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)

Alkaline phosphatase activity of rat serum was reduced 50% by fasting the animal for 24 hours. Diabetes, induced by alloxan or streptozotocin, increased serum alkaline phosphatase 3- to 5-fold in fed rats and the elevated activity was reduced by insulin administration. In the absence of insulin, fasting alone was able to reduce the serum alkaline phosphatase of diabetic rats to control values. The elevated serum isozyme was found to be of intestinal origin by the use of appropriate inhibitors and electrophoretic mobility following neuraminidase treatment. It is concluded that food intake, particularly the hyperphagia of diabetes, plays a major role in regulating the concentration of intestine and serum alkaline phosphatase in the rat.
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PMID:Effects of experimental diabetes and food intake on rat intestine and serum alkaline phosphatase. 62 74

The intracisternal administration of insulin (0.2 U./kg.) to anesthetized dogs resulted in an increase of arterial immunoreactive insulin and a decrease of plasma glucose relative to a control injection. The arterial responses were significantly attenuated when the insulin was administered to the cisternum of subdiaphragmatically vagotomized dogs. When cerebrospinal fluid glucose was lowered by injecting pneumococcal neuraminidase intracisternally, no peripheral hyperinsulinemia resulted, indicating that increased spinal fluid insulin and its consequent increase of glucose uptake, rather than decreased spinal fluid glucose, is necessary to elicit the vagally mediated insulin secretion and hypoglycemia. It is hypothesized that increased spinal fluid insulin causes an increased glucose uptake of some glucoregulatory area of the brain and that the elicited reflex is vagally mediated pancreatic insulin secretion.
Diabetes 1975 Oct
PMID:Effect of intracisternal insulin on plasma glucose and insulin in the dog. 110 Apr 59

Rat kidney sialidase levels have been reported to be markedly altered in pathological states such as diabetes. This was associated with a modification of sialic acid levels. Therefore, it was interesting to study the variations of kidney sialidase and sialyltransferase activities and sialic acid content according to sex and age. This was carried out from birth to 210 days of age. The substrates used were sialyl alpha(2-3)[3H]-lactitol for sialidase activity, asialofetuin and [14C]-CMPNeu5Ac for sialyltransferase activity. In males sialidase activity increased until 32 days then slightly declined. In females, the activity increased and leveled off at 135 days of age. Higher sialidase activity was observed in females than in males from 56 days of age. Gonadectomy had no effect on this activity. In both sexes, sialyltransferase activity decreased markedly with age. This activity was higher in females than in males, whereas sialic acid levels varied only moderately with age and were slightly higher in females.
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PMID:Sex and age dependence of rat kidney sialidase. 130 56

We adapted the electrophoretic method of bone alkaline phosphatase (ALP) determination using neuraminidase from Vibrio cholerae to separate bone and liver ALP on cellulose acetate membrane. Treatment of separator plus serum (1:8, neuraminidase 111 U/l in final) for 10 min at room temperature (25 +/- 1 degree C) and subsequent electrophoresis made it possible to quantify bone ALP activity simply and rapidly. The precision of the data was at the level of CV of 1.6% (within-day) and 4.7% (day-to-day), with recovery rates of 97-103%. The normal range of bone ALP activity depended on age and sex. Seventy-eight diabetes mellitus (DM) patients, excluding those with renal failure, were divided into two groups of those with and without osteopenia with matching of age (+/- 3 years) and sex. Bone ALP (P < 0.001) and total ALP (P < 0.05) activities and urine calcium/creatinine ratio (P < 0.05) were significantly higher in DM with osteopenia than in DM without osteopenia. Therefore, bone formation and absorption may be accelerated in DM with osteopenia in comparison with DM without osteopenia.
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PMID:Cellulose acetate electrophoretic determination of bone alkaline phosphatase activity in healthy subjects and diabetic patients with and without osteopenia. 142 53

