muramidase and Diabetes-Mellitus

Topics: Albumins; Amylases; Calcium; Chlorides; Diabetes Mellitus; Eye Diseases; Female; Globulins; Glucose; Humans; Hydrogen-Ion Concentration; Lipids; Magnesium; Male; Manganese; Muramidase; Oxidoreductases; Phosphates; Phosphoric Monoester Hydrolases; Potassium; Proteins; Sodium; Tears; Zinc

Attaining a good glycaemic control is usually the target for therapy in diabetic patients as this is expected to prevent both acute and chronic complications. Oral infections are however very common among diabetic patients despite the presence of many immunologic proteins in the saliva. This study was designed to determine the impact of glycaemic control on levels of these proteins in diabetic patients.. Salivary lysozyme, histatins, immunoglobulin A and immunoglobulin G were measured in diabetic patients. The levels of these immunologic proteins were compared between patients whose HbA1c were less than 7% and those whose values were greater than or equal to 7%.. A total of 95 participants were recruited for this study with 37 (38.9%) of them having a median HbA1c of 6.3% (IQR 5.3- 6.6) and the remaining 58 (61.1%) having a median HbA 1c of 9.1% (IQR 8.1-10.5). There was no significant difference in salivary lysozyme (31.24 vs 33.77 ng/ml; p = 0.69), histatins (9.65 vs 9.17 ng/ml; p = 0.27), IgA (12.79 vs 12.19 μg/ml; p = 0.16) and IgG (31.29 vs 32.49 μg/ml; p = 0.85) between the group with good and those with poor glycaemic control.. This study showed that glycaemic control does not impact the levels of salivary immunologic proteins in diabetic patients, so quality attention should be given to oral care to avoid the development of oral complications.. L'obtention d'un bon contrôle glycémique est généralement l'objectif du traitement des patients diabétiques, car il est censé prévenir les complications aiguës et chroniques. Les infections buccales sont cependant très fréquentes chez les patients diabétiques malgré la présence de nombreuses protéines immunologiques dans la salive. Cette étude a été conçue pour déterminer l'impact du contrôle glycémique sur les niveaux de ces protéines chez les patients diabétiques.. Le lysozyme, les histatines, l'immunoglobuline A et l'immunoglobuline G salivaires ont été mesurés chez les patients diabétiques. Les niveaux de ces protéines immunologiques ont été comparés entre les patients dont le HbA1c était inférieur à 7 % et ceux dont les valeurs étaient supérieures ou égales à 7 %.. Au total, 95 participants ont été recrutés pour cette étude, 37 (38,9 %) d'entre eux ayant une HbA1c médiane de 6,3 % (IQR 5,3- 6,6) et les 58 autres (61,1 %) ayant une HbA1c médiane de 9,1 % (IQR 8,1- 10,5). Il n'y avait pas de différence significative dans le lysozyme salivaire (31,24 vs 33,77 ng/ml ; p= 0,69), les histatines(9,65 vs 9,17 ng/ml ; p= 0,27), les IgA (12,79 vs 12,19 ?g/ml ; p= 0,16) et les IgG (31,29 vs 32,49 ?g/ml ; p= 0,85) entre le groupe avec un bon et celui avec un mauvais contrôle glycémique.. Cette étude a montré que le contrôle glycémique n'a pas d'impact sur les niveaux de protéines immunologiques salivaires chez les patients diabétiques, une attention de qualité devrait donc être accordée aux soins bucco-dentaires pour éviter le développement de complications orales.. Diabète, Contrôle glycémique, Protéines salivaires, Cavité orale, Protéines immunologiques.

Topics: Antiviral Agents; Diabetes Mellitus; Glycated Hemoglobin; Glycemic Control; Histatins; Humans; Immunoglobulin A; Immunoglobulin G; Muramidase

