Structures and functions of the sugar chains of glycoproteins

Kobata, Akira

doi:10.1007/978-3-642-78046-2_17

Cited by 25 publications

(35 citation statements)

References 131 publications

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“…It is known that glycoproteins with very similar individual monosaccharides content may vary in glycosylation patterns [27,28]. Therefore, we examined the reactivity of the urinary glycoproteins with specific lectins using an ELISA.…”

Section: Reactivity With Lectinsmentioning

confidence: 99%

Tamm–Horsfall protein isolated from urine of pregnant and non‐pregnant women has similar oligosaccharides

Olczak

Kubicz

Kokot

et al. 1998

Eur J Clin Investigation

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Section: Reactivity With Lectinsmentioning

confidence: 99%

Tamm–Horsfall protein isolated from urine of pregnant and non‐pregnant women has similar oligosaccharides

Olczak

Kubicz

Kokot

et al. 1998

Eur J Clin Investigation

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“…More importantly, it is possible that the hyaluronidase activity in cells from non-testicular origin may be lower than that of the testis due to differences in the pattern of glycosylation. Variations in glycosylation patterns have been shown to exist among tissues [31] and glycosylation levels have been reported to influence hyaluronidase activity of SPAM1 in the mouse and horse [10,32]. Note that in the mouse, tissue differences in glycosylation patterns have been reported for the testis and epididymis [33].…”

Section: Discussionmentioning

confidence: 99%

SPAM1 (PH-20) protein and mRNA expression in the epididymides of humans and macaques: utilizing laser microdissection/RT-PCR

Evans

Zhang

Martin‐DeLeon

2003

Reprod Biol Endocrinol

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BackgroundThe Sperm Adhesion Molecule 1 (SPAM1) is an important sperm surface hyaluronidase with at least three functions in mammalian fertilization. Previously our laboratory reported that in the mouse, in addition to its expression in the testis, Spam1 is synthesized in the epididymis where it is found in membranous vesicles in the principal cells of the epithelium in all three regions. Since SPAM1 is widely conserved among mammals the aim of the study was to determine if its expression pattern in the epididymis is conserved in rodents and primates.MethodsWe used laser microdissection (LM)/RT-PCR on frozen and paraffin-embedded epididymal sections of humans (n = 3) and macaques (n = 2) as well as in situ transcript hybridization to determine if transcripts are present in the epididymal epithelium. Western analysis and immunohistochemistry were used to detect and confirm the protein expression, and hyaluronic acid substrate gel electrophoresis analyzed its hyaluronidase activity. An in silico analysis of the proximal promoter of SPAM1 was also performed to identify relevant putative transcription binding sites for the androgen receptor.ResultsWe demonstrate that mRNA unique to SPAM1 is present in the principal cells of the epididymal epithelium in all individuals of both species studied. SPAM1 protein is present in all three regions of the epididymis, as well as the vas deferens, and is localized similarly to the transcripts. SPAM1 was shown to have hyaluronidase activity at pH 7.0. In the proximal promoter of SPAM1 were uncovered putative epididymal transcription factor binding sites including androgen receptor elements (AREs), consistent with epididymal expression.ConclusionsThese findings allow us to conclude that epididymal SPAM1 is conserved in at least two mammalian classes, rodents and primates. This conservation of expression suggests that the protein is likely to play an important function, possibly in sperm maturation.

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“…Glycans that are covalently attached to proteins can modulate protein properties such as folding, activity, stability, trafficking, and recognition [1]. These functions are known to be important to multicellular organisms, which require highly organized intercellular interactions, and therefore the expression of incomplete or modified glycans often leads to embryonic death or congenital disease [2,3].…”

Section: Introductionmentioning

confidence: 99%

TbGT8 is a bifunctional glycosyltransferase that elaborates N-linked glycans on a protein phosphatase AcP115 and a GPI-anchor modifying glycan in Trypanosoma brucei

Nakanishi¹,

Karasudani²,

Shiraishi³

et al. 2014

Parasitology International

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The procyclic form of Trypanosoma brucei expresses procyclin surface glycoproteins with unusual glycosylphosphatidylinositol-anchor side chain structures that contain branched N-acetyllactosamine and lacto-N-biose units. The glycosyltransferase TbGT8 is involved in the synthesis of the branched side chain through its UDP-GlcNAc: βGal β1-3N-acetylglucosaminyltransferase activity. Here, we explored the role of TbGT8 in the mammalian bloodstream form of the parasite with a tetracycline-inducible conditional null T. brucei mutant for TbGT8. Under non-permissive conditions, the mutant showed significantly reduced binding to tomato lectin, which recognizes poly-N-acetyllactosamine-containing glycans. Lectin pull-down assays revealed differences between the wild type and TbGT8 null-mutant T. brucei, notably the absence of a broad protein band with an approximate molecular weight of 110 kDa in the mutant lysate. Proteomic analysis revealed that the band contained several glycoproteins, including the acidic ecto-protein phosphatase AcP115, a stage-specific glycoprotein in the bloodstream form of T. brucei. Western blotting with an anti-AcP115 antibody revealed that AcP115 was approximately 10 kDa smaller in the mutant. Enzymatic de-N-glycosylation demonstrated that the underlying protein cores were the same, suggesting that the 10-kDa difference was due to differences in N-linked glycans. Immunofluorescence microscopy revealed the colocalization of hemagglutinin epitope-tagged TbGT8 and the Golgi-associated protein GRASP. These data suggest that TbGT8 is involved in the construction of complex poly-N-acetyllactosamine-containing type N-linked and GPI-linked glycans in the Golgi of the bloodstream and procyclic parasite forms, respectively.

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Structures and functions of the sugar chains of glycoproteins

Cited by 25 publications

References 131 publications

Tamm–Horsfall protein isolated from urine of pregnant and non‐pregnant women has similar oligosaccharides

Tamm–Horsfall protein isolated from urine of pregnant and non‐pregnant women has similar oligosaccharides

SPAM1 (PH-20) protein and mRNA expression in the epididymides of humans and macaques: utilizing laser microdissection/RT-PCR

TbGT8 is a bifunctional glycosyltransferase that elaborates N-linked glycans on a protein phosphatase AcP115 and a GPI-anchor modifying glycan in Trypanosoma brucei

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