Histochemical analysis of rat testicular glycoconjugates. 2. ?-galactosyl residues in O- and N-linked glycans in seminiferous tubules

Jones, Carolyn J.P.; Morrison, Christopher A.; Stoddart, R. W.

doi:10.1007/bf01046164

Cited by 46 publications

(28 citation statements)

References 15 publications

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“…Although dramatic changes to carbohydrate structures during the development of testicular cells were suggested by histological analysis using a series of lectins (24), it is very difficult to determine the precise structure of such carbohydrates. In order to detect whether the GalNAc␤1-3GlcNAc structure exists or not, a tool is needed for probing such a structure.…”

Section: Discussionmentioning

confidence: 99%

A Novel Human β1,3-N-Acetylgalactosaminyltransferase That Synthesizes a Unique Carbohydrate Structure, GalNAcβ1-3GlcNAc

Hiruma

Togayachi

Okamura

et al. 2004

Journal of Biological Chemistry

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We found, using a BLAST search, a novel human gene (GenBank TM accession number BC029564) that possesses ␤3-glycosyltransferase motifs. The full-length open reading frame consists of 500 amino acids and encodes a typical type II membrane protein. This enzyme has a domain containing ␤1,3-glycosyltransferase motifs, which are widely conserved in the ␤1,3-galactosyltransferase and ␤1,3-N-acetylglucosaminyltransferase families. The putative catalytic domain was expressed in human embryonic kidney 293T cells as a soluble protein. Its N-acetylgalactosaminyltransferase activity was observed when N-acetylglucosamine (GlcNAc) ␤1-O-benzyl was used as an acceptor substrate. The enzyme product was determined to have a ␤1,3-linkage by NMR spectroscopic analysis, and was therefore named ␤1,3-Nacetylgalactosaminyltransferase-II (␤3GalNAc-T2). The acceptor substrate specificity of ␤3GalNAc-T2 was examined using various oligosaccharide substrates. Gal-␤1-3(GlcNAc␤1-6)GalNAc␣1-O-para-nitrophenyl (core 2-pNP) was the best acceptor substrate for ␤3GalNAc-T2, followed by GlcNAc␤1-4GlcNAc␤1-O-benzyl, and GlcNAc␤1-6GalNAc␣1-O-para-nitrophenyl (core 6-pNP), among the tested oligosaccharide substrates. Quantitative real time PCR analysis revealed that the ␤3Gal-NAc-T2 transcripts was restricted in its distribution mainly to the testis, adipose tissue, skeletal muscle, and ovary. Its putative orthologous gene, m␤3GalNAc-T2, was also found in a data base of mouse expressed sequence tags. In situ hybridization analysis with mouse testis showed that the transcripts are expressed in germ line cells. ␤3GalNAc-T2 efficiently transferred GalNAc to N-glycans of fetal calf fetuin, which was treated with neuraminidase and ␤-galactosidase. However, it showed no activity toward any glycolipid examined. Although the GalNAc␤1-3GlcNAc␤1-R structure has not been reported in humans or other mammals, we have discovered a novel human glycosyltransferase producing this structure on N-and O-glycans.

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Section: Discussionmentioning

confidence: 99%

A Novel Human β1,3-N-Acetylgalactosaminyltransferase That Synthesizes a Unique Carbohydrate Structure, GalNAcβ1-3GlcNAc

Hiruma

Togayachi

Okamura

et al. 2004

Journal of Biological Chemistry

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“…Both O-and N-glycans can occur in the same glycoprotein. In the rat testis it has been demonstrated that both types of glycoconjugate are present (Martlnez-Menfirguez et al, 1993;Jones et al, 1993), but no information is available for the epididymis. Many methods have been employed to determine the type of glycoconjugate present; for example, use has been made of ]3-elimination (which cleaves the O-glycoconjugates) in combination with 0018-2214 9 1995 Chapman & Hall lectins.…”

