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Query: UMLS:C0011849 (diabetes)
 277,896 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Noninsulin-dependent diabetes is associated with a decrease in the activity of sarcolemmal phosphatase 1, but no change in the activities of phosphatase 2A, 2B, or 2C. Also unaffected by diabetes were the activities of protein kinase C, cAMP-dependent protein kinase and calcium-calmodulin protein kinase. Because of the decrease in phosphatase 1 activity, 32P incorporation into sarcolemmal phosphoproteins catalyzed by either intrinsic protein kinases or extrinsic cAMP-dependent protein kinase was elevated in the diabetic. Among the proteins whose phosphorylation was elevated in diabetes was the phospholamban-like protein, which has been implicated in the regulation of ATP-dependent calcium transport. The phosphate-linked increase could be prevented by exposing the membranes to a phosphatase inhibitor and either extrinsic cAMP-dependent protein kinase or alamethicin. In addition to the phosphatase-linked effects, analysis of individual sarcolemmal phosphoproteins by SDS-polyacrylamide gel electrophoresis indicated that diabetes caused a specific elevation in membrane phosphorylation of some proteins (43 kDa and 78 kDa), but a decrease in the phosphorylation state of other phosphoproteins (31 kDa and 49 kDa). The data indicate that membrane phosphorylation is dramatically altered by diabetes. The possibility that this contributes to altered myocardial function is discussed.
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PMID:Defective sarcolemmal phosphorylation associated with noninsulin-dependent diabetes. 215 49

Macrophages internalize and degrade proteins modified by advanced glycosylation end products (AGEs) via a specific receptor (AGE-R). Chemical cross-linking studies with AGE-bovine serum albumin have demonstrated that the molecular weight of this receptor is approximately 90,000. We previously established that the binding constant (Ka) of this receptor site for the chemically synthesized model AGE, 2-(2-furoyl)-4(5)-(2-furanyl)-1H- imidazole-butyric acid (FFI-BA), on cells of the mouse macrophagelike cell line RAW 264.7 is identical to that for AGE proteins. Therefore, FFI was used as an affinity matrix in the first purification step of the AGE-R. The membranes of RAW 264.7 cells were solubilized in octyl-beta-glucoside and subjected to affinity chromatography on FFI-sepharose and gel permeation on Superose 6 fast protein liquid chromatography. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis analysis of this material revealed a high enrichment of a 90,000-Mr protein that had AGE binding activity. Approximately 25% of the protein at this step was the 90,000-Mr protein. The 90,000-Mr membrane protein was purified to homogeneity by rechromatographing the material on Superose 12 in the presence of SDS before and after reduction with 2-mercaptoethanol. After these harsh conditions, the 90,000-Mr protein lost AGE binding activity. Additional cross-linking studies on human peripheral monocytes revealed an AGE-R protein of identical size to that on RAW 264.7 cells, suggesting the relatively highly conserved nature of this molecule.(ABSTRACT TRUNCATED AT 250 WORDS)
Diabetes 1990 Dec
PMID:Isolation of surface binding protein specific for advanced glycosylation end products from mouse macrophage-derived cell line RAW 264.7. 217 9

Both adrenalectomy and chemically induced diabetes mellitus cause a marked decrease of pancreatic amylase activity in rats, but it is unknown whether these effects are the result of a direct or indirect mechanism. The synthesis of various pancreatic enzymes has been studied in isolated pancreatic acini from sham-operated, castrated, and adrenalectomized animals as well as in animals that have been both adrenalectomized and castrated. Protein synthesis was measured by pulse labeling of acini with [35S]methionine followed by either trichloroacetic acid precipitation of total protein and counting or by SDS-PAGE and autoradiography, and additionally by in vitro translation of extracted pancreatic RNA using rabbit reticulocytes. Adrenalectomy resulted in a 70% reduction of amylase activity per milligram of acinar protein as a result of a decrease in amylase synthesis. This reduction in amylase synthesis is a consequence of a decrease in the amount of mRNA coding for amylase. After adrenalectomy, plasma concentrations of the following were reduced compared to controls: corticosterone to 0.45%, insulin to 11%, and glucose to approximately 66%. Addition of glucose to the drinking water caused an increase in insulin and plasma glucose, but this was not followed by an increase in amylase activity. We postulate that corticosterone directly regulates amylase synthesis in the rat pancreas.
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PMID:Role of glucocorticosteroids in the regulation of pancreatic amylase synthesis. 247 63

