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)

Early morning urine specimens were obtained from two groups of non-insulin dependent diabetic patients and a group (43 subjects) of normal controls. The diabetic patients were divided into two subgroups according to the degree of diabetic control as judged by their glycosylated haemoglobin (HbA1) levels (well-controlled, 47 subjects; poorly controlled, 51 subjects). The concentration of the low-molecular-weight enzyme (lysozyme) was determined in each urine specimen and related to the concentration of creatinine (lysozyme/creatinine). The mean urinary lysozyme concentration was higher in each of the two diabetic groups as compared with the control group. However, it was not significantly different between the two diabetic groups. These result suggest that there is no association between the degree of glycaemic control and tubular proteinuria.
Diabetes Res Clin Pract 1994 Nov
PMID:Low-molecular-weight (tubular) proteinuria is not related to glycaemic control in non-insulin dependent diabetes mellitus. 787 44

Secretory immunoglobulin A, lactoferrin, lysozyme and tear specific pre-albumin were analyzed in stimulated tear fluid of 25 diabetic patients without retinopathy and in 29 diabetic patients with (pre) proliferative retinopathy using high performance liquid chromatography. Results were compared to those obtained in 26 healthy controls to determine the effect of diabetes mellitus on the exocrine function of the main lacrimal gland. Sodium dodecyl sulfate polyacrylamide gel electrophoresis onto minigels was performed on 20 tear samples for verification of high performance liquid chromatography fractions recorded. The mean total protein values in tear fluid (Bradford assay) of diabetics without retinopathy, with retinopathy and healthy controls did not differ significantly (mean in mg/ml +/- SD: 6.4 +/- 2.2, 5.9 +/- 2.0 and 5.7 +/- 1.7, respectively; Mann-Whitney; p > 0.02). High performance liquid chromatography showed an increased secretory immunoglobulin A and decreased peak 5 OD280 (+56% and -38%, respectively; p < 0.02) in patients without retinopathy, whereas in patients with retinopathy lysozyme was increased (+27%; p < 0.01) and tear specific pre-albumin and peak 5 OD280 decreased (-24% and -42%, respectively; p < 0.04), when compared to healthy controls. These inconsistent differences do not uniformly suggest an exocrine dysfunction of the main lacrimal gland in diabetic patients.
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PMID:Analysis of tear fluid proteins in insulin-dependent diabetes mellitus. 797 68

The sialochemical parameters total protein, immunoglobulin A, lysozyme, amylase, sodium, potassium, calcium as well as flow rate were estimated in parotid saliva (PS) and submandibular saliva (SMS) in the course of differential diagnostics of salivary gland diseases. In addition to this the quantitative polyacrylamide gel electrophoresis based on 80 PS and 80 SMS normal secretions was performed. Sialochemistry was performed on parotid adenomas (29), carcinomas (9); sialadenosis (8); acute (8) and chronic (13) sialadenitis; dental caries (12 PS and 12 SMS); cystic fibrosis (21 PS and 12 SMS); diabetes mellitus (13 PS and 13 SMS); and hyperthyroilism (9 PS and 9 SMS). Our sialochemical analysis does not allow to distinguish between benign and malignant parotid neoplasms. The significant decrease of sodium in sialadenosis and increase of sodium and total protein in sialadenitis as well as interesting results in cystic fibrosis, diabetes mellitus and dental caries, are emphasised.
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PMID:[Sialochemical studies of isolated secretions of the major salivary glands of the head]. 798 22

Significant advances were made this year in the understanding of serum amyloid A isotypes and in the definition of different amyloid light-chain proteins. Increasing numbers of hereditary amyloid-related transthyretin mutations have been reported (more than 30 to date). Two new hereditary amyloid proteins in several different kinships have appeared, ie, fibrinogen A alpha and lysozyme, each with a single point mutation. Both were found in patients with non-neurogenic hereditary amyloidosis with severe nephropathy. In islet amyloid polypeptide, the amyloid of adult-onset diabetes, the amino-acid sequence Ala-Ile-Leu-Ser at positions 25 to 28 appears to be critical for fibrillogenesis.
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PMID:Proteins of the systemic amyloidoses. 803 80