Section: Introductionmentioning

confidence: 96%

Histochemical study of glycoconjugates in the epididymis of the hamster (Mesocricetus auratus)

et al. 1995

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The glycoconjugates of hamster epididymis were investigated with conventional and lectin histochemistry. A zone of the caput epididymis, with particular histochemical characteristics, has been differentiated. beta-Elimination in combination with lectins was used to establish the presence and distribution of N- and O-linked glycoconjugates. The epithelium, spermatozoa and the intertubular matrix were rich in glycoconjugates. The Golgi apparatus and stereocilia of the principal cells were intensely positive with HPA, PNA and SBA lectins. beta-Elimination indicated that these cells contained abundant O-linked glycoconjugates. Apical and clear cells presented a common lectin affinity; their reactivities towards WGA and UEA-I were very positive. These cells probably contain abundant N-glycoconjugates. The spermatozoa were stained by periodic acid-Schiff (PAS) and by all the lectins (especially in the acrosome), except by those with an affinity for alpha-L-fucosyl residues; the most intense reaction was found with HPA, WGA, PNA and SBA. Changes in the sperm lectin binding along the ductus were observed: sperm flagellum abruptly acquired WGA and PNA labelling from the posterior caput, and HPA reactivity was negative only in the zone between the caput and the corpus.

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“…Cells Tissues Organs 2007;185: [269][270][271][272][273][274][275][276][277][278][279][280][281][282][283][284] 271 SBA, SNA-1, MAA, PAA and WGA were also exposed to neuraminidase (0.1 units/ml, type VI from Clostridium perfringens , Sigma) [Jones et al, 1992] for 2 h at 37 ° C before incubation in the lectin to cleave off terminal sialic acid. Comments on the results of pretreatment with neuraminidase will be restricted to those which showed a clear effect.…”

Section: Glycosylation Of Hemomonochorial Placentaementioning

confidence: 99%

Glycosylation at the Fetomaternal Interface in Hemomonochorial Placentae from Five Widely Separated Species of Mammal: Is There Evidence for Convergent Evolution?

Jones

Carter

Aplin

et al. 2007

Cells Tissues Organs

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Hemomonochorial placentation occurs in diverse species. We have examined placental glycosylation in five widely separated mammals with this type of placentation – lesser hedgehog tenrec (Echinops telfairi), spotted hyena (Crocuta crocuta), nine-banded armadillo (Dasypus novemcinctus), human (Homo sapiens) and guinea pig (Cavia porcellus) – in order to assess whether evolutionary convergence to the hemomonochorial state is accompanied by a similar convergence of glycan expression. Placentae from 2 E. telfairi, 3 C. crocuta, 1 D. novemcinctus, 4 womenand 1 C. porcellus were fixed and processed into epoxy resin. Binding of twenty-three lectins was assessed using a semiquantitative ranking system. The trophoblast apical/microvillous membrane of all five species showed marked similarities in glycosylation. In the N-linked series, there were abundant bi/tri-antennary complex chains, while the non-bisected variants were much scarcer. All species had plentiful N-acetyl lactosamine sequences; at chain termini, binding to Galβ1,4GlcNAc and Galβ1,3GalNAc sequences was greatly enhanced after neuraminidase treatment. In all species, terminal NeuNAcα2,3 residues were detected. The tenrec had unusually abundant terminal N-acetyl galactosamine. The basal plasma membrane/basal lamina showed glycosylation patterns distinct from the microvillous membrane in each case, indicating chemical diversity of the two opposite faces of trophoblast. Similar classes of glycan at the hemochorial interface suggest conservation of function. The observed lectin binding patterns suggest broad similarities of glycosylation that may have arisen by convergent evolution.

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Histochemical analysis of rat testicular glycoconjugates. 2. ?-galactosyl residues in O- and N-linked glycans in seminiferous tubules

Cited by 46 publications

References 15 publications

A Novel Human β1,3-N-Acetylgalactosaminyltransferase That Synthesizes a Unique Carbohydrate Structure, GalNAcβ1-3GlcNAc

A Novel Human β1,3-N-Acetylgalactosaminyltransferase That Synthesizes a Unique Carbohydrate Structure, GalNAcβ1-3GlcNAc

Histochemical study of glycoconjugates in the epididymis of the hamster (Mesocricetus auratus)

Glycosylation at the Fetomaternal Interface in Hemomonochorial Placentae from Five Widely Separated Species of Mammal: Is There Evidence for Convergent Evolution?

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