Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0011849 (diabetes)
 277,896 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The accumulation of 3H-fucose labelled glycoprotein and 35S-methionine labelled protein carried by the retrograde axonal transport in the sensory fibres of the sciatic nerve was examined on the day after injection of streptozotocin in rats. The accumulation of fucose-label was reduced (2.8 +/- 0.4 (SD) versus 2.1 +/- 0.5 (arbitrary units), 2p = 0.0044) indicating a decreased retrograde flux of glycoproteins. This early transport abnormality could have a key role in the development of peripheral neuropathy in diabetes.
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PMID:Retrograde axonal transport. A possible role in the development of neuropathy. 616 98

An alpha-amylase inhibitor isolated from Streptomyces tendae, strain 4158 was re-purified by chromatography on CM- and DEAE-cellulose column. Two inhibitors could be characterized: alpha-amylase inhibitor Hoe-467 A (with aspartic acid as N-terminal residue), and alpha-amylase inhibitor Hoe-467 S (with serine as N-terminal residue). The primary structure was determined by automatic Edman-degradation procedures of the aziranized inhibitor and tryptic peptides, derived from digestions of the performic oxidized, aziranized and maleylated inhibitor, respectively. The alpha-amylase inhibitor Hoe-467 A consists of 74 residues and has a calculated molecular weight of 7958. It is composed of all common amino acids except methionine and phenylalanine. Digestion with pepsin was carried out to determine the disulfide bonds. Two fractions could be isolated, containing one cystine each giving information about the positions of the disulfide bridges. The possible clinical application of the inactivator (diabetes mellitus) is pointed out.
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PMID:[The sequence of the alpha-amylase inhibitor Hoe-467 A (alpha-amylase inactivator Hoe-467 A) from Streptomyces tendae 4158]. 616 65

It was shown that insulin stimulated and hydrocortisone inhibited 14C'glycine and 3H methionine incorporation into the skeletal muscle polysome, cytosol and total proteins of rats alloxan diabetes. Hydrocortisone inhibitory effect was slightly diminished after insulin administration when both hormones were used simultaneously. The blood glucose content of diabetic rats decreased under insulin action and rose after hydrocortisone use. It was concluded that the inhibition of skeletal muscle protein metabolism may be caused not only by insulin deficiency, but also by glucocorticoid hormone excess.
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PMID:[Incorporation C14-glycine and H3-methionine into total and cytoplasmic proteins of rat skeletal muscles in insulin deficiency and glucocorticoid hormone excess]. 617 59

Islet cell surface antibodies (ICSA) have been generated to investigate relations between recognition of specific antigens and cytotoxic reactions on pancreatic islet cells. Sera from rabbits which had been directly immunized with islet cells or intact rat islets exhibited positive immunofluorescence with both rat and rabbit pancreatic islet cells. Analysis by SDS polyacrylamide gel electrophoresis and autoradiography of islet cells proteins prelabeled with [35S]methionine revealed that these sera precipitated a specific protein of Mr 40000. Serum from immunized rabbits stimulated 51Cr-release in suspensions of dispersed islet cells prepared from neonatal rats. Absorption to lymphocytes and liver powder removed antibodies that were cytotoxic to lymphocytes but complement-mediated cytotoxicity against islet cells persisted. Circulating ICSA neither in rabbits nor in rats caused changes in blood glucose. Moreover, no major alterations of islet cells in the immunized rabbits were observed upon electron microscopic examination. It is concluded that ICSA are capable of recognizing specific islet cell antigens and thus mediate complement-dependent cytotoxic reactions in vitro, but the mere presence of ICSA is obviously not sufficient to induce diabetes in vivo under the conditions used.
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PMID:Absence of cytotoxicity of islet cell surface antibodies in vivo despite complement-mediated cytotoxic effects to islet cells in vitro. 620 50

A protocol has been developed for maintaining isolated rat adipose cells in primary tissue culture. Using this protocol, cells remain fully viable and responsive to insulin for at least 24 h, as assessed by measuring 3-0-methylglucose transport, lipogenesis from [U-14C]glucose, and the incorporation of [35S]methionine into total membrane protein. The acute insulin-induced internalization of its own receptor was then examined by biosynthetically labeling cells in culture with either [35S]methionine or [3H]glucosamine, maximally inducing receptor internalization with a 30-min incubation in the presence of saturating insulin, and preparing plasma and low-density microsomal membrane fractions by differential ultracentrifugation. Receptors were immunoprecipitated with anti-receptor antiserum, and the receptor subunits separated by NaDodSO4-PAGE under reducing conditions and analyzed by autoradiography. When cells not acutely treated with insulin are examined, both the 135K alpha- and 95K beta-receptor subunits are prominently labeled in the plasma membrane fraction, but only faintly labeled in the low-density microsomal membrane fraction. Following the induction of maximal acute receptor internalization, both subunits are decreased by 20-30% in the plasma membrane fraction and concomitantly increased in the low-density microsomal membrane fraction. However, the relative molecular weights and labeling intensities of the two subunits remain constant and correspond to those observed in the biosynthetically labeled human lymphocyte receptor. A minor band of Mr congruent to 190K is also labeled, but its labeling intensity is similar in the two membrane fractions from basal cells and does not change in response to insulin.(ABSTRACT TRUNCATED AT 250 WORDS)
Diabetes 1984 Jan
PMID:Insulin-induced internalization of the insulin receptor in the isolated rat adipose cell. Detection of both major receptor subunits following their biosynthetic labeling in culture. 636 Jul 64

