Degeneration of Duodenal Glands in the Cat

doi:10.1086/277596

Duodenal Glands of the Pony (Equus caballus)

Anatomia Histologia Embryologia ◽

10.1111/j.1439-0264.1991.tb00285.x ◽

1991 ◽

Vol 20 (1) ◽

pp. 1-9 ◽

Cited By ~ 5

Author(s):

K. Takehana ◽

J. Masty ◽

M. Abe ◽

M. Yamaguchi

Keyword(s):

Equus Caballus ◽

Duodenal Glands

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Histochemistry of the duodenal glands of the cat and horse

Cells Tissues Organs ◽

10.1159/000144575 ◽

1976 ◽

Vol 94 (3) ◽

pp. 449-456 ◽

Cited By ~ 9

Author(s):

D. Oduor-Okelo

Keyword(s):

Duodenal Glands

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Different Forms of TFF2, A Lectin of the Human Gastric Mucus Barrier: In Vitro Binding Studies

International Journal of Molecular Sciences ◽

10.3390/ijms20235871 ◽

2019 ◽

Vol 20 (23) ◽

pp. 5871 ◽

Cited By ~ 10

Author(s):

Franziska Heuer ◽

René Stürmer ◽

Jörn Heuer ◽

Thomas Kalinski ◽

Antje Lemke ◽

...

Keyword(s):

Molecular Mass ◽

Gastric Mucus ◽

Binding Studies ◽

Binding Characteristics ◽

Duodenal Glands ◽

Vitro Binding ◽

Trefoil Factor Family ◽

Mucus Barrier ◽

Mass Form

Trefoil factor family 2 (TFF2) and the mucin MUC6 are co-secreted from human gastric and duodenal glands. TFF2 binds MUC6 as a lectin and is a constituent of the gastric mucus. Herein, we investigated human gastric extracts by FPLC and identified mainly high- but also low-molecular-mass forms of TFF2. From the high-molecular-mass forms, TFF2 can be completely released by boiling in SDS or by harsh denaturing extraction. The low-molecular-mass form representing monomeric TFF2 can be washed out in part from gastric mucosa specimens with buffer. Overlay assays with radioactively labeled TFF2 revealed binding to the mucin MUC6 and not MUC5AC. This binding is modulated by Ca2+ and can be blocked by the lectin GSA-II and the monoclonal antibody HIK1083. TFF2 binding was also inhibited by Me-β-Gal, but not the α anomer. Thus, both the α1,4GlcNAc as well as the juxtaperipheral β-galactoside residues of the characteristic GlcNAcα1→4Galβ1→R moiety of human MUC6 are essential for TFF2 binding. Furthermore, there are major differences in the TFF2 binding characteristics when human is compared with the porcine system. Taken together, TFF2 appears to fulfill an important role in stabilizing the inner insoluble gastric mucus barrier layer, particularly by its binding to the mucin MUC6.

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The Duodenal Glands of Brunner in Man, Their Distribution and Quantity: An Anatomical Study.

Archives of Internal Medicine ◽

10.1001/archinte.1947.00220110127012 ◽

1947 ◽

Vol 79 (5) ◽

pp. 587

Keyword(s):

Anatomical Study ◽

Duodenal Glands

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Isolation and partial characterization of rat duodenal-gland (Brunner's-gland) mucus glycoprotein

Biochemical Journal ◽

10.1042/bj2030779 ◽

1982 ◽

Vol 203 (3) ◽

pp. 779-785 ◽

Cited By ~ 10

Author(s):

H L Smits ◽

P J M van Kerkhof ◽

M F Kramer

Keyword(s):

Small Intestine ◽

Chemical Composition ◽

Protein Content ◽

Density Gradient Centrifugation ◽

Gradient Centrifugation ◽

Mucous Cells ◽

Present Evidence ◽

Mucus Glycoprotein ◽

Duodenal Glands

A mucus glycoprotein was isolated from the duodenal glands of the rat and purified by repeated density-gradient centrifugation. The characterized glycoprotein is unique to the mucous cells of the duodenal glands and is not present in parts of the small intestine devoid of these glands. The chemical composition of the purified glycoprotein is characteristic for glycoproteins of the mucin-type. Its protein content is relatively high and amount to 35% by weight. No neuraminic acid and little sulphate (2%) is present. Evidence is presented that the native glycoprotein is built up from subunits held together via disulphide bridges in a non-glycosylated region of the protein core.

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