The reactive α-oxoaldehyde, methylglyoxal reacts with different proteins to form Advanced Glycation End Products (AGEs) through Maillard reaction. Its level increases significantly in diabetic condition. Here, we have investigated the effect of different concentrations of methylglyoxal (200-400 µM) on the monomeric protein, hen egg white lysozyme (HEWL) following incubation for 3 weeks. Reaction of methylglyoxal with HEWL induced considerable changes in tertiary structure of the protein, but no significant alteration in secondary structure, as evident from different spectroscopic and biophysical studies. Interestingly, methylglyoxal modification was found to enhance the thermal stability of the protein and reduce its sensitivity to stress-induced aggregation. Finally, peptide mass fingerprinting revealed modification of arginine (Arg-45, Arg-14, Arg-68 or Arg-72) and lysine (Lys-116) residues of the protein to AGE adducts, namely, hydroimidazolone, tetrahydropyrimidine, and carboxyethyllysine. Methylglyoxal-derived AGE adducts (MAGE) appear to be responsible for the observed changes in protein. As demonstrated in the present study, the findings may highlight a possible therapeutic potential of the α-oxoaldehyde against protein misfolding and conformational disorder.Communicated by Ramaswamy H. Sarma.

Topics: Diabetes Mellitus; Egg White; Glycation End Products, Advanced; Maillard Reaction; Muramidase; Protein Folding; Pyruvaldehyde

More than 20 unique diseases such as diabetes, Alzheimer's disease, Parkinson's disease are caused by the abnormal aggregations of pathogenic proteins such as amylin, β-amyloid (Aβ), and α-synuclein. All pathogenic proteins differ from each other in biological function, primary sequences, and morphologies; however, the proteins are toxic when aggregated. Here, we investigated the cellular toxicity of pathogenic or non-pathogenic protein aggregates. In this study, six proteins were selected and they were incubated at acid pH and high temperature. The aggregation kinetic and cellular toxicity of protein species with time were characterized. Three non-pathogenic proteins, bovine serum albumin (BSA), catalase, and pepsin at pH 2 and 65 °C were stable in protein structure and non-toxic at a lower concentration of 1 mg/mL. They formed aggregates at a higher concentration of 20 mg/mL with time and they induced the toxicity in short incubation time points, 10 min and 20 min only and they became non-toxic after 30 min. Other three pathogenic proteins, lysozyme, superoxide dismutase (SOD), and insulin, also produced the aggregates with time and they caused cytotoxicity at both 1 mg/mL and 20 mg/mL after 10 min. TEM images and DSC analysis demonstrated that fibrils or aggregates at 1 mg/mL induced cellular toxicity due to low thermal stability. In DSC data, fibrils or aggregates of pathogenic proteins had low thermal transition compared to fresh samples. The results provide useful information to understand the aggregation and cellular toxicity of pathogenic and non-pathogenic proteins.

Topics: alpha-Synuclein; Alzheimer Disease; Amyloid beta-Peptides; Catalase; Cell Line; Diabetes Mellitus; Humans; Insulin; Islet Amyloid Polypeptide; Models, Molecular; Muramidase; Parkinson Disease; Pepsin A; Protein Aggregates; Protein Aggregation, Pathological; Protein Structure, Secondary; Serum Albumin, Bovine; Superoxide Dismutase

Glycation occurs in vivo as a result of the nonenzymatic reaction of carbohydrates (and/or their autoxidation products) with proteins, DNA, or lipids. Protein glycation causes loss-of-function and, consequently, the development of diabetic-related diseases. Glycation also boosts protein aggregation, which can be directly related with the higher prevalence of aggregating diseases in diabetic people. However, the molecular mechanism connecting glycation with aggregation still remains unclear. Previously we described mechanistically how glycation of hen egg-white lysozyme (HEWL) with ribose induced its aggregation. Here we address the question of whether the ribose-induced aggregation is a general process or it depends on the chemical nature of the glycating agent. Glycation of HEWL with glycolaldehyde occurs through two different scenarios depending on the HEWL concentration regime (both within the micromolar range). At low HEWL concentration, non-cross-linking fluorescent advanced glycation end-products (AGEs) are formed on Lys side chains, which do not change the protein structure but inhibit its enzymatic activity. These AGEs have little impact on HEWL surface hydrophobicity and, therefore, a negligible effect on its aggregation propensity. Upon increasing HEWL concentration, the glycation mechanism shifts toward the formation of intermolecular cross-links, which triggers a polymerization cascade involving the formation of insoluble spherical-like aggregates. These results notably differ with the aggregation-modulation mechanism of ribosylated HEWL directed by hydrophobic interactions. Additionally, their comparison constitutes the first experimental evidence showing that the mechanism underlying the aggregation of a glycated protein depends on the chemical nature of the glycating agent.