Diabetes is accompanied by impaired platelet function and accelerated vascular disease. To find out whether a correlation exists between these two complications, and if modifications occurring in diabetic platelets influence their relationship with endothelium, we have studied the interaction between platelets isolated from plasma of diabetic patients and bovine valvular endothelial cells (VEC), in culture. For quantitative analysis, normal and diabetic [3H]-adenine-labeled platelets were incubated with confluent VEC grown in Dulbecco's modified Eagle medium, containing 4.5 g/l glucose, for 30 min at 37 degrees C. After extensive washing and solubilization of the monolayer, the calculated adhesion index showed a two-fold increased adherence of diabetic platelets to VEC as compared to normal platelets. Statistical analysis (by Pitman randomization test) indicated that the adhesion was significantly higher (p = 0.0003) than that of normal platelets to VEC. To partially identify the membrane components implicated in the adhesion process, either platelets or VEC were treated with neuraminidase, trypsin or heparinase prior to the adhesion assay. Trypsin or neuraminidase treatment of platelets significantly diminished their adherence to VEC, suggesting a role of platelets sialylated glycoproteins in the adhesion process. Neuraminidase or heparinase treatment of VEC increased the adhesion of both normal and diabetic platelets, indicating that the cell membrane sialyl residues and heparan sulfate participate in the normal thromboresistant properties of VEC. Transmission and scanning electron microscopy revealed a close apposition between platelets and VEC with the formation of an adhesion plaque, characterized by fine fibrillar bridges between the plasma membranes of the two cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Increased adhesion of human diabetic platelets to cultured valvular endothelial cells. 145 40

We investigated the prevalence and characteristics of intestinal alkaline phosphatase (ALP; EC 3.1.3.1) identified in human serum by cellulose acetate electrophoresis in 8% of fasting serum samples from hospital patients (n = 500) and in 35% of fasting serum samples from patients with diabetes mellitus (n = 106; not differentiated between types 1 and 2). The intestinal ALP electrophoretic band was usually heterogeneous and contained two major subtypes of ALP. Isoelectric focusing of intestinal-ALP-positive serum treated with levamisole and neuraminidase (EC 3.2.1.18) revealed two distinct regions of enzymatic activity that comigrated with ALP extracted from small intestinal and colonic mucosa. Anodic intestinal ALP was resistant to treatment with levamisole and neuraminidase and comigrated with ALP from small intestinal mucosa. The more-cathodic intestinal ALP, which comigrated with ALP from colonic mucosa, was completely inhibited by levamisole and converted by neuraminidase to a species with a more basic pI than that of neuraminidase-digested tissue-nonspecific form. This component of intestinal ALP may be of vascular origin.
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PMID:Prevalence and properties of the intestinal alkaline phosphatase identified in serum by cellulose acetate electrophoresis. 156 15

We investigated by enzyme electrophoresis after prolonged neuraminidase treatment the activity of "intestinal variant" (alpha 2-globulin mobility) alkaline phosphatase (EC 3.1.3.1; ALP) in the plasma of 189 patients selected for disorders (diabetes mellitus, liver cirrhosis, and chronic renal failure) with a known high frequency of increased plasma intestinal (beta-globulin mobility) ALP activity. The overall frequency of the variant ALP was 23.8%, whereas in the samples showing intestinal ALP it was 45.0%. The variant ALP was not observed in the absence of intestinal ALP, nor in patients of blood group A. Its frequency did not differ significantly between the different patient groups. Quantification of the variant ALP by densitometry was unsatisfactory but the quantity could be estimated by subtracting the intestinal ALP activity measured by electrophoresis from the activity determined by immunoassay with monoclonal antibody that reacts with both the intestinal and the variant forms. This indicated median activity of 12 U/L for the variant, approximately equal to that of the concomitant intestinal ALP. From the effects of papain and bromelain treatments, we suggest that "intestinal variant" represents intestinal ALP with attached membrane-binding domain.
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PMID:Intestinal variant alkaline phosphatase in plasma in disease. 170 Jul 41

