Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.23.5 (
cathepsin D
)
4,130
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The effect of insulin on the concentration of different glycosaminoglycan (CG) fractions was different in different segments of aorta. Chondroitin sulphate A and heparin were increased in the aortic arch, thoracic and abdominal aorta, while chondroitin sulphate B and C were increased only in the aortic arch and abdominal aorta. Heparin sulphate and hyalutonic acid were increased only in the abdominal aorta. In the liver, significant increases occurred in all GG fractions. All enzymes studied which are involved in the biosynthesis of GG precursors, i.e. glucosaminphosphate isomerase, UDP glucose dehydrogenase and glucose-1-phosphate uridylyltransferase, were increased in the animals of the insulin group, while all enzymes involved in the degradation of GG, i.e. hyalurono glucosidase, beta-glucosaminidase, arylsulphatase, and
cathepsin D
, were decreased. Concentration of hepatic PAPS, activity of the sulphate-activiting system and sulphotransferase increased on administration of insulin.
Acta
Diabetol
Lat
PMID:Insulin and metabolism of glycosaminoglycans in rabbits. 71 66
GAG metabolism was investigated in rats with experimentally induced diabetes. In comparison to control animals, the uptake of 35S-sulfate was diminished in tissues of diabetic animals. Streptozotocin-induced diabetes showed a significant decrease in the content of GAG fractions except that of non-sulfated GAG in liver and kidney which was unchanged as compared to the control group. In rats rendered diabetic by alloxan, non-sulfated GAG increased appreciably in liver and kidney whereas highly sulfated GAG remained unchanged. In the skins of alloxan-diabetic rats both total and sulfated GAG decreased significantly. The activities of liver beta-glucuronidase, beta-N-acetyl glucosaminidase and
cathepsin D
were significantly increased in rats treated with streptozotocin and alloxan. In streptozotocin-diabetic rats, renal beta-glucuronidase and beta-N-acetyl glucosaminidase activities were reduced while
cathepsin D
activity was similar to that of controls. The renal beta-N-acetyl glucosaminidase and
cathepsin D
activities of alloxan-treated rats were not significantly different from normal but their beta-glucuronidase was significantly increased. In the spleen of streptozotocin-diabetic rats all the enzymes were increased except beta-N-acetyl glucosaminidase which remained unaltered. Increased excretion of uronic acid was observed in diabetic groups. These results collectively indicate that both streptozotocin- and alloxan-induced diabetes altered the synthesis and catabolism of GAG.
Acta
Diabetol
Lat
PMID:Influence of streptozotocin- and alloxan-induced diabetes on the metabolism of glycosaminoglycans. 624 Jan 83