Topics: Acetaldehyde; Animals; Chickens; Diabetes Mellitus; Glycation End Products, Advanced; Glycosylation; Hydrophobic and Hydrophilic Interactions; Muramidase; Protein Conformation; Proteins; Spectrometry, Fluorescence; Surface Properties

To study a recombined chimeric peptide consisting of lysozyme N-terminal sequence and exendin-4 (shortly LYZ(N)-EX4) as a dual-action peptide for diabetes.. LYZ(N)-EX4 was recombined into plasmid pET-32a(+) and expressed in Escherichia coli. The fusion protein was separated by affinity chromatography and hydrolyzed by enterokinase to prepare LYZ(N)-EX4. The chimeric peptide was digested by thrombin and the digests were analyzed by HPLC. The secondary peptides were identified by mass spectrometry. Biological activities of the thrombin digests were determined in vitro, using NIT-1 cells for insulin promoting action and using human white blood cells (WBC) for anti-AGEs action.. The fusion protein was highly expressed in E. coli and LYZ(N)-EX4 was obtained via hydrolysis of the fusion protein. The thrombin digests of LYZ(N)-EX4 were separated by HPLC into two peaks, which were identified as LYZ(N) and EX4 by mass spectrametry. Functional studies found that the digests were able to antagonize the effects of AGEs on expression of RAGE mRNA in WBC, promote cell activity, stimulate PDX-1 mRNA expression and increase insulin secretion by NIT-1 cells, suggesting the actions of LYZ(N) and EX4 on the cells.. LYZ(N)-EX4 was sensitive to thrombin digestion, and the secondary peptides LYZ(N) and EX4 could function as anti-AGEs and insulin-promoting peptides, respectively.

Topics: Animals; Diabetes Mellitus; Escherichia coli; Exenatide; Humans; Hypoglycemic Agents; Insulin; Leukocytes; Mice; Muramidase; Peptides; Recombinant Proteins; RNA, Messenger; Thrombin; Venoms

Diabetes mellitus is characterized by hyperglycemia that plays an important role in the pathogenesis of diabetic complications including cardiovascular diseases. Moreover, hyperglycemia induces increased generation of advanced glycation end products (AGEs). The activation of platelets is associated with the development of cardiovascular diseases.. The question whether AGEs acutely induce platelet activation as a response to exogenous stimulus is addressed.. The effect of AGEs derived from food and human serum being purified by lysozyme affinity chromatography was examined by incubating in vitro freshly isolated blood platelets from fasted subjects at various concentrations and different time points. Platelet activation, determined as expression of surface markers CD62 and CD63, and the presence of the receptor for AGEs (RAGE) in platelet membranes was measured by flow cytometric analysis using specific antibodies.. Incubation with food-derived as well as serum-derived AGEs stimulated significantly the expression of CD62 up to 7.1-fold and CD63 up to 2.2-fold at the platelet surface membrane as a function of concentration and time. Incubation with thrombin or AGEs significantly increased RAGE expression twofold at the platelet surface membrane.. The increase in surface activation marker and RAGE expression in platelets, resulting from concentrations of AGEs that occur in vivo after a meal or a drink as a source of exogenous AGEs, points to signaling mechanisms for food AGEs that could favor the precipitation of acute postprandial ischemic events.

Topics: Adolescent; Adult; Aged; Antigens, CD; Biomarkers; Chromatography, Affinity; Diabetes Complications; Diabetes Mellitus; Female; Flow Cytometry; Glycation End Products, Advanced; Humans; Male; Middle Aged; Muramidase; Platelet Activation; Platelet Membrane Glycoproteins; Tetraspanin 30; Young Adult

Topics: Animals; Diabetes Mellitus; Glucose; Glycation End Products, Advanced; Humans; Lipid Bilayers; Models, Biological; Muramidase; Oxidative Stress; Oxygen; Pyridoxamine; Reactive Oxygen Species; Tryptophan