Pentosidine is a fluorescent protein cross-link and glycoxidation marker for the advanced glycation reaction in diabetes, aging, and uremia. We raised polyclonal antibodies in New Zealand White rabbits against this hapten coupled to keyhole limpet hemocyanin. The antibodies detected by ELISA reacted strongly with free pentosidine but not with pentosidine-like compounds. The working range of the competitive ELISA for standard pentosidine was 0.1-100 pmol. Pentosidine was detectable in bovine serum albumin incubated with ribose as a function of incubation time. Immunoblotting studies showed that pentosidine specifically stained in oligomers of lysozyme incubated with ribose. Digestion with protease (Pronase E, 20 g/kg) as well as acid hydrolysis enhanced the immunoreactivity of samples, the pentosidine values in digested human plasma correlating with those measured by HPLC (r = 0.98). Pentosidine in diabetic and uremic plasma digested with Pronase E was significantly higher than normal (P < 0.01; mean +/- SD): 1620 +/- 1940 and 2630 +/- 1320 [corrected] nmol/L, respectively, vs 151 +/- 55 nmol/L (normal). Amounts of pentosidine in hydrolyzed skin collagen increased with age and were increased in diabetes and uremia. This ELISA provides a new tool for assessing the role of the advanced Maillard reaction in aging and age-related diseases.
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PMID:ELISA of pentosidine, an advanced glycation end product, in biological specimens. 807 89

Macrophages are present in the initial phase of the autoimmune process involved in the destruction of the endocrine pancreas in IDDM via the secretion of cytokines such as IL-1 beta. Macrophages also secrete lysozyme. Besides its action on the bacterial cell wall, lysozyme has an important physiological and immunological role. Human lysozyme is an in-situ modulator of the inflammatory reactions. We investigate the protective role of human lysozyme in vitro against the cytotoxic effect of IL-1 beta or of IL-1 beta combined with IFN-gamma on isolated rat islets. Precultured newborn rat islets were incubated with human or chicken lysozyme (50.000 U/ml) over 3 days. Human IL-1 beta (100 U/ml) or IL-1 beta (5 U/ml) + INF-gamma (100 U/ml) was added for the last 2 days and tritiated thymidine for the last 24 hrs. In another set of experiments, islets were exposed simultaneously to human lysozyme and IL-1 beta. Only pretreatment with human lysozyme abolished the lowering of the labelling index of the islet cell induced by IL-1 beta or by IL-1 beta and INF-gamma. Pycnotic nuclei were abundant in islets treated with IL-1 alone while they were not when islets were pretreated with human lysozyme. Chicken lysozyme had no protective effect in the same protocol. Human lysozyme was not protective when applied simultaneously with IL-1. Pretreatment of the islets by human lysozyme does not prevent the reduction of the insulin secretion induced by IL-1 beta. Human and chicken lysozyme differ further in their action when tested on fibroblasts proliferation. Only human lysozyme stimulates the latter. In conclusion, only human lysozyme seems to have a protective effect against the cytotoxicity of IL-1 in combination or not with IFN-gamma on islet cells in vitro. Moreover, to be protected, the islets have to be pretreated with lysozyme before the IL-1 application. Our in vitro results imply that natural aspecific immunity and its relation to the secretory function of the macrophage might be crucial for the prevention of the initial assault responsible for the onset of the immune process leading to insulin dependent diabetes.
Diabetes Res Clin Pract 1994 Mar
PMID:Prevention of the cytotoxic effect of IL-1 by human lysozyme on isolated rat islets. 807 Mar 6

