Types of oligosaccharide sulphation, depending on mucus glycoprotein source, corpus or antral, in rat stomach

Goso, Yukinobu; Hotta, Kyoko

doi:10.1042/bj2640805

Cited by 22 publications

(7 citation statements)

References 28 publications

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“…PGM34 extensively stained surface mucous cells in the fundic region, but only slightly stained pyloric gland cells (Figs 7Aa and 7Bb). In our previous study, we demonstrated that the 6‐sulfo H sequence is predominantly found on oligosaccharides of mucin present in the fundus region, whereas this sequence was only rarely found in the pyloric region [19]. Thus, this biochemical result is compatible with the immunohistochemical reactivity of PGM34 in the rat gastric section.…”

Section: Discussionsupporting

confidence: 77%

A monoclonal antibody, PGM34, against 6‐sulfated blood‐group H type 2 antigen, on the carbohydrate moiety of mucin

et al. 2007

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Mucin, a major component of mucus, is a highly O‐glycosylated, high‐molecular‐mass glycoprotein extensively involved in the physiology of gastrointestinal mucosa. To detect and characterize mucins derived from site‐specific mucous cells, we developed a monoclonal antibody, designated PGM34, by immunizing a mouse with purified pig gastric mucin. The reactivity of PGM34 with mucin was inhibited by periodate treatment of the mucin, but not by trypsin digestion. This suggests that PGM34 recognizes the carbohydrate portion of mucin. To determine the epitope, oligosaccharide‐alditols obtained from pig gastric mucin were fractionated by successive gel‐filtration, ion‐exchange, and normal‐phase HPLC, and tested for reactivity with PGM34. Two purified oligosaccharide‐alditols that reacted with PGM34 were obtained. Their structures were determined by NMR spectroscopy as Fucα1–2Galβ1–4GlcNAc(6SO3H)β1–6(Fucα1–2Galβ1–3)GalNAc‐ol and Fucα1–2Galβ1–4GlcNAc(6SO3H)β1–6(Galβ1–3)GalNAc‐ol. None of the defucosylated or desulfated forms of these oligosaccharides reacted with PGM34. Thus, the epitope of PGM34 was determined as the Fucα1–2Galβ1–4GlcNAc(6SO3H)β‐ sequence. Immunohistochemical examination of rat gastrointestinal tract showed that PGM34 stained surface mucous cells close to the generative cell zone in the gastric fundus and goblet cells in the small intestine, but only slightly stained antral mucous cells in the stomach. These data, taken together, show that PGM34 is a very useful tool for elucidating the role of mucins with characteristic sulfated oligosaccharides.

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Section: Discussionsupporting

confidence: 77%

A monoclonal antibody, PGM34, against 6‐sulfated blood‐group H type 2 antigen, on the carbohydrate moiety of mucin

et al. 2007

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“…A GlcNAc6ST activity was also found to be present in the Golgi fraction of rat stomach; this enzyme acts on rat gastric mucin to form a product characterized as 6-SO 4 -GlcNAcβ1-3Galβ1-3GalNAc [8]. 6-Sulphated GlcNAc has been found in all regions of the rat stomach [8,70]. GlcNAc6ST activity is also present in human respiratory mucosa [4], rat sublingual gland [71], rat colon and cells derived from the colon [58,60,71].…”

Section: Glcnac6stsmentioning

confidence: 97%

Sulphotransferases acting on mucin-type oligosaccharides

Brockhausen

2003

Biochemical Society Transactions

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This review summarizes the occurrence, properties and role in mucin O-glycosylation pathways of the various members of glycoprotein sulphotransferase families. Although a number of sulphotransferases have been cloned that act on mucin-type substrates in vitro, it is still difficult to determine exactly which enzymes are responsible for mucin sulphation in vivo. Sulphotransferases play a critical role in determining the chemical, physical and biological properties of mucins. Several of these enzymes have been shown to differ in expression and activity in cancer and inflammation.

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“…Moreover, the CCK-B/gastrin receptor was shown to be involved in this mechanism (7). In the previous study, mucins obtained from the corpus and antrum of rat gastric mucosa were shown to differ in the chemical composition of their carbo hydrate moieties and subunit structures (12,13). These results and an immunohistochemical observation (14) strongly indicate that there are different types of mucus producing cells in the corpus and antrum, and the regula tory mechanism on mucin biosynthesis might differ be tween these two types of cells.…”

Section: Z-300 N-[3-[3-(piperidinomethyl)phenoxy]propyl]-2mentioning

confidence: 82%

Effects of Z-300, a New Histamine H2-Receptor Antagonist, on Mucin Biosynthesis in Rat Gastric Mucosa.

et al. 1994

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ABSTRACT-We examined the effects of Z-300 (N-[3-[3-(piperidinomethyl)phenoxy]propyl]-2-(2-hydroxy ethyl-l-thio)acetamido• 2-(4-hydroxy benzoyl)benzoate), a newly-synthesized selective histamine H2-receptor antagonist, on mucin in rat gastric mucosa. Deep corpus mucin content increased significantly to 127% of the control after the administration of 30 mg/kg of Z-300, whereas that in the antral mucosa did not in crease. The addition of Z-300 significantly increased [3H]-labeled mucin in the corpus region. In the antrum, biosynthetic activity showed no significant change by 10-8-10-5 M of Z-300. These results suggest that Z 300 not only inhibits acid secretion but may also promote gastric mucus metabolism in the corpus region.

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Types of oligosaccharide sulphation, depending on mucus glycoprotein source, corpus or antral, in rat stomach

Cited by 22 publications

References 28 publications

A monoclonal antibody, PGM34, against 6‐sulfated blood‐group H type 2 antigen, on the carbohydrate moiety of mucin

A monoclonal antibody, PGM34, against 6‐sulfated blood‐group H type 2 antigen, on the carbohydrate moiety of mucin

Sulphotransferases acting on mucin-type oligosaccharides

Effects of Z-300, a New Histamine H2-Receptor Antagonist, on Mucin Biosynthesis in Rat Gastric Mucosa.

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