IDDM results from the destruction of pancreatic beta-cells by autoreactive T-cells that appear to avoid deletion early in development, possibly due to improper interaction with antigen-presenting cells (APCs) resident in the thymus or periphery. In the nonobese diabetic (NOD) mouse, there exists a defect in APC function characterized by its failure to fully mature upon stimulation. The NOD mouse thus provides an excellent model for the investigation of APC dysfunction and development and how these relate to the incidence of autoimmune diabetes. We initiated studies of APC function in the NOD mouse with respect to antigen processing and presentation, using a well-characterized antigen hen egg lysozyme (HEL) and comparing it with the closely related, major histocompatibility complex (MHC) (I-Ag7) identical, diabetes-resistant mouse strain NOR. Proliferation assays comparing NOD and NOR HEL-specific T-cells demonstrated that the T-cell proliferation response of the NOD mouse to both native and denatured forms of the antigen is lower than that of NOR. When crisscross proliferation experiments were conducted using purified T-cells and irradiated spleen cells as APCs from both strains, the results demonstrated that the defect in proliferation resided in the APC compartment of activation. The levels of intracellular glutathione (GSH) were compared in splenic macrophages from NOD and NOR mice; it was found that on antigenic stimulation, NOR macrophages produced significantly more intracellular GSH than did NOD macrophages, even under hyperglycemic (50 mmol/l glucose) conditions. The lower amount of GSH seen in the NOD may result in less efficient processing of antigen, and subsequently, lower levels of T-cell activation.

Topics: Animals; Antigen-Presenting Cells; Cell Division; Diabetes Mellitus; Epitopes; Glucose; Glutathione; Immunity, Innate; Intracellular Membranes; Macrophages; Male; Mice; Mice, Inbred NOD; Mice, Inbred Strains; Muramidase; Spleen; T-Lymphocytes

Obese human subjects have increased protein-tyrosine phosphatase (PTPase) activity in adipose tissue that can dephosphorylate and inactivate the insulin receptor kinase. To extend these findings to skeletal muscle, we measured PTPase activity in the skeletal muscle particulate fraction and cytosol from a series of lean controls, insulin-resistant obese (body mass index > 30) nondiabetic subjects, and obese individuals with non-insulin-dependent diabetes. PTPase activities in subcellular fractions from the nondiabetic obese subjects were increased to 140-170% of the level in lean controls (P < 0.05). In contrast, PTPase activity in both fractions from the obese subjects with non-insulin-dependent diabetes was significantly decreased to 39% of the level in controls (P < 0.05). By immunoblot analysis, leukocyte antigen related (LAR) and protein-tyrosine phosphatase 1B had the greatest increase (threefold) in the particulate fraction from obese, nondiabetic subjects, and immunodepletion of this fraction using an affinity-purified antibody directed at the cytoplasmic domain of leukocyte antigen related normalized the PTPase activity when compared to the activity from control subjects. These findings provide further support for negative regulation of insulin action by specific PTPases in the pathogenesis of insulin resistance in human obesity, while other regulatory mechanisms may be operative in the diabetic state.

Topics: Adult; Body Weight; Cell Fractionation; Chromatography, Gel; Deoxyglucose; Diabetes Mellitus; Diabetes Mellitus, Type 2; Humans; Immunoblotting; Insulin; Insulin Resistance; Middle Aged; Muramidase; Muscle, Skeletal; Obesity; Phosphoprotein Phosphatases; Phosphorylation; Protein Tyrosine Phosphatases; Receptor-Like Protein Tyrosine Phosphatases, Class 4; Receptor, Insulin; Receptors, Cell Surface; Substrate Specificity

We present a case of proliferative fasciitis arising adjacent to an operative scar of the right lower leg of a patient with chronic lymphatic leukemia, diabetes mellitus, and multiple subcutaneous angiolipomas. A 61-year old man had a hard mass in his right lower leg that had rapidly increased in size in the past 10 days. The mass was microscopically composed of a dense proliferation of spindle cells forming interlacing fascicles admixed with an inflammatory infiltrate of lymphocytes and eosionphils, focal hemorrhage, and myxomatous change as typically seen in nodular fasciitis as well as many characteristic ganglion cell-like giant cells. Immunohistochemically, most of the spindle-shaped cells were positive for vimentin and alpha-actin, whereas the ganglion cell-like giant cells were positive for vimentin and negative for alpha-actin and lysozyme. We suggest that the main component cells of proliferative fasciitis are fibroblastic in nature, many of which are myofibroblasts in large part, whereas the ganglion cell-like giant cells are related more closely to fibroblasts rather than histiocytes or pericytes. Additionally, proliferating cell nuclear antigen (PCNA) stain revealed that many of the fibroblastic cells showed high proliferative activity, especially in the hypercellular areas, although there was no significant difference in PCNA staining between the focus traumatized by the needle biopsy and the nontraumatized areas.