The effects of insulin and insulin-like growth factor I (IFG-I) on protein synthesis were compared in muscle isolated from lean and goldthioglucose (GTG)-obese mice. Two types of skeletal muscles, the red soleus and the white extensor digitorum longus (EDL) muscles, were studied. In muscles from lean mice, 6.7 nM insulin and 50 nM IGF-I caused a similar maximal stimulation of tyrosine incorporation in total proteins (40% increase). However, the potency of IGF-I was only 5-10% that of insulin both in soleus and in EDL muscles (EC50 approximately equal to 6 nM for IGF-I and 0.5 nM for insulin). Basal rate of protein synthesis was identical in muscles from GTG-obese and lean mice. Similarly, a comparable increase in the rate of protein synthesis was obtained using maximally effective concentrations of insulin and IGF-I in both lean and GTG-obese animals. SDS-polyacrylamide gel electrophoresis analysis of proteins labeled with 35S-methionine confirmed that, in muscles from lean and GTG-obese animals, insulin and IGF-I increased overall protein synthesis in a similar manner. These results suggest that the protein synthesis machinery is not impaired in GTG-induced obesity, which is therefore not associated with resistance to insulin for its effect on protein metabolism.
Diabetes 1983 May
PMID:Insulin and insulin-like growth factor I. Effects on protein synthesis in isolated muscles from lean and goldthioglucose-obese mice. 640 79

Phosphatidylethanolamine N-methylation was studied in cardiac sarcolemma 8 weeks after the induction of chronic experimental diabetes in rats by a streptozotocin injection (65 mg/kg, iv). Incorporation of radiolabeled methyl groups from S-adenosyl-L-methionine into intramembranal phosphatidylethanolamine, assayed under optimal conditions, confirmed the existence of three catalytic sites involved in the sequential methyl transfer reactions. Total methyl group incorporation at all three sites was significantly depressed in diabetic myocardium, but this change was reversible by a 14-day insulin therapy to the diabetic animals. Measurements of phospholipid N-methylation activity at different times indicated that the depression was evident at 6 weeks after the induction of diabetes. This defect was also seen for the individual methylated lipid products (monomethyl-, dimethylphosphatidylethanolamine, and phosphatidylcholine) specifically formed at each catalytic site. Experiments with different concentrations of S-adenosyl-L-methionine revealed that, for all three sites, the apparent affinity for the methyl donor did not change, whereas the apparent Vmax values were significantly lowered in diabetes. The results of this study identify a defect in the sarcolemmal phosphatidylethanolamine N-methylation in diabetic cardiomyopathy.
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PMID:Sarcolemmal phosphatidylethanolamine N-methylation in diabetic cardiomyopathy. 647 54

The native or modified alpha-amylase inhibitor Hoe 467A - isolated from the culture medium of Streptomyces tendae 4158 - and overlapping peptides were degraded by the automatic Edman technique. The oxidized or aminoethylated or oxidized and maleoylated inhibitor was digested with trypsin and the native inhibitor with pepsin. Further digestion with Staphylococcus aureus proteinase was also carried out. After peptic digestion two cystin peptides were isolated, which allowed the establishment of the disulfide bonds. The alpha-amylase inhibitor is a polypeptid consisting of 74 amino-acid residues with a molecular mass of 7958 Da. The inhibitor is composed of all naturally occurring amino acids except methionine and phenylalanine and shows no sequence homology to known inhibitors. The clinical and pharmacological importance in respect to the inhibitors ability for inactivation of human salivary and pancreatic alpha-amylase is discussed. Especially the proteinase resistance of the inhibitor enables a clinical application in human (e.g. Diabetes mellitus) per os.
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PMID:[The primary structure of the alpha-amylase inhibitor Hoe 467A from Streptomyces tendae 4158. A new class of inhibitors]. 660 9

Polyadenylated RNA extracted from anglerfish islets was translated in a wheat germ cell-free system containing [35S]methionine in the presence and absence of microsomal membranes prepared from a canine pancreas. Labeled translation products were analyzed by immunoprecipitation with an antiserum to porcine glucagon, followed by electrophoresis of the translation products and immunoprecipitated proteins on SDS polyacrylamide gels. In the absence of microsomal membranes two proteins of Mr = 14,500 and Mr = 12,500 were specifically immunoprecipitated with antiglucagon serum. Addition of microsomal membranes to the translation reactions resulted in a diminution of the labeled protein of Mr = 14,500 and a marked increase in the immunoreactive protein of Mr = 12,500. The protein of Mr = 12,500 was resistant to degradation by proteolytic enzymes added to translation reactions, indicating that it was segregated within microsomal vesicles. These results are consistent with synthesis of anglerfish islet glucagon in the form of a pre-prohormonal precursor (Mr = 14,500) containing a leader sequence that is cotranslationally cleaved from the protein by enzymes associated with microsomal membranes to produce a smaller intermediate prohormonal precursor (Mr = 12,500) of pancreatic glucagon (Mr = 3500).
Diabetes 1980 Jul
PMID:Glucagon precursors identified by immunoprecipitation of products of cell-free translation of messenger RNA. 699 42

The intensity of labelled amino acid incorporation into spleen total proteins of albino rat with experimental diabetes was studied as influenced by hydrocortisone, insulin and both hormones simultaneously. Hydrocortisone inhibits and insulin stimulates the [14C] glycine and [3H] methionine incorporation into total proteins of alloxan-diabetic rat spleen. Under simultaneous administration of both hormones the inhibitory hydrocortisone effect is allayed by insulin. It is suggested that an increased level of glucocorticoid hormones in blood is one of the reasons of protein metabolism disturbance under diabetes mellitus.
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PMID:[Effect of hydrocortisone and insulin on (14C)-glycine and (3H)-methionine incorporation into spleen proteins in alloxan-diabetic rats]. 702 Jan 95


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