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Biomedical subjects

S M Bose

Publications and source records attributed to S M Bose.

At least 55 records · Page 3Linked to original sources
PubMed1983

Effect of protein malnutrition on the cross-linking of gingival and uterine collagen in rats.

The effect of protein malnutrition on gingival and uterine collagen cross-linking was studied in female albino rats. The gingival and uterine samples were taken on the 28th day of the experimental period in both groups; the percent reversibility of neutral salt-soluble collagen, and the susceptibility of insoluble collagen to denaturing agents (to KSCN, urea, or pronase) were increased in gingival and uterine samples of protein-deficient animals. The analysis of gingival and uterine samples showed alpha 1 and alpha 2 subunits of neutral salt-soluble collagen appreciably increased, but beta 11 and beta 12 chains and the aldehyde content were significantly decreased in protein-deficient animals compared to controls. The results indicate that in protein deficiency the cross-linking and maturation of collagen are impaired.

Animals↗
PubMed1982

Effect of protein malnutrition on the crosslinking of dermal collagen in aging.

The effect of protein malnutrition on collagen crosslinking was studied in different age groups of rats. The percent of reversibility of neutral salt-soluble collagen gel and the susceptibility of insoluble collagen to denaturing agents and pronase decreased with aging. The electrophoretic pattern of neutral salt-soluble collagen on sodium dodecyl sulphate polyacrylamide gels showed a decrease of alpha 1 and alpha 2 subunits and an increase of beta-components, resulting in a decrease of alpha/beta ratio in aging. There was a significant decrease in the aldehyde content of neutral salt-soluble collagen during age. Protein deficiency was found to impair the crosslinking and the effect was greater in younger animals than in older ones.

Age Factors↗
PubMed1982

Effect of indomethacin and naproxen on the metabolism of glycosaminoglycans.

Indomethacin and naproxen were examined regarding their effects on glycosaminoglycan metabolism in normal albino rats. The biosynthesis of sulphated glycosaminoglycans as evaluated by the uptake of [35S-]sulphate and the content of glycosaminoglycans were measured in specimens of skin, liver and kidney. The results indicated that the biosynthesis of sulphated glycosaminoglycans was significantly inhibited by both these drugs, thus reflecting their anti-inflammatory properties. The catabolism of glycosaminoglycans was followed by estimating the activities of lysosomal glycohydrolases, viz., beta-glucuronidase, beta-N-acetyl glucosaminidase and cathepsin D in liver, kidney and spleen and urinary excretion of hexosamine and uronic acid. The results, considered collectively, indicated that both indomethacin and naproxen depressed the metabolism of glycosaminoglycans.

Acetylglucosaminidase↗
PubMed1981

Effect of adjuvant induced arthritis on the mechanical properties and thermal behavior of skin and tendon.

In rats with adjuvant induced arthritis, the mechanical properties and thermal behavior of the skin and tendon were studied during the acute and chronic phase of the disease. Among the mechanical properties, the tensile strength and elastic modulus were found to decrease markedly both in the skin and tendon of arthritic rats while the extensibility did not show any significant change during the course of the disease. The thermal behavior, namely, shrinkage temperature, denaturation temperature, isometric tension and the temperature at isometric tension were decreased appreciably both in the skin and tendon of arthritic rats, the decrease being prominent during the chronic phase of arthritis. Both the mechanical properties and thermal behavior were correlated with biochemical parameters such as total collagen content and the ratio of the total activity of 14C-hydroxyproline of soluble collagens to insoluble collagen. The results support the concept of impaired collagen crosslinking in adjuvant induced arthritis. Prednisolone and L-thyroxine were administered to arthritic rats and the changes in the mechanical properties and thermal behavior of the skin and tendon of arthritic rats were studied. Both prednisolone and L-thyroxine increased the decreased values of tensile strength and elastic modulus of the skin and tendon in adjuvant induced arthritis. Similarly the decreased values in the thermal behavior of arthritic rats were found to be increased by treatment with prednisolone and L-thyroxine. Results indicated correlations with the beneficial action of prednisolone and L-thyroxine on the impaired collagen crosslinking in adjuvant induced arthritis.

Animals↗
PubMed1981

Effect of indomethacin and naproxen on the metabolism of collagen in adjuvant-induced arthritis.

The effect of indomethacin and naproxen on collagen metabolism was studied in arthritic animals after an injection of [3H]-proline, both the specific and total radioactivity of [3H]-hydroxyproline being determined in skin collagen fractions and in urine. It was found that collagen synthesis and conversion of soluble to insoluble collagen are diminished, accompanied by an increased collagen degradation in untreated arthritic animals. Administration of indomethacin and naproxen to arthritic animals accelerated the synthesis of collagen and conversion soluble to insoluble collagen and inhibited the catabolism of collagen.

Animals↗
PubMed1980

Effect of adjuvant arthritis on collagenase and certain lysosomal enzymes in relation to the catabolism of collagen.

The activity of collagenase, cathepsin B1, cathepsin D and Hyaluronidase was determined in skin, bone, liver, kidney, spleen and serum of adjuvant induced arthritic rats during the acute and chronic phase of the disease. Collagenase was assayed directly in tissue extract by a solution method using radioactive labelled substrate. The activity of collagenase, cathepsin B1 and D was found to increase significantly at both phases of the disease. The activity of hyaluronidase decreased significantly in liver, kidney and spleen of arthritic rats, while in skin, bone and serum no significant change was observed. The results are discussed with respect to catabolism of collagen in adjuvant induced arthritis. Prednisolone and L-thyroxine were administered to arthritic rats and the activity of collagenase, cathepsin B1, cathepsin D and hyaluronidase was determined in the treated groups during the acute and chronic phase of the disease. Prednisolone was found to suppress the development of arthritis which, in turn, decreased the increased activity of collagenase and lysosomal enzymes cathepsin B1 and D in tissues and serum of arthritic rats. L-Thyroxine was found to slowly diminish the development of inflammation and its beneficial action was found in mesenchymal tissues and skin of arthritic rats but not in bone.