Topics: Actins; Angiolipoma; Biopsy, Needle; Cell Division; Cicatrix; Coloring Agents; Diabetes Mellitus; Eosinophils; Fasciitis; Fibroblasts; Giant Cells; Hemorrhage; Histiocytes; Humans; Immunohistochemistry; Leg Dermatoses; Leukemia, Lymphocytic, Chronic, B-Cell; Lymphocytes; Male; Middle Aged; Muramidase; Neoplasms, Multiple Primary; Proliferating Cell Nuclear Antigen; Skin Neoplasms; Vimentin

After a hyperglycaemic episode, glycated proteins remain in the body until removed by protein turnover. We have shown that in the absence of free sugar, such proteins can crosslink to native proteins, forming mixed dimers. They can also induce native proteins to crosslink into homodimers, presumably by release of a soluble crosslinking agent. Similar reactions in vivo could be responsible for the deposition of serum proteins in diabetic kidney, nerve and other tissues. Exposure to glycating sugar for brief periods, or a low concentration, still produced glycated protein capable of crosslinking to other proteins under sugar-free conditions. These crosslinks are nonfluorescent, unlike the advanced glycation endproducts usually observed.

Topics: Cross-Linking Reagents; Diabetes Mellitus; Electrophoresis, Polyacrylamide Gel; Female; Fructose; Glycation End Products, Advanced; Glycosylation; Humans; Hyperglycemia; Lactoglobulins; Macromolecular Substances; Muramidase; Spectrometry, Fluorescence

Why diabetes is associated with abnormally high susceptibility to infection remains unknown, although two major antibacterial proteins, lysozyme and lactoferrin, have now been shown to specifically bind glucose-modified proteins bearing advanced glycation end products (AGEs). Exposure to AGE-modified proteins inhibits the enzymatic and bactericidal activity of lysozyme, and blocks the bacterial agglutination and bacterial killing activities of lactoferrin. Peptide mapping revealed a single AGE binding domain in lysozyme and two AGE binding domains in lactoferrin; each domain contains a 17- to 18- amino acid cysteine-bounded loop motif (CX15-16C) that is markedly hydrophilic. Synthetic peptides corresponding to these motifs in lysozyme and lactoferrin exhibited AGE binding activity, and similar domains are also present in other antimicrobial proteins. These results suggest that elevated levels of AGEs in tissues and serum of diabetic patients may inhibit endogenous antibacterial proteins by binding to this conserved AGE-binding cysteine-bounded domain 'ABCD' motif, thereby increasing susceptibility to bacterial infections in the diabetic population.

Topics: Amino Acid Sequence; Animals; Anti-Infective Agents; Binding Sites; Conserved Sequence; Diabetes Mellitus; Glycation End Products, Advanced; Humans; Lactoferrin; Molecular Sequence Data; Muramidase; Protein Binding

Some urinary enzymes (NAG, AAP, lysozyme) considered to be sufficiently sensitive and reliable markers of renal damage were controlled in 20 patients with cirrhosis of the liver and in 20 healthy control subjects. The results, stated as mean +/- SD, showed a statistically very significant increase (p < 0.01) of NAG and lysozyme in cirrhotics. Furthermore, this increase could be at least in part related with the seriousness of clinical condition. On the basis of these results, we think the urinary dosage of NAG and lysozyme is, in the subjects with liver cirrhosis, a bloodless method to show an early renal damage.

Topics: Acetylglucosaminidase; Adult; Aged; Aged, 80 and over; Aminopeptidases; Ascites; Butyrylcholinesterase; CD13 Antigens; Clinical Enzyme Tests; Diabetes Mellitus; Female; Humans; Kidney Diseases; Liver Cirrhosis; Male; Middle Aged; Muramidase; Time Factors

Nonenzymatic glycation has been found to increase in a variety of proteins in diabetic patients. The present study examined a possibility of preventing glycation and subsequent structural modifications of proteins by alpha-lipoic acid (thioctic acid) as lipoate, a substance which has gained attention as a potential therapeutic agent for diabetes-induced complications. Incubation of bovine serum albumin (BSA) at 2 mg/ml with glucose (500 mM) in a sterile condition at 37 degrees C for seven days caused glycation and structural modifications of BSA observed by SDS-PAGE, near UV absorption, tryptophan and nontryptophan fluorescence, and fluorescence of an extrinsic probe, TNS (6-(p-toluidinyl)naphthalene-2-sulfonate). When BSA and glucose were incubated in the presence of lipoate (20 mM), glycation and structural modifications of BSA were significantly prevented. Glycation and inactivation of lysozyme were also prevented by lipoate. These results suggest a potential for the therapeutic use of lipoic acid against diabetes-induced complications.

Topics: Diabetes Mellitus; Glucose; Glycosylation; Humans; Muramidase; Serum Albumin, Bovine; Thioctic Acid

The potential value of eight commercial available polymer-based reversed-phase (RP) columns for peptide and protein separations was evaluated using crude acetic acid extracts of normal and diabetic human pancreata and mixtures of pure polypeptides as samples. All columns were characterized with acetic acid gradients in water as mobile phase, and different chromatographic profiles were obtained depending on the type of polymer column (bare or derivatized) and the type of ligand. Some of the columns were virtually free from effects related to the polymer skeleton whereas in others the separation was influenced by both the ligand and the polymeric backbone. Two selected polymeric RP columns were, together with a silica-based C4 column, further characterized with acetonitrile gradients in trifluoroacetic acid (TFA), and the separation temperature was found to have a drastic effect on the separation efficiency for proteins with mol. wt. greater than 6000 dalton. No such effect was seen for polypeptides with mol. wt. less than 6000 dalton. Mixtures of pure peptides and proteins were separated using acetic acid gradients in water, acetonitrile or isopropanol, and normally the highest efficiency was found with the use of acetonitrile as mobile phase modifier. Isopropanol was less suitable as an organic modifier. The separation of the beta-lactoglobulin A- and B-chains may be used to give a rapid estimate of the chromatographic usability of polymer-based RP-columns for peptide and protein separations in acetic acid gradients in water and in acetonitrile gradients. Recoveries for insulin, proinsulin, growth hormone, ovalbumin and human serum albumin were measured for several polymer-based RP columns eluted with acetic acid gradients in water and with acetonitrile-based mobile phases. The highest recoveries of serum albumin and ovalbumin were found after elution with acetic acid gradients in water.

Topics: Acetates; Acetic Acid; Acetonitriles; Chromatography, High Pressure Liquid; Diabetes Mellitus; Humans; Insulin; Lactoglobulins; Muramidase; Ovalbumin; Pancreas; Peptides; Polymers; Serum Albumin; Trifluoroacetic Acid

Topics: Diabetes Mellitus; Humans; Infusions, Intravenous; Muramidase; Serum Albumin

Topics: Adult; Aged; Diabetes Mellitus; Female; Humans; Male; Middle Aged; Muramidase; Skin

Topics: Adolescent; Adult; Child; Child, Preschool; Diabetes Mellitus; Female; Humans; Kidney Function Tests; Kidney Tubules; Male; Middle Aged; Muramidase; Radioimmunoassay

Reduced bacterial killing by polymorphonuclear leucocytes has been reported in patients with diabetes mellitus. Whether this is due to reduced content of bactericidal granular proteins has not been determined. We therefore immunochemically measured the content of myeloperoxidase, lactoferrin, lysozyme, cathepsin G and elastase in polymorphonuclear leucocytes from 50 insulin-treated diabetic patients. The peroxidase activity was also measured. Normal contents of myeloperoxidase and lactoferrin as well as normal peroxidase activity were found. The average contents of cathepsin G, elastase and lysozyme were 2.5, 3.2 and 2.6 micrograms/10(6) polymorphonuclear leucocytes, respectively, and thus 14, 45 and 18% higher than the contents of normal polymorphonuclear leucocytes. The results indicate that reduced intracellular killing of bacteria demonstrated in previous studies in diabetic patients does not appear to be related to a reduction in the content of bactericidal proteins.

Topics: Age Factors; Blood Bactericidal Activity; Cathepsin G; Cathepsins; Diabetes Mellitus; Humans; Lactoferrin; Muramidase; Neutrophils; Pancreatic Elastase; Peroxidase; Serine Endopeptidases; Time Factors

Topics: Blood Bactericidal Activity; Diabetes Mellitus; Humans; Muramidase; Phagocytosis

Topics: Diabetes Mellitus; Glucuronidase; Granuloma; Humans; L-Lactate Dehydrogenase; Muramidase; Necrobiosis Lipoidica

Neutrophil granulocyte chemotaxis and intraneutrophilic and plasma levels of lysozyme as well as the number of T and B lymphocytes and lymphocyte transformation in vitro on stimulation with mitogens and microbial antigens were studied in four groups of patients with diabetes mellitus (DM). Twelve patients with insulin-dependent diabetes mellitus (IDDM) and ketoacidosis and 4 patients with non-insulin-dependent diabetes mellitus were studied at the time of diagnosis and before and after start of treatment. Ten patients with IDDM of less than 10 years' duration which had been difficult to regulate well and 10 patients with IDDM well regulated for more than 20 years were studied at their regular outpatient visits. Apart from a slight increase in plasma lysozyme in group 1 from the first to the second examination, we found no differences between diabetics and healthy control persons. It is concluded that if patients with DM are more susceptible to infections, it is probably caused by elements of neutrophil or lymphocyte function not examined in this study or by factors unrelated to immunity.

Topics: Adolescent; Adult; Aged; B-Lymphocytes; Chemotaxis, Leukocyte; Diabetes Mellitus; Female; Humans; Leukocyte Count; Lymphocyte Activation; Lymphocytes; Male; Middle Aged; Muramidase; Neutrophils; T-Lymphocytes

Lysozyme activity was significantly reduced in the skin of patients with clinical diabetes, but not in the skin of other diabetics or in serum of all these patients. Sex and age had no influence on serum or skin lysozyme activity in either nondiabetic or diabetic subjects. The reduction of cutaneous lysozyme activity is suggested as a factor for the seriousness and the relapses of cutaneous infections in subjects with clinical diabetes.

Topics: Adult; Aged; Diabetes Complications; Diabetes Mellitus; Female; Humans; Male; Middle Aged; Muramidase; Recurrence; Skin; Skin Diseases, Infectious

Topics: Adult; Aged; Diabetes Mellitus; Female; Humans; Male; Middle Aged; Muramidase; Skin

The excretion of alanine aminopeptidase in the urine is changed by several factors influencing the tubuli. The diabetics increasedly excrete alanine aminopeptidase in the urine, apparantly as an expression of an increased cell moulting of the tubuli. Whether the increased alanine aminopeptidase activity of the urine may indicate a diabetic nephropathy, is to be clarified only by means of bioptic investigations of the kidneys. Streptomycin can also like a nephrostasis as a sequel of a decompensated cor pulmonale increase the activity of alanine aminopeptidase of the urine.

Topics: Aminopeptidases; Diabetes Mellitus; Diabetic Nephropathies; Diabetic Retinopathy; Female; Humans; Male; Muramidase; Sex Factors

Topics: Adult; Aged; Albuminuria; Antibody Formation; Blood Glucose; Creatinine; Diabetes Mellitus; Diabetic Nephropathies; Female; Growth Hormone; Humans; Insulin; Kidney; Male; Metabolic Clearance Rate; Middle Aged; Muramidase; Proteinuria

Topics: Bacterial Infections; Diabetes Mellitus; Hodgkin Disease; Humans; Leukemia; Leukemia, Monocytic, Acute; Leukemia, Myeloid; Leukocytes; Lymphoma, Large B-Cell, Diffuse; Muramidase

Topics: Aldehydes; Animals; Antibodies; Bacteriophages; Biphenyl Compounds; Diabetes Mellitus; Guinea Pigs; Immune Sera; Immunoglobulin G; Indicators and Reagents; Insulin; Muramidase; Protein Binding; Proteins; Rabbits; Ribonucleases; Serum Albumin, Bovine

Topics: Aging; Blood Cell Count; Blood Chemical Analysis; Clinical Enzyme Tests; Diabetes Mellitus; Geriatrics; Humans; Japan; Leukocyte Count; Leukocytes; Muramidase; Nuclear Warfare; Radiation Injuries; Respiratory Tract Diseases; Sex; Syphilis; Tuberculosis

Topics: Anti-Infective Agents, Local; Blood Coagulation; Dermatologic Agents; Diabetes Mellitus; Humans; Muramidase