Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A comparative biochemical and morphological study was made of calf aortic smooth muscle cells found in situ and grown in vitro under various conditions. Striking alterations in enzyme contents, physical properties, and morphological appearances of lysosomes, endoplasmic reticulum, plasma membranes and, to a lesser extent, mitochondria were observed upon culturing of calf aortic smooth muscle cells. These changes first appeared in cells growing out of tissue explants. They developed further upon subculturing of the cells and depended greatly on the culture conditions used. The alterations included increases in specific activities of some 5- to 25-fold of four acid hydrolases, an average ninefold increase in 5' -nucleotidase, sevenfold increase in cytochrome oxidase, and fourfold increase in neutral alpha-glucosidase in subcultured smooth muscle cells compared to aortic cells in situ. Cell fractionation studies showed significant shifts in the equilibrium densities of plasma membranes, microsomes, and lysosomes, but not of mitochondria, in smooth muscle cells growing out from explants and in subcultured cells, compared to cells isolated from intact aortas. Although the cells grown in vitro exhibited typical phenotypic features of smooth muscle cells such as abundant myofilaments and surface vesicles, alterations in the morphological appearance of the endoplasmic reticulum, Golgi apparatus, and, especially, lysosomes were observed. These results demonstrate significant differences in specific cellular characteristics and functions of aortic smooth muscle cells grown in vitro compared to aortic cells in situ.
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PMID:Subcellular fractionation and morphology of calf aortic smooth muscle cells. Studies on whole aorta, aortic explants, and subcultures grown under different conditions. 19 7

Rat pancreatic endocrine tumours were induced by administration of streptozotocin plus nicotinamide. Fifteen to eighteen months later tumours with wet weights of 0.1 to 224 mg were isolated. These tumours were compared with normal rat pancreatic islets. Insulin release from perifused tumours was stimulated by D-glucose, L-leucine, 2-ketoisocaproate, and D-glyceraldehyde, potentiated by theophylline and inhibited by norepinephrine. Compared with isolated rat pancreatic islets, however, insulin secretory responsiveness to glucose stimulation and insulin content were reduced in tumour tissue. Hypoglycaemia in tumour bearing rats and impaired diffusion of insulin out of the tumours may explain this difference. The pattern of enzyme activities observed in tumour tissue was typical for pancreatic endocrine tissue. The activities of succinate dehydrogenase, the two types of the monoamine oxidase, and alpha-glucosidase were in the normal range in tumour tissue. Only the activities of 5'nucleotidase and glutamate dehydrogenase were decreased. Immunocytochemical analysis of the tumours revealed that they contained an average of 91% B-cells. In addition 8% of D-cells were encountered. Proportions of A-cells and PP-cells ranged below 1%. Thus this endocrine tumour of the pancreas with a high proportion of functionally intact B-cells is an interesting model for studying regulation of secretion and endocrine tumour development.
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PMID:Secretory, enzymatic, and morphological characterization of rat pancreatic endocrine tumours induced by streptozotocin and nicotinamide. 299 5

Rectal biopsy specimens from control subjects and from patients with Crohn's colitis, non-rectal Crohn's disease, and acute ulcerative colitis were homogenized in isotonic sucrose and subjected to analytical subcellular fractionation by sucrose density gradient centrifugation. The gradient fractions and tissue homogenates were assayed for marker enzymes for the principal organelles: 5'nucleotidase (plasma membrane), malate dehydrogenase (mitochondria), catalase (peroxisomes), lactate dehydrogenase (cytosol), N-acetyl-beta-glucosaminidase (lysosomes), and neutral-alpha-glucosidase (endoplasmic reticulum). In normal tissue there was a distinct plasma membrane peak at density 1.12 g/ml. In tissue from patients with Crohn's disease the activity was increased approximately twofold even when the rectum showed no evidence of histological involvement. A second plasma membrane component was noted in Crohn's disease at density 1.19 g/ml. The total activity of the mitochondrial enzyme was similar in the various patient groups, but there was evidence of mitochondrial damage. There were no significant alterations in activity and density gradient distributions of catalase or of neutral alpha-glucosidase in the various patient groups, although less membrane-bound lactate dehydrogenase was noted in the patients with inflammatory bowel disease. There was a reduction of both cytosolic and particulate N-acetyl-beta-glucosaminidase in ulcerative colitis and a selective reduction in particulate activity in non-rectal Crohn's disease, demonstrating lysosomal alterations in these disorders. These results indicate selective and specific alterations in the principal subcellular organelles, especially the plasma membrane, lysosomes, and mitochondria, in the inflammatory bowel disease.
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PMID:Subcellular fractionation of rectal biopsy homogenates from patients with inflammatory bowel disease. 399 79

The activity of the marker enzymes lactase, sucrase, neutral alpha-glucosidase, alkaline phosphatase, gamma-glutamyl transferase, leucyl-beta-naphthylamidase (brush border); 5-nucleotidase (basolateral membrane); and acid phosphatase and N-acetyl-beta-glucosaminidase (lysosomes) in jejunal biopsies from patients with the stagnant-loop syndrome and controls was studied. The activity of gamma-glutamyl transferase was increased in the patient group; the activity of the other enzymes did not differ significantly in patients and controls. The DNA to protein ratio was increased in the patient group. The results do not support the hypothesis of epithelial damage in the human stagnant-loop syndrome.
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PMID:Enzymatic activities in jejunal biopsy specimens from patients with the stagnant-loop syndrome. 614 77

Circulating non-T lymphocytes had higher activities of 5'nucleotidase (plasma membrane), neutral alpha-glucosidase (endoplasmic reticulum) and basal leucine amino-peptidase than did T lymphocytes. Activities of catalase (peroxisomes), malate dehydrogenase (mitochondria), lactate dehydrogenase (cytosol) and N-acetyl-beta-glucosaminidase, beta-glucuronidase and acid phosphatase (lysosomes), were similar in the lymphocyte subfractions. Lymphocyte 5'nucleotidase (plasma membrane) in patients with common variable hypogammaglobulinaemia is much lower than normal. However, the decrease is less marked in X-linked hypogammaglobulinaemia, chronic lymphatic leukaemia or protein loosing enteropathy or in lymphocytes isolated from cord blood. Cells from patients with nephrotic syndrome had normal levels of 5'nucleotidase. Other plasma membrane marker enzymes (gamma-glutamyl transferase, leucine amino-peptidase) were normal in lymphocytes from patients with common variable hypogammaglobulinaemia. There is a selective reduction of mitochondrial (malate dehydrogenase) and cytosolic (lactate dehydrogenase) enzymes, with normal activities of lysosomal, peroxisomal and endoplasmic reticulum enzymes, in patients with common variable hypogammaglobulinaemia. The lymphocyte subcellular organelles in normal subjects and patients with common variable hypogammaglobulinaemia have similar properties on sucrose density gradient centrifugation. It is suggested that lymphocytes from patients with common variable hypogammaglobulinaemia show a specific enzymopathy and that this is not simply a reflection of cellular immaturity.
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PMID:Lymphocyte enzyme activities in immunodeficiency syndromes with particular reference to common variable hypogammaglobulinaemia. 630 45