Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The synergistic effects of dexamethasone (DEX) and thyroxine (T4) on the postnatal maturation of the 13-d-old rodent small intestine has been studied. Previous studies have shown that hydrocortisone and T4 produced a synergistic response in enzyme maturation. However, T4 elevates corticosteroid-binding globulin, which reduces the clearance of hydrocortisone. Thus, the apparent synergy between T4 and hydrocortisone may have been due to increased glucocorticoid availability. DEX, which does not bind to corticosteroid-binding globulin, was given (d8-12) at 25 pmol (i.e. 0.01 micrograms)/g body wt/d as established by a dose-response study in which this dose of DEX induced one third the maximum response in sucrase activity. In this way, synergy with T4 (130 pmol/g body wt/d, i.e. 0.1 micrograms/g body wt/d, d 5-12) could still be observed. Glucoamylase, lactase, acid beta-galactosidase, alkaline phosphatase, and sucrase activities were determined in two regions of the small intestine. Overall, the results for the two hormones administered alone showed intestinal maturation to be not significantly affected in the T4 group and partially stimulated in the DEX group. When combined, DEX + T4 synergistically increased jejunal sucrase, ileal glucoamylase, and duodenal alkaline phosphatase, and lowered ileal acid beta-galactosidase. The striking exceptions to the general pattern were two brush border enzymes that normally decline during intestinal maturation, namely ileal alkaline phosphatase and jejunal and ileal lactase. For these enzymes, DEX alone did not elicit precocious maturation, and there was no evidence for a synergistic interaction of these two hormones. Serum corticosterone concentrations also were measured. When corticosterone concentrations were compared with enzyme activity, no correlation was found.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Synergistic effects of thyroxine and dexamethasone on enzyme ontogeny in rat small intestine. 140 67

Studies of intestinal enzyme development and regulation relevant to the human infant require an animal model with a rate of maturation similar to that of the human infant. Hanford miniature pigs were weaned at 3 days of age to a standard swine weaning formula. At 1, 2, 3, 4, 5, and 6 wk of age, duodenal jejunal, and ileal segments were analyzed for protein content and lactase, sucrase, maltase, glucoamylase, and acid beta-galactosidase activities. Protein content of the small intestine changed significantly with age only in the ileum (p less than 0.05). Lactase activity fell significantly with age in all segments of the small intestine (p less than 0.001); activity was highest in the jejunum. Sucrase and maltase activities were present in all segments of the small intestine at 1 wk of age. Sucrase increased significantly (2-fold, p less than 0.02) with age only in the ileum and maltase increased significantly with age in the jejunum (by 50%, p less than 0.05) and the ileum (3-fold, p less than 0.001). Activities were highest in the jejunum. Glucoamylase activity was present at 1 wk of age and showed a small but significant increase with age only in the duodenum (p less than 0.005). Acid beta-galactosidase activity demonstrated small but significant decreases with age in all small intestinal segments. Glucoamylase and acid beta-galactosidase activities were similar in all segments. In the 6-wk-old pigs, activities of all the enzymes tested were similar to those found in young human infants.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The miniature pig as an animal model for the study of intestinal enzyme development. 312 4

The lysosomal enzymes cathepsin D (E.C. 3.4.23.5), alpha-glucosidase (E.C. 3.2.1.20) and beta-galactosidase (E.C. 3.2.1.23), potentially involved in the breakdown of the peptide component and the disaccharide units of basement membrane glycoproteins, were studied in the kidney cortex and liver of streptozotocin-diabetic mice. In the liver of diabetic mice, as compared to controls, an increase was found for the total activity (measured in frozen-thawed homogenates) of cathepsin D (+135%, P less than 0.01) and beta-galactosidase (+32%, P less than 0.05). In the kidney a decrease was observed for both the free activity (measured in 12,000 g supernatant) and the total activity of these two enzymes (cathepsin D: -62% and -24%; beta-galactosidase: -29% and -23%; P less than 0.05 in all instances). Alpha-glucosidase did not show significant changes in either tissues. Total protein content of the two organs did not change significantly with diabetes and therefore cannot account for the enzyme alterations observed. These data indicate that the response of kidney to diabetes is opposite to that of liver (decrease versus increase in catabolic enzymes), and suggest decreased degradation of basement membrane in some tissues in diabetes, which may contribute to the thickening of basement membrane and therefore to the development of microangiopathy.
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PMID:Cathepsin D and other hydrolases in the kidney of streptozotocin-diabetic mice. Possible relevance to microangiopathy. 393 Mar 80