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Biomedical subjects

H Shinkai

Publications and source records attributed to H Shinkai.

At least 127 records · Page 7Linked to original sources
PubMed1987

Age-related changes of the dermatan sulfate containing small proteoglycans in bovine tendon.

Sulfated proteoglycans of fetal, newborn and adult bovine tendon are extracted with neutral salt and then with 4 M guanidine HCl in the presence of proteinase inhibitors. Dermatan sulfate containing small proteoglycans are separated from chondroitin sulfate rich proteoglycans by CsCl-gradient centrifugation, by affinity chromatography using concanavalin A and by molecular sieve chromatography. These proteoglycans are comprised of a core protein with an average Mr of about 53,000 on polyacrylamide gel electrophoresis with SDS and of dermatan sulfate side chains with Mr 25,000-38,000 by gel chromatography. The tryptic peptides patterns observed in the small proteoglycans from newborn calf and adult bovine tendon are identical but are distinct from those of embryonic calf tendon. The patterns of the tryptic peptides of the core proteins from embryonic calf tendon are similar to those from the dermatan sulfate proteoglycans of calf skin. These results indicated that genetically independent genes of the core proteins from dermatan sulfate proteoglycans in tendon tissues were expressed by aging.

Aging↗
PubMed1987

Acidic glycosaminoglycans, isolation and structural analysis of a proteodermatan sulfate from dermatosparactic calf skin.

Dermatan sulfate and hyaluronic acid are the major glycosaminoglycan components of dermatosparactic and normal calf skin but the ratio of hyaluronic acid to dermatan sulfate is 50-70% higher in dermatosparactic calf skin than that in normal calf skin. Hyaluronic acid in normal calf skin could be extracted to 93% of the total by NaCl and guanidine hydrochloride, while in dermatosparactic calf skin 57% of hyaluronic acid remained in the insoluble material after NaCl and guanidine hydrochloride extraction. The recovery of proteodermatan sulfate in NaCl extracts was similar in normal and dermatosparactic skin. The amount of proteodermatan sulfate extracted in guanidine hydrochloride form normal calf skin was 2-4 fold higher than that from dermatosparactic calf skin. No significant difference between dermatosparactic and normal calf skin proteodermatan sulfate could be detected in terms of size of the core protein (Mr = 55,000) by sodium dodecyl sulfate polyacrylamide gel electrophoresis, amino acid analysis, immunological cross-reactivity using polyclonal antibodies against either dermatosparactic or normal calf skin core protein, tryptic peptides or size of dermatan sulfate chains (Mr = 17,000-18,000) on gel chromatography.

Animals↗
PubMed1986

Two species of dermatan sulfate proteoglycans with different molecular sizes from newborn calf skin.

Two species of dermatan sulfate-proteoglycans (DS-PGs) were isolated from calf skin. The first species, PDS-H (high-molecular-weight proteodermatan sulfate), contains the core protein with a molecular weight of either about 55,000 or 53,000. Both the core proteins are capable of binding to concanavalin A (Con A). The second species, PGs-L (low-molecular-weight proteoglycan containing dermatan sulfate and/or chondroitin sulfate), contains a core protein of Mr = 20,000 that did not bind to Con A. Tryptic peptide mappings revealed that Mr = 55,000 core protein and Mr = 53,000 core protein were of the same origin. However, the tryptic peptides and the amino acid composition of PGs-L core protein were completely different from those of PDS-H core proteins. The polyclonal antibodies against Mr = 55,000 core protein reacted with both the core proteins of Mr = 55,000 and Mr = 53,000 but not with the core protein from PGs-L. The DS was found to be the only glycosaminoglycan component of PDS-H. That is, the glycosaminoglycan from PDS-H was composed of 46% iduronosylhexosamine units and 54% glucuronosylhexosamine units, while the glycosaminoglycan of PGs-L was composed of 30% iduronosylhexosamine units and 70% glucuronosylhexosamine units.

Animals↗
PubMed1986

Two cases of adult T-cell leukaemia.

A 70-year-old male and a 46-year-old female, both living in Japan, were seen because of multiple erythematous papules and plaques on the trunk and extremities. The peripheral white blood cell counts were increased to 30,000-80,000/mm3. The majority of white cells had characteristic lobulated and deeply indented nuclei. The patients and most of their family members had anti-ATLV antibody. Using an OKT series of monoclonal antibodies the tumour cells were found to be T-cells. Trisomy 21 was detected in the first case and ATL virus proviral DNA in the second.

Aged↗
PubMed1986

[Göttingen miniature swine as a model for diet-induced atherosclerosis].

