Altered synthesis of some secretory proteins in pancreatic lobules isolated from streptozotocin-induced diabetic rats
- Univ. of Lund (Sweden)
The in vitro incorporation of (35S)cysteine into lipase, colipase, amylase, procarboxypeptidase A and B, and the serine proteases and total proteins was studied in pancreatic lobules isolated from normal and diabetic rats with or without insulin treatment. The incorporation of (35S)cysteine into total proteins was 65% greater in pancreatic lobules from diabetic animals than from normal rats. The increased incorporation was partly reversed by insulin treatment (2 U/100 g/day for 5 days) of diabetic rats. The relative rates of biosynthesis for amylase and the procarboxypeptidases in diabetic pancreatic lobules were decreased by 75 and 25%, respectively, after 1 h of incubation, while those for lipase, colipase, and the serine proteases were increased by 90, 85, and 35%, respectively. The absolute rates of synthesis for these enzymes changed in the same direction as the relative rates in diabetic lobules, except that for the procarboxypeptidases, which did not change. The changed rates of biosynthesis for the pancreatic enzymes were reversed by insulin treatment of the diabetic rats. Kinetic studies showed that the incorporation of (35S)cysteine into amylase, lipase, and colipase was linear until up to 2 h of incubation in normal pancreatic lobules, while in the diabetic lobules the incorporation into lipase and colipase was accelerated, reaching a plateau level already after 1 h of incubation. It is concluded that the biosynthesis of pancreatic secretory proteins in diabetic rats is greatly changed both in terms of quantity and kinetics.
- OSTI ID:
- 7136888
- Journal Information:
- Pancreas; (USA), Vol. 5:2; ISSN 0885-3177
- Country of Publication:
- United States
- Language:
- English
Similar Records
Protective effect of bioflavonoid myricetin enhances carbohydrate metabolic enzymes and insulin signaling molecules in streptozotocin–cadmium induced diabetic nephrotoxic rats
Diabetes in the rat is associated with a reversible postreceptor defect in cholecystokinin action
Related Subjects
DIABETES MELLITUS
PATHOGENESIS
PROTEINS
BIOSYNTHESIS
AMYLASE
CYSTEINE
IN VITRO
LIPASES
PANCREAS
PEPTIDE HYDROLASES
RADIOIMMUNOASSAY
RATS
SCINTILLATION COUNTING
SULFUR 35
AMINO ACIDS
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOASSAY
BODY
CARBOXYLESTERASES
CARBOXYLIC ACIDS
COUNTING TECHNIQUES
DAYS LIVING RADIOISOTOPES
DIAGNOSTIC TECHNIQUES
DIGESTIVE SYSTEM
DISEASES
ENDOCRINE DISEASES
ENDOCRINE GLANDS
ENZYMES
ESTERASES
EVEN-ODD NUCLEI
GLANDS
GLYCOSYL HYDROLASES
HYDROLASES
IMMUNOASSAY
IMMUNOLOGY
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
MAMMALS
METABOLIC DISEASES
NUCLEI
O-GLYCOSYL HYDROLASES
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
ORGANS
RADIOASSAY
RADIOIMMUNODETECTION
RADIOIMMUNOLOGY
RADIOISOTOPES
RODENTS
SULFUR ISOTOPES
SYNTHESIS
THIOLS
TRACER TECHNIQUES
VERTEBRATES
550901* - Pathology- Tracer Techniques