How peptide-major histocompatibility complex (MHC) class II complexes are naturally generated is still unknown, but accumulating evidence suggests that unfolding proteins or long peptides can become bound to class II molecules at the dominant determinant before proteolytic cleavage. We have compared the immunogenicity of hen egg-white lysozyme (HEL) in nonobese diabetic (NOD), (NOD x BALB/c)F1, and E(d) alpha transgenic NOD mice. We find that a response to the subdominant ANOD-restricted determinant disappears upon introduction of an E(d) molecule, and is restored when scission of HEL separates this determinant from its adjoining, competitively dominant, E(d)-restricted determinant. This suggests that the E(d) molecule binds and protects its dominant determinant on a long peptide while captured neighboring determinants are lost during proteolysis. These results provide clear evidence for "determinant capture" as a mechanism of determinant selection during antigen processing and a possible explanation for MHC-protective effects in insulin-dependent diabetes mellitus.
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PMID:Determinant capture as a possible mechanism of protection afforded by major histocompatibility complex class II molecules in autoimmune disease. 822 14

The salivary composition and flow rate were examined in 20 patients with insulin-dependent diabetes mellitus (IDDM) and in 19 patients with non-insulin-dependent diabetes mellitus (NIDDM) and compared with 20 healthy controls. Resting and stimulated whole and submandibular saliva was analyzed. Significantly lower resting salivary flow rates were found in the IDDM patients as compared to the NIDDM group. In the IDDM patients potassium concentration in resting saliva was significantly higher compared with healthy controls and in stimulated whole saliva compared with NIDDM patients. No difference in salivary total protein, amylase, lactoferrin, or lysozyme was found among the three groups examined. The IgA concentration of the IDDM patients was significantly higher in whole resting saliva compared with controls and in the submandibular saliva compared with both NIDDM patients and controls. No difference was found between controls and the diabetic patients examined in prevalence of complaint of dry mouth. The salivary flow rates, however, were significantly lower in the three subgroups with dry mouth compared with the subgroups without this complaint. Caries were detected in 100% of the diabetic patients and controls. No correlation was observed between the incidence of caries and any of the salivary parameters examined. A higher prevalence and severity of periodontal disease was detected in the diabetic patients as compared to the controls. A significant positive correlation was found between the gingival index and the concentrations of total protein, albumin, lysozyme, and lactoferrin in whole resting saliva in the three groups examined.
J Diabetes Complications
PMID:Oral health and salivary composition in diabetic patients. 848 52

1. The effects of AL0671, a novel potassium channel opener, on protein glycation and low-density lipoprotein (LDL) oxidation were tested. 2. AL0671 dose-dependently inhibited both fluorescence development of bovine serum albumin and cross-linking of lysozyme. These inhibitory effects for glycation were no less potent than aminoguanidine. 3. AL0671 dose-dependently inhibited both increase in negative charge and apo B-100 fragmentation during incubation of LDL with Cu2+. In addition, AL0671 significantly decreased the LDL degradation in rat peritoneal macrophages. 4. Neither pinacidil nor levcromakalim inhibited protein glycation and LDL oxidation. 5. Antioxidant properties of AL0671 might be due to its potent electron-donating ability, and this agent is expected to be useful for hypertensive diabetes.
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PMID:AL0671, a new potassium channel opener, inhibits nonenzymatic glycation of protein and LDL oxidation. 891 39

One hundred and thirty-one patients with diabetes mellitus type 1 (IDDM) and 20 healthy controls were checked for the presence of periodontal diseases and for some oral microbiological parameters. Results demonstrated that IDDM patients, who were well compensated from both the metabolic and clinical point of view, showed a prevalence for periodontopathies, which only differed slightly from controls. Only the presence of gingivitis was significantly higher in IDDM patients than in healthy subjects. Both anaerobic and aerobic microbial flora did not show substantial differences for either group. Among the salivary antibacterial factors studied, lysozyme was significantly decreased in diabetic patients compared to controls. It is concluded that IDDM patients undergo periodontal complications with a frequency quite close to that of non-diabetic healthy subjects, when the disease is under strict metabolic and clinical control.
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PMID:Periodontal disease, oral microbial flora and salivary antibacterial factors in diabetes mellitus type 1 patients. 898 24


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