We assessed the heterogeneity in the islet cell cytoplasmic antibody (ICA) response of insulin-dependent diabetes mellitus (IDDM) patients via indirect immunofluorescence on frozen sections of human, bovine, and porcine pancreas. The three substrates detected comparable frequencies of ICA positives among the IDDM sera tested, whereas control sera were ICA negative on all three substrates. However, individual IDDM serum samples showed heterogeneity in ICA binding on the three pancreata. Of 28 sera tested on all three substrates, 22 were ICA positive on human pancreas, three were ICA positive on bovine pancreas, and two were ICA positive on porcine pancreas. Sensitivity of ICA epitopes to neuraminidase treatment and periodate oxidation suggests that glycoconjugates are recognized by serum ICA. Cholera toxin blocked ICA binding. However, the functional cholera toxin receptor ganglioside Gm1 is resistant to neuraminidase treatment and periodate oxidation. Therefore, it is unlikely that Gm1 is the ICA determinant. These data suggest that not all ICA antigens are equivalently expressed on islets from different pancreata and/or that each individual responds to a hierarchy of islet antigens such that restricted patterns of specific ICA binding are found.
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PMID:Heterogeneity in the specificity of the islet cell cytoplasmic antibody response in insulin-dependent diabetes mellitus. 170 23

The IgG from a patient (Italy 2 [I2]) with hypoglycemia, due to autoantibodies to the insulin receptor, was purified on protein A Sepharose into two fractions that were tested in various human tissues and cells. The IgG fraction that bound protein A (absorbed IgG [IgGa]) nearly completely inhibited the binding of 125I-labeled insulin to various cells or tissues (placenta, IM-9, adipocytes, HEp-2-larynx cells, Epstein-Barr virus lymphocytes) but not greater than 50% of 125I-labeled insulin binding to human liver membranes. Conversely, both the IgG fraction from this patient, which did not bind protein A (flow-through IgG [IgGb]), and the IgGa fraction from a second similar patient (Italy 1 [I-1]) almost completely inhibited the binding of 125I-labeled insulin to liver membranes. The IgGa fraction from patient I-2 did not change receptor affinity because 50% inhibition of 125I-labeled insulin binding was not affected by either the presence or absence of these IgG fractions. Furthermore, liver binding data were not due to cross-reaction of 125I-labeled insulin to the insulinlike growth factor I receptor, and treatment of liver membranes with neuraminidase did not alter the inhibitory effect of the IgGa fraction from patient I-2 on 125I-labeled insulin binding to liver. Binding inhibition experiments performed with cells transfected with and overexpressing the -12 (human insulin receptor [HIR]-A) or the +12 (HIR-B) variant of HIR revealed that the IgGa fraction from patient I-2 inhibited 125I-labeled insulin binding to the HIR-A receptor but not to the HIR-B receptor.(ABSTRACT TRUNCATED AT 250 WORDS)
Diabetes 1992 Jan
PMID:Evidence that two naturally occurring human insulin receptor alpha-subunit variants are immunologically distinct. 172 40

We have studied a combined effect of glycosylated low density lipoproteins (LDL) on the cholesterol content of cells cultured from unaffected human aortic intima. Native LDL did not alter the intracellular cholesterol level while glycosylated LDL taken in the concentration of 50 and 100 mg/ml increased the cell cholesterol content by 30 and 70 percent, respectively. The effect of the same concentrations of glycosylated LDL treated with neuraminidase (desialylated-glycosylated LDL) was twice as powerful. Desialylated LDL in the concentration of 50 and 100 mg/ml raised the cholesterol level by 1.4- and 2.1-fold, respectively. Simultaneous incubation of cells with glycosylated (50 mg/ml) and desialylated (50 mg/ml) LDL brought about a 3.4-fold increase in intracellular cholesterol. The obtained data suggest that intensive development of atherosclerosis in diabetes mellitus may be partially explained by synergic effects of desialylated and glycosylated lipoproteins as well as LDL with both types of modification.
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PMID:[Combined effects of desialylated and glycosylated low density lipoproteins on lipid content of human aortic intima cells in vitro]. 174 69


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