Twenty-four Göttingen Miniature Swine/csk, in order to evaluate their potential usefulness as a model for experimental atherosclerosis studies, were fed diets of three types, a high-fat plus high cholesterol diet, a high-fat diet, and a commercial diet. Each group consisted of 4 males and 4 females. Swine fed the experimental diet were investigated by gross, microscopic and serum biochemical examination on the 1st, 3rd, 6th and 9th month after start of experimentation. Lesions of atherosclerosis were observed in the high-fat plus high-cholesterol diet group. After a month on the experimental diet, intimal thickening was detected in the abdominal aorta just above the origin of internal iliac artery, left coronary artery and ascending aorta by microscopic examination. Thereafter, on the 9th month after the start, there was more extensive and severe atherosclerosis. These lesions were classified into two types by the difference in the histologic architecture of arterial wall. One was fatty streaks that were in thoracic aorta belonging to the elastic type and the other was fibrous plaques that were in abdominal aorta and iliac artery and so on, belong to the transitional or muscular type. High-fat plus high-cholesterol diet feeding led to elevated serum cholesterol and beta-lipoprotein levels, and had an effect on several kinds of metabolism. All of the swine fed high-fat or commercial diet had little gross, microscopic lesions and had no change in serum cholesterol and beta-lipoprotein levels. Hypercholesterolemia and hyper-beta-lipoproteinemia had a close relation to the development and acceleration of atherosclerosis. It was possible to show that the diet induced atherosclerosis was similar in quality to that observed in humans, and that the Göttingen miniature swine was a suitable animal for the study of atherosclerosis.

Animals↗
PubMed1985

An acidic glycoprotein (100-K fucose-rich glycoprotein) from calf skin.

A new acidic glycoprotein was isolated from 4 M-guanidiunium chloride which had been extracted from neutral-salt-insoluble fractions of neonatal calf skin. During the process of purification, the glycoprotein co-migrated with proteodermatan sulphate and its sugar components mainly consisted of fucose, mannose and hexosamine. A broad band obtained by sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis suggested that the molecular weight was 100,000. High-voltage electrophoresis, revealed acidic fragments in its tryptic peptides, while its oligosaccharide chains were shown to have on acidic nature by electrophoresis on a cellulose acetate membrane. These results show that the glycoprotein differs from other glycoproteins (fibronectin, laminin, entactin, nidogen and the 31-K protein of chondrocyte membrane) which have been reported in connective tissues.

Animals↗
PubMed1983

Isolation and some structural analyses of a proteodermatan sulphate from calf skin.

A proteodermatan sulphate was isolated from 0.15 M-NaCl and 0.45 M-NaCl extracts of newborn-calf skin. The proteoglycan was separated from collagen and hyaluronic acid by precipitation with cetylpyridinium chloride and CsCl-density-gradient centrifugation. Further purification was performed by ion-exchange, affinity and molecular-sieve chromatography. The proteoglycan bound to concanavalin A-Sepharose in 1 M-NaCl. It gave a positive reaction with periodic acid/Schiff reagent and contained 8.3% of uronic acid. The dermatan sulphate, the only glycosaminoglycan component, was composed of 74% iduronosylhexosamine units and 26% glucuronosylhexosamine units. The Mr was assessed to be 15000-20000 by gel chromatography. The core protein was found to be a sialoglycoprotein that had O-glycosidic oligosaccharides with N-acetylgalactosamine at the reducing termini. The molar ratio of oligosaccharide chains to dermatan sulphate was approx. 3:1. From these results the proposed structure of proteodermatan sulphate is: one dermatan sulphate chain (average Mr 17500), three O-glycosidic oligosaccharide chains and probably N-glycosidic oligosaccharide chain(s) bound to one core-protein molecule (Mr 55000).

Amino Acids↗
PubMed1983

Evidence for the presence and structure of asparagine-linked oligosaccharide units in the core protein of proteodermatan sulphate.

The N-glycosidically linked oligosaccharides were liberated by hydrazinolysis from purified proteodermatan sulphate from newborn-calf skin and reduced with NaB3H4 at the reducing terminal sugar. One asparagine-linked oligosaccharide chain was linked to one core-protein molecule in proteodermatan sulphate. Structural sequences were analysed by using exoglycosidase digestion. These oligosaccharides were composed of di- and tri-antennary oligosaccharide structures of complex type.

Animals↗
PubMed1983

Characterization of oligosaccharide units of p-N-collagen type III from dermatosparactic bovine skin.

p-N-collagen type III was extracted from dermatosparactic and normal fetal bovine skin and purified by ion-exchange chromatography using DEAE- and CM-cellulose. Asparagine-linked sugar chains were fractionated by high voltage paper chromatography from the products obtained after hydrazinolysis and reduction with NaB3H4. These oligosaccharides composed of neutral and acidic components are mannose-containing oligosugars of the complex type. Their abundance is much higher in dermatosparactic p-N-collagen type III.

Animals↗
PubMed1981

Comparable content of hydroxylysine-linked glycosides in subcomponents C1q of the first component of human, bovine and mouse complement.

The hydroxylysine-glycosides in bovine and mouse C1q are directly quantified in parallel with those in human C1q after the alkaline hydrolysis of these molecules. Human, bovine and mouse C1q contain 68.3, 66.3 and 64.0 hydroxylysine-galactosylglucose residues in each of these molecules respectively. Only human C1q contains 2.5 residues of hydroxylysine-galactose per molecule, and both of bovine and mouse C1q contain no detectable hydroxylysine-monosaccharides in their molecules. The percentage of hydroxylysine residues glycosylated to total hydroxylysine residues in each of these molecules is calculated to be 86.4, 92.0 and 95.1% for human, bovine and mouse C1q respectively and is comparable with each other. The percentages of hydroxylysine residues resistant to periodate oxidation to total hydroxylysine residues in these molecules were 61.1, 65.3 and 74.3% for human, bovine and mouse C1q respectively and were significantly lower than those estimated by the direct quantification of hydroxylysine-glycosides after the alkaline hydrolysis of these molecules.

Animals↗