Acute Disease↗
PubMed1980

Influence of prostaglandins E1 and E2 on collagen metabolism in adjuvant induced arthritis.

In rats with adjuvant induced arthritis, the ihnfluence of PGE1 and PGE2 on collagen metabolism was investigated after an injection of 3H-proline, both the specific and total radioactivity of 3H-ydroxyproline being determined in skin collagen fractions and in urine. In untreated animals with adjuvant induced arthritis, a decrease in the collagen synthesis accompanied by a retardation in the conversion of soluble to insoluble collagen was observed. It was also found that the catabolism of collagen is intensified. Subcutaneous administration of PGE1 (1 mg/kg body weight twice daily) to arthritic animals accelerated the conversion of soluble to insoluble collagen and inhibited the catabolism of collagen, but remained ineffective on the decreased synthesis of collagen observed in arthritic animals. PGE2 normalised on the changes in collagen metabolism - accelerated the synthesis of collagen and the conversion of soluble to insoluble collagen and inhibited the catabolism of collagen.

Animals↗
PubMed1979

Influence of prednisolone and L-thyroxine on the changes in collagen metabolism in rats with adjuvant-induced arthritis.

In rats with adjuvant-induced arthritis the effects of prednisolone and L-thyroxine on the changes in collagen metabolism were investigated both in the skin and tendon during the acute and chronic phase of the arthritis. In untreated animals with adjuvant-induced arthritis, a decrease in the collagen synthesis accompanied by an increase in the catabolism of collagen and a retardation in the conversion of soluble to insoluble collagen were noted both in the skin and tendon during the course of the disease. Prednisolone was found to accelerate the conversion of soluble to insoluble collagen and to inhibit the enhanced catabolism of collagen in rats with adjuvant-induced arthritis. L-Thyroxine accelerated the conversion of soluble to insoluble collagen in adjuvant-induced arthritic rats more effectively than prednisolone but was less effective with regard to the inhibition of enhanced catabolism of collagen. However, the synthesis of collagen in adjuvant-induced arthritis was improved by both prednisolone and L-thyroxine.

Acute Disease↗
PubMed1979

Effect of protein deficiency on the metabolism of glycoproteins and glycosaminoglycans in albino rat skin.

1. The total content of neutral sugars in skin of the weanling albino rats kept on the protein-deficient diet was increased by about 40%; this was mainly due to the increased concentration of galactose. The content of sialic acid was increased by about 20%. The collagen nitrogen was decreased significantly, with a concomitant increase of non-collagen nitrogen. At the same time, the content of sulphated glycosaminoglycans in skin was significantly decreased and that of non-sulphated glycosaminoglycans was increased. 2. Protein-deficient diet enhanced the activities of the protein-bound carbohydrate-degrading lysosomal hydrolases, viz. cathepsin D (EC 3.4.4.23), N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30) and beta-D-glucuronidase (EC 3.2.1.31) both in liver and skin. The activity of liver hyaluronidase (EC 3.2.1.35) was also increased upon limitation of protein supply. 3. The changes observed in skin were accompanied by increased concentration of the protein-bound hexoses, hexosamines and sialic acids in serum, and of hexosamine and uronic acid in urine. The serum fucose remained unchanged.

Animals↗
PubMed1978

Hydroxyproline-rich glycoprotein in the seed coat of field bean.

1. The seed coats of field bean (Dolichos lablab var. lignosus) were found to contain bound hydroxyproline (0.26 g per 100 g dry weight) extractable in 30% with 5% trichloroacetic acid or in 90% with 10% potassium hydroxide. 2. The alkaline extract was fractionated by DEAE-cellulose chromatography into several hydroxyproline-containing fractions, composed of protein and carbohydrate in varying proportions. From the major fraction, a hydroxyproline-containing glycoprotein fraction was isolated by Sephadex G-200 chromatography. It gave a single band on agar-gel electrophoresis, and contained: protein (23.1%), arabinose (11.2%), galactose (13.4%), glucose (17.6%), mannose (22.6%) and uronic acids (11.3%). The content of hydroxyproline in the protein moiety was about 9%. Hydrolysis of the glycoprotein fraction with barium hydroxide yielded three components containing hydroxyproline and arabinose at the ratios of 1:2, 1:3 and 1:4.

Chromatography, DEAE-Cellulose↗
PubMed1976

Glycoprotein nature of tannase in Aspergillus niger.

1. Tannase (tannin acyl-hydrolase, EC 3.1.1.20) was isolated from the culture medium of Aspergillus niger and purified about 200-fold. On polyacrylamide-gel electrophoresis it gave a single band. 2. The molecular weight of the enzyme was of the order of 55 000 as determined by gel filtration. The enzyme contains 21.5% of carbohydrates (mannose and glucose). 3. Treatment of tannase with alkaline borohydride decreased the content of threonine, serine and mannose, suggesting that the carbohydrate-peptide linkage is of the O-glycoside type, involving mannose linked to threonine and serine.

Aspergillus↗