Circulating insulin-like growth factor binding protein (IGF BP) activity is increased in animals with streptozotocin-induced diabetes. Separation of BPs by SDS/PAGE for ligand and immunoblot analysis revealed that a 32,000 molecular weight BP is present and increased in diabetic serum. This BP is immunologically distinct from the low molecular weight fetal rat BP (rBP2) and is related to the human amniotic fluid BP (hBP1) that is increased in patients with insulin dependent diabetes mellitus.
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PMID:Identification of a type 1 insulin-like growth factor binding protein (IGF BP) in serum from rats with diabetes mellitus. 247 84

In order to investigate the early renal damage in diabetes mellitus, 89 diabetics without proteinuria by dipsticks and 67 normal control subjects were examined by means of SDS-PAGE. The relationships between electrophoretic patterns of urinary protein and duration of diabetes, age of patients, metabolic controls and stages of retinopathy were examined. 1) The percentage of higher molecular weight (MW) proteins (67,000 less than or equal to MW) was larger in diabetics than that in controls. Especially the percentage of proteins with MW between 67,000 and 94,000, which include transferrin was 13.9 +/- 6.9% in diabetics, significantly higher than that in controls (10.3 +/- 5.1%) (P less than 0.01). On the contrary, the percentage of low MW proteins (MW less than 67,000) was relatively small in diabetics. 2) The excretion of higher MW proteins increased until 16 years of diabetic duration, however that decreased after 16 years. Especially in the group with duration longer than 20 years, excretion of low MW proteins increased. 3) Electrophoretic patterns of urinary proteins in patients with good metabolic control were similar to those in normal controls. 4) Excretion of higher MW proteins increased in patients with retinopathic complication suggesting the progression to microangiopathy. From the above results, we concluded that increased excretion of higher MW proteins in diabetics may be the results of GBM damages in protein selectivity. In patients with longer history of diabetes, predominant excretion of urinary low MW proteins may be the result of tubular dysfunction due to macroangiopathy.
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PMID:[A study of microproteinuria in patients with diabetes mellitus]. 259 18

The specific activities of membrane-bound maltase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20) in isolated brush border membranes (BBMs) of alloxan-induced diabetic, glucose-infused and maltose-infused rabbits were 30%, 140% and 160%, respectively, of those of control rabbits. Differences in the relative activities of trehalase (EC 3.2.1.28), another disaccharidase, in these groups were similar but less marked. However, the activities of two other marker enzymes of the brush border, alkaline-phosphatase and gamma-glutamyl transpeptidase, were similar in the 4 groups of rabbits. The decreases in the activities of the two disaccharidases were due to changes in the Vmax values of the enzymes without change in their Km values for maltose and trehalose. The maltase activities in the 4 groups showed similar dependences on Tris-HCl, KCl and NaCl. The electrophoretic profiles of the BBMs of the 4 groups on SDS-polyacrylamide gel showed slight differences. From these results, we conclude that diabetes, glucose infusion and maltose infusion probably change the concentrations of active enzymes in the BBM of the kidney in rabbits.
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PMID:Comparisons of maltase activities in kidney brush border membranes from normal, diabetic, glucose-infused and maltose-infused rabbits. 266 45

The discovery of a cold-labile cytosolic acetyl-CoA hydrolase of high activity in rat liver by Prass et al. [(1980) J. Biol. Chem. 255, 5215-5223] has questioned the importance of mitochondrial acetyl-CoA hydrolase for the formation of free acetate [Grigat et al. (1979) Biochem. J. 177, 71-79] under physiological conditions. Therefore this problem has been reevaluated by comparing various properties of the two enzymes. Cold-labile cytosolic acetyl-CoA hydrolase bands with an apparent Mr of 68000 during SDS/polyacrylamide gel electrophoresis, while the native enzyme elutes in two peaks with apparent Mr of 136000 and 245000 during gel chromatography in the presence of 2 mM ATP. The mitochondrial enzyme elutes under the same conditions with an apparent Mr of 157000. Under conditions where the cold-labile enzyme binds strongly to DEAE-Bio-Gel and ATP-agarose, the mitochondrial enzyme remains unbound. The cold-labile enzyme can be activated 14-fold by ATP, half-maximal activation occurring already at 40 microM ATP. AdoPP[NH]P, AdoPP[CH2]P and GTP have a similar though weaker effect. ADP as well as GDP can completely inhibit the cold-labile enzyme with 50% inhibition occurring for both nucleotides at about 1.45 microM. The binding of ATP and ADP is competitive. Acetyl phosphate and pyrophosphate have no effect on the activity of the cold-labile enzyme. The mitochondrial acetyl-CoA hydrolase is not affected by these nucleotides. CoASH is a strong product inhibitor (approximately equal to 80% inhibition at 40 microM CoASH) of the cold-labile enzyme, but only a weak inhibitor of the mitochondrial enzyme. Under in vivo conditions the activity of the cold-labile cytosolic acetyl-CoA hydrolase can be no more than 7% of the activity calculated for mitochondrial acetyl-CoA hydrolase under the same conditions. Accordingly the mitochondrial enzyme seems to be mainly responsible for the formation of free acetate by the intact liver, especially in view of the fact that the substrate specificity of the mitochondrial enzyme is much higher (activity ratios acetyl-CoA/butyryl-CoA 4.99 and 1.16 for the mitochondrial and the cold-labile enzyme respectively). Alloxan diabetes neither increased the activity of the cold-labile enzyme nor that of the mitochondrial enzyme. No experimental support has been found yet for the hypothesis that the acetyl-CoA hydrolase activity of the cold-labile enzyme represents the side-activity of an acetyl-transferase.
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PMID:On the regulation of cold-labile cytosolic and of mitochondrial acetyl-CoA hydrolase in rat liver. 285 46

Investigations were carried out to clarify the role of autoimmune phenomena in the pathogenesis of cataract in the adult human lens. Studies were carried out to determine the presence of serum antibodies to lens protein in patients with senile cataract, in patients with diabetes mellitus with and without cataract, and in healthy adult controls using the interfacial test and the gel-diffusion technique. Non-specific antibodies were removed by adsorption of sera with homogenized rat liver. A high proportion of healthy adults was found to have anti-lens protein antibodies (44.4% by the gel-diffusion method). In contrast, patients with cataract and diabetic patients with no cataract demonstrated double this incidence (82% and 80%), while all diabetic patients with cataract showed the presence of antibodies (P = 0.0002). The possible causes for the development of lens antibodies in normal healthy humans are discussed. Also, the causes for the higher incidence of lens antibodies in patients with cataract and in diabetic subjects with no clinical evidence of cataract are considered in relation to cataract formation. Homogenates of cataractous lenses when investigated revealed the presence of both IgG and IgM immunoglobulins, the former probably to a greater extent. Fluorescent microscopy on cryosections of senile and diabetic cataractous lenses revealed the presence of immunoglobulins within the lens. The antigen in the immune complexes isolated from homogenized cataractous lenses was characterized by the SDS-polyacrylamide gel electrophoresis method. A single band was consistently obtained and the molecular weight of the protein was estimated to be between 35,000 and 40,000. The strong possibility of auto-antibodies to lens protein being of aetiological significance in the pathogenesis of cataract is discussed.
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PMID:The role of autoimmune phenomena in the pathogenesis of cataract. 311 83

The antibacterial activity against Escherichia coli K 12 in 153 samples of amniotic fluid (AF) in 15 to 40 weeks of pregnancy were investigated by a new micromethod. Fifty-six mothers had an uncomplicated pregnancy while various complications (maternal diabetes, cholestasis of pregnancy, pregnancy induced hypertension, blood group isoimmunization and fetal growth retardation) were present in 97 cases. A significant (p less than 0.001) improvement of antibacterial activity was observed with advancing pregnancy. The highest antibacterial activity in AF was observed in cases with intrauterine growth retardation. In other respects the effect of various diseases was negligible.
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PMID:Antibacterial capacity in amniotic fluid in normal and complicated pregnancies. 331 Aug 22

Previous studies have shown that several factors--such as alloxan-induced diabetes, adrenalectomy, or removal of the thyroid-parathyroid gland complex--can influence the flow rate, protein concentration, and protein composition of rat parotid saliva. The present study was undertaken to explore further the influence of glucocorticoids and thyroxine on rat parotid saliva in hormonally intact animals. As compared with untreated animals, adult male rats treated with 10 micrograms dexamethasone per 100 g body weight for eight days demonstrated a 75% reduction in volume of parotid saliva secreted in response to a uniform stimulus. The protein concentration of the saliva was increased three-fold. Sodium dodecyl sulfate polyacrylamide gel electrophoresis showed relative decreases in acidic and basic proline-rich proteins and in a protein identified as Fraction V, while amylase was increased. The electron microscopic appearance of the granules was markedly different from that of the control, in that the granules exhibited an electron-dense periphery and core, with the remainder of the granule having an electronlucent appearance. In contrast, rats treated for eight days with 20 micrograms thyroxine per 100 g body weight exhibited a 50% increase in volume of saliva collected in response to a secretory stimulus. Although the concentration of protein was not different from that of the control, gel electrophoresis showed relative increases in acidic and basic proline-rich proteins and a decrease in Fraction V. Amylase was unchanged. The secretory granules of thyroxine-treated rats were electronlucent and amorphous. The granules appeared to coalesce within the cell.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Regulation of salivary proteins. 347 73


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