Ganglioside expression in tissues of mice lackingβ2-microglobulin

Abstract

SUMMARYThis study presents a comparative analysis of gangliosides from lymphoid (spleen and thymus) and other (brain, liver, lungs and muscle) tissues of C57BL/6 mice lacking the gene for b 2 -microglobulin (b 2 M), a constitutive component of the MHC class I molecule. Ganglioside fractions in the tissues of mice homozygous (b 2 M-/-) and heterozygous (b 2 M-/+) for the gene deletion were determined by high performance thin-layer chromatography (HPTLC), followed by immunostaining with specific polyclonal antibodies. Ubiquitous gangliosides G M3 (Neu5Ac) and G M3 (Neu5Gc) were the dominant gangliosides in the lungs of the control b 2 M-/+ mice, whereas the homozygous knockout mice had substantially decreased expression of these structures. The lungs of the b 2 M-/-mice also had reduced expression of T-lymphocyte-specific G M1b -type gangliosides (G M1b and GalNAc-G M1b ). b 2 M-deficient mice also had more G M1a and G D1a gangliosides in the liver, and several neolacto-series gangliosides were increased in the brain and lungs. This study provides in vivo evidence that the b 2 M molecule can influence the acquisition of a distinct ganglioside assembly in different mouse organs, implicating its non-immunological functions.

Analysis of fluorescently labeled glycosphingolipid-derived oligosaccharides following ceramide glycanase digestion and anthranilic acid labeling

“…This is comparable to that obtained previously, when using ceramide glycanase followed by 2-AB labeling, where 160 fmol of GSL-derived oligosaccharide was detected [4]. However, there are a number of other factors that can inXuence method sensitivity such as (a) substrate concentration (there is a lack of linearity above substrate concentrations of 150 M) [4], (b) amount of protein (typically 1 mg wet tissue equivalent is taken for GSL analysis but consistent results have been achieved with cellular protein amounts above 100 g) and (c) known diVerences in GSL expression when analyzing diVerent species and tissue samples [19][20][21][22].…”

Exogenous incorporation of neugc-rich mucin augments n-glycolyl sialic acid content and promotes malignant phenotype in mouse tumor cell lines

“…This enzyme is present in animals from the deuterostome lineage [ 18 ], which includes all higher mammals. The expression of this particular enzyme is the reason for NeuGc presence in most murine normal tissues [ 19 , 20 ]. In humans, an exon deletion/frameshift mutation in the CMAH gene renders the major pathway for NeuGc production non functional [ 21 ].…”

Expression of Neutral Glycosphingolipids in the Brain, Lymphoid Organs and Lungs of Mice Lacking β₂-Microglobulin

“…The brain of both groups of animals was negative for Gg3, Gg4 and Gb3 immunostaining. Abundant expression of Gg3, Gg4, and Gb3 was found in the lungs of control ␤ 2 M+/-mice, that mice with gene knockout for ␤ 2 M exhibit reduced expression of gangliosides in different tissues, including the brain and lymphoid organs [5] . In this study, we analyzed the expression of neutral GSLs in the brain as an immunologically privileged organ, in the thymus and spleen as primary and secondary lymphoid organs, respectively, and lungs as a common site of antigen entrance.…”