A Study of Acidic Glycosaminoglycans in Human Gastric Tissue

Sekino, Takafumi; Murata, Katsumi; Saito, Yasuhiro; Tsubura, K.

doi:10.1159/000198052

Cited by 16 publications

(16 citation statements)

References 14 publications

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“…It shows that the pre dominant AGAG in the kidney tissue mi grated like the standard HS. In calcium acetate buffer, the specific globe-like shape of HA was clearly detected in the kidney AGAG of agedsubjects as had been detected in human gastric tissue [18], The intermediated spot correspond ing to the standard DS was also found. Fastmoving spots corresponding to the standard C-4S and C-6S were stained rather faintly.…”

Section: Resultssupporting

confidence: 59%

Age-Dependent Distribution of Acidic Glycosaminoglycans in Human Kidney Tissue

Murata¹,

Horiuchi²

1978

Nephron

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Acidic glycosaminoglycans (AGAG) of human kidneys prepared from subjects of different ages were purified and determined by an enzymic assay with chondroitinases. The resulting disaccharide units and the undigested AGAG after digesting with the enzymes were identified by paper chromatography, electrophoresis and thin-layer chromatography. The age-dependent changes were: heparan sulfates accounted for 43–74% of total AGAG and the proportion to total AGAG appeared to decrease with advancing age. Dermatan sulfate remained without change. The proportion of hyaluronic acid appeared to decrease at 19–21 years and increased again with aging. The ratio of the 4-type chondroitin sulfate to the 6-type decreased with advancing age.

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Section: Resultssupporting

confidence: 59%

Age-Dependent Distribution of Acidic Glycosaminoglycans in Human Kidney Tissue

Murata¹,

Horiuchi²

1978

Nephron

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“…These proteo-DSs ranged in molecular size from 80,000 to 285,000, and were classified as small PGs. However, there have been few studies on proteo-DS from gastrointestinal tract regions possessing elasticity (Sekino et al 1977;Sekino and Murata 1978). In this study, the molecular size of proteo-DS from the gastrointestinal tract was estimated to be more than 8 X 105.…”

Section: Discussionmentioning

confidence: 80%

“…The main component of PGs in the gastrointestinal tract is proteodermatan sulfate (proteo-DS) (Sekino et al 1977; Sekino and Murata 1978;Iozzo et al 1982; Nagai et al 1985). However, only limited details of the chemical nature and physiological function of proteo-DS in the gastrointestinal tract are available (Sekino et al 1977; Sekino and Murata 1978).…”

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confidence: 99%

Comparative Studies on Proteodermatan Sulfate of Bovine Gastrointestinal Tract.

Kawasaki

1993

Tohoku J. Exp. Med.

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KAWASAKI, H. Comparative Studies on Proteodermatan Sulfate of BovineGastrointestinal Tract. Tohoku J. Exp. Med., 1993, 171(3), 255-266 Proteodermatan sulfate was extracted from four areas of the bovine gastrointestinal tract (esophagus, stomach, small intestine and colon) with 4 M guanidine-HC1 and then purified by ion-exchange and gel filtration chromatography. Dermatan sulfate chains which made up proteodermatan sulfate from each area were separately prepared by Pronase P and endo-f3-xylosidase digestion. The properties of the proteodermatan sulfate and dermatan sulfate chains were compared using electrophoresis and high-performance liquid chromatography. The molecular size of proteodermatan sulfate purified from each area was estimated to be greater than 8 X 105, and the molecular sizes of dermatan sulfate chains from esophagus, stomach, small intestine, and colon were 27,000, 24,500, 21,000, and 21,500, respectively. The dermatan sulfate chains from the esophagus were slightly undersulfated in comparison with the others. These results show that the molecular sizes of proteodermatan sulfate from different regions of the gastrointestinal tract are similar to each other, but are larger than those from other tissues. Dermatan sulfate chains differed from each other to a slight degree with respect to chain length and sulfation, that from the esophagus being the largest. These differences in proteodermatan sulfate structure seem to reflect the organ specificities of the gastrointestinal tract.bovine gastrointestinal tract; proteodermatan sulfate; endo-/3-xylosidase; extracellular matrix; glycosaminoglycan Proteoglycans (PGs) are important structural macromolecules in the extracellular matrix (Antonopoulos et al. 1974;Vogel and Fisher 1986). Interest in PGs

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“…The preparation and analysis of GAGs were carried out as described in the literature [4,5,8,[13][14][15]. The tissues, 1.98 g mean wet tissue weight, were cut with scissors in pieces (3 mm3) and imme diately boiled to inactivate any endogenous enzymatic activity.…”

Section: Samplesmentioning

confidence: 99%

Glycosaminoglycan Components in Duodenum with Advancing Age and in Patients with Progressive Systemic Sclerosis

Murata¹,

Sekino

Ikeda

et al. 1995

Digestion

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The glycosaminoglycan (GAG) components in normal human duodenal tissue and in duodenal GAGs of patients with progressive systemic sclerosis (PSS) were characterized at the macromolecular level by electrophoresis combined with various GAG-specific digestion. High-performance liquid chromatographic assay quantified various unsaturated disaccharides derived from chondroitin sulfate and dermatan sulfate isomers (DS). The data obtained showed that on average, the total GAG content was 1.02 mg as uronic acid/g dry tissue weight, and the main GAGs were DS (33% of total GAGs), and heparan sulfates (HS, 27%), followed by hyaluronic acid (HA, 14%) and over-sulfated DS (10%), and small amounts of chondroitin, chondroitin-4- and -6-sulfates (C-4S and C-6S, totally 16%). With advancing age, the proportion of DS, HS and oversulfated DS increased, while HA, chondroitin and C-4S decreased. The composition of duodenal GAGs in PSS patients was similar to that in the aged: a higher proportion of DS isomers and HS and a lower proportion of HA and chondroitin. As the structure of sulfated GAGs differs with advancing age and in patients with PSS, GAGs may have a role in duodenal function and metabolism.

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A Study of Acidic Glycosaminoglycans in Human Gastric Tissue

Cited by 16 publications

References 14 publications

Age-Dependent Distribution of Acidic Glycosaminoglycans in Human Kidney Tissue

Age-Dependent Distribution of Acidic Glycosaminoglycans in Human Kidney Tissue

Comparative Studies on Proteodermatan Sulfate of Bovine Gastrointestinal Tract.

Glycosaminoglycan Components in Duodenum with Advancing Age and in Patients with Progressive Systemic Sclerosis

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