellum. Levels of paragloboside and its other derivatives, similar to SGGLs, were also significantly reduced in the Purkinje cell abnormality mutants pcd/pcd, sg/sg, Lc /+, and nr / nr but were normal in other cerebellar mutants, such as quaking ( qk / qk ), weaver ( wv / wv ), and reeler ( rl / rl ), where Purkinje cells are not involved. Thus, the entire paragloboside family of glycolipids is primarily associated with Purkinje cells in the cerebellum. Although levels of monoclonal antibody HNK‐1‐reactive glycolipids were reduced in the Purkinje cell abnormality mutants, HNK‐1‐reactive glycoproteins were not affected in these mutants.