Age-Dependent Distribution of Acidic Glycosaminoglycans in Human Kidney Tissue

Murata, Katsumi; Horiuchi, Yoshihiko

doi:10.1159/000181203

Cited by 38 publications

(36 citation statements)

References 21 publications

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“…As far as the author's knowledge, however, no paper has appeared on the biochemical aspects of the constitution of the human esophagus. The present paper reports the constituents of esophageal AGAG in healthy individuals by electrophoretic characterization and enzymic assay as reported previously (Murata 1975;Murata and Horiuchi 1978 (Fig. 2).…”

supporting

confidence: 55%

“…1977). Proportionally high contents of HA and DS in the esophagus are rather similar to those of skin tissue (Loewi 1961) and the medullar portion of the kidney (Murata 1975). The binding capacity of HA to water is quite high and it would hydro phoretically maintain water in the site of tissues (Laurent 1971).…”

Section: Discussionmentioning

confidence: 99%

“…3). Since the eluate in 1.75 M was not attacked with chondroitinase-AC but was attacked with chondroitinase-ABC, the AGAG in the eluate was supposed to be DS (Yamagata et al 1968;Murata 1975;Sekino et al 1977). Judging from the enzymic susceptibility, the main AGAG in the 1.75 M and 1 .25 M eluates seemed Thin-layer chromatographic separation of the AGAG undigested with chondroitinase-AC indicated that the main hexosamines in the 1.0 M and 1.75 M eluates were glucosamine and galactosamine, respectively, suggesting that the undigested AGAG in the 1.0 M and 1.75 M eluates were HS and DS, respectively.…”

mentioning

confidence: 99%

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Acidic Glycosaminoglycans in Human Esophagus Tissue

Sekino

Murata

Saito

1979

Tohoku J. Exp. Med.

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supporting

confidence: 55%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Acidic Glycosaminoglycans in Human Esophagus Tissue

Sekino

Murata

Saito

1979

Tohoku J. Exp. Med.

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“…The procedure was performed as described by DiFerrante (6). Crude tissue AMPS were prepared by methods reported previously (1 8,19).…”

Section: Methodsmentioning

confidence: 99%

Acid Mucopolysaccharide (AMPS) Abnormality in Multiple Sulfatase Deficiency: Chemical Compositions of AMPS in Urine and Liver

et al. 1982

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Summarvtissues and cultured skin fibroblasts (I, 2. 10.20.21). This disorderExtensive chemical analyses of acid mucopolysaccharides (AMPS) were carried out in the urine and tissues (liver and brain) from a Japanese patient and two European patients with multiple sulfatase deficiency (MSD). The Japanese patient with MSD contained excessive quantities of heparan sulfate and moderately increased chondroitin sulfate A/C. Urinary excretion of AMPS in MSD heterozygotes was increased 2-fold compared to our controls. The urinary pattern of AMPS in the mother of the MSD patient showed an increase of 18% heparan sulfate and 36% dermatan sulfate whereas the urinary excretion pattern in the father was increased 21% for heparan sulfate as contrasted to controls (chondroitin sulfate A. 50-52%: chondroitin sulfate C. 38-46%; andheparan sulfate, 3-I&).Seventy-five % of the AMPS and the MSD liver was heparan sulfate rather than dermatan sulfate. The degree of accumulation of AMPS in the MSD liver was 30-50 times that of the control.Cerebral gray matter from the MSD patient contained 30-40 times that of control (relative increase of heparan and dermatan sulfate) whereas only a 5-fold increase was observed in white matter. It seems that a major site of accumulated AMPS appears to be in the gray matter.Carbohydrate analysis of the AMPS obtained from MSD urine and tissues was performed by: enzyme digestion with testicular hyaluronidase, heparitinase and chondroitinase ABC, cellulose acetate electrophoresis, Dowex-1 column chromatography and amino sugar analysis by amino acid analyzer. These findings indicate that the major accumulated AMPS in MSD urine and liver is heparan sulfate and thus, the predominant AMPS metabolic defect in MSD is heparan sulfate degradation. SpeculationThe accumulation of negatively charged AMPS, particularly the increased he~aran sulfate in the nervous svstem of oatients with MSD, leads io cellular dysfunction resulting in changes in the net charge of neuronal cells.

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“…Two such tissues, in which the chemical nature of GAGs has been studied, are colon (for references see Thornton, Hunt & Huckerby, 1983) and the kidney (Allalouf, Ber & Sharon, 1964;Castor & Greene, 1968;Constantopoulos, Louie & Dekaban, 1973;Murata, 1975) of several species. It has been suggested (Macknight, Mason, Rose & Sherman, 1982) that in rabbit colon binding not only might explain the apparent distribution of tissue Na+ but that binding within crypts might facilitate Na+ absorption from Na+-poor fluids.…”

Section: Introductionmentioning

confidence: 99%

Characteristics of ionic binding by rat renal tissue in vitro.

Law¹

1984

The Journal of Physiology

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4. In cortical slices in media containing equimolar Cl-and other monovalent anions, binding occurred according to the sequence acetate < salicylate < Cl-< SCN-; Cl-was completely displaced by P043-.5. When medium pH was lowered, Na+ binding was markedly reduced in both regions, whereas C1-binding increased (and became significant in outer medulla).6. In NaCl solutions, Na+ binding capacity was saturated at control Na+ concentrations. When [Na+] was progressively reduced (iso-osmolality being maintained by addition ofurea), bound Na+ in both regions was nearly linearly related to log medium [Na+].7. Raising medium osmolality with urea caused decreased Na+ binding and increased Cl-binding in both regions.8. Na+ binding in both regions was significantly reduced by pre-treatment with chondroitinase ABC.9. Binding of both ions was independent of temperature within the range 2-37°C.10. The possibility is raised that renal ionic binding might influence vectorial ion transport by affecting free ion activity in the region of the transporting cells.

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Age-Dependent Distribution of Acidic Glycosaminoglycans in Human Kidney Tissue

Cited by 38 publications

References 21 publications

Acidic Glycosaminoglycans in Human Esophagus Tissue

Acidic Glycosaminoglycans in Human Esophagus Tissue

Acid Mucopolysaccharide (AMPS) Abnormality in Multiple Sulfatase Deficiency: Chemical Compositions of AMPS in Urine and Liver

Characteristics of ionic binding by rat renal tissue in vitro.

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