beta glucosidase/nekroz

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Serum cytosolic beta-glucosidase activity in a rat model of necrotizing enterocolitis.

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The diagnosis of necrotizing enterocolitis (NEC) is made from a combination of clinical and radiographic findings. There are no useful screening biochemical markers of intestinal injury. The serum concentration of cytosolic beta-glucosidase (CBG), an enzyme found primarily in enterocytes, is

Rubber Tree (Hevea brasiliensis) Bark Necrosis Syndrome III: A Physiological Disease Linked to Impaired Cyanide Metabolism.

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First attempts to discriminate between tapping panel dryness (TPD) and bark necrosis (BN), two Hevea sp. bark diseases leading to the cessation of latex production, showed differences in latex biochemical characteristics (1). Further, contrary to TPD, BN is characterized by inner phloem necrosis

Urinary enzyme excretion during renal papillary necrosis induced in rats with ethyleneimine.

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N-Acetyl-beta-glucosaminidase, beta-galactosidase, beta-glucosidase, acid and alkaline phosphatase were monitored in urine kidney homogenates and serum of rats with papillary damage induced with ethyleneimine. Serum urea levels, total protein in the urine and urine volume were monitored throughout

Physiological compensation in antisense transformants: specific induction of an "ersatz" glucan endo-1,3-beta-glucosidase in plants infected with necrotizing viruses.

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Plant class I glucan endo-1,3-beta-glucosidases (beta-1,3-glucanase; 1,3-beta-D-glucan glucanohydrolase, EC 3.2.1.39) have been implicated in development and defense against pathogen attack. Nevertheless, beta-1,3-glucanase deficiencies generated by antisense transformation of Nicotiana sylvestris

Effects of β-glucosidase hydrolyzed products of harpagide and harpagoside on cyclooxygenase-2 (COX-2) in vitro.

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Harpagide (1) and harpagoside (2) are two iridoid glycosides existing in many medicinal plants. Although they are believed to be the main bioactive compounds related to the anti-inflammatory efficacy of these plants, the mechanisms of their anti-inflammatory activities remain unclear. The results of

Differential augmentation by recombinant human tumor necrosis factor-alpha of neutrophil responses to particulate zymosan and glucan.

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Zymosan (Z) and its major insoluble carbohydrate component beta-linked glucan activate human neutrophils (PMN) through a trypsin-sensitive recognition mechanism. This mechanism is believed to involve the PMN CR3R. Both Z and glucan generated dose and time-dependent release of the secondary lysosomal

Antibody-guided enzyme therapy of cancer producing cyanide results in necrosis of targeted cells.

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A number of enzyme/prodrug activation approaches for the treatment of cancer have been reported to date with varying success. We describe progress in the development of a system based on a beta-glucosidase enzyme in combination with a naturally occurring "prodrug," the sugar linamarin, which

Anti-inflammatory activity of aucubin by inhibition of tumor necrosis factor-alpha production in RAW 264.7 cells.

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To elucidate a possible mechanism for the anti-inflammatory action of iridoid glycosides, the effects of both aucubin (AU) and its hydrolyzed product (H-AU) by beta-glucosidase treatment were studied on the production of TNF-alpha in RAW 264.7 cells. H-AU suppressed the production of both mRNA for

Adult type 3 Gaucher disease as manifestation of R463C/Rec Nci I mutation: first reported case in the world literature.

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Gaucher disease is the most common lysosomal storage disorder. It is autosomal recessive in nature and results from mutations in the GBA gene coding for acid beta glucosidase. It is classified into three types based on CNS involvement and its severity. Type 3, or chronic neuronopathic Gaucher

Type I Gaucher disease with bullous pemphigoid and Parkinson disease: A case report.

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BACKGROUND Gaucher disease (GD) is a rare genetic lysosomal storage disorder inherited in an autosomal recessive pattern. GD is due to the deficiency of a lysosomal enzyme, acid beta-glucosidase (or glucocerebrosidase). Type 1 Gaucher disease (GD1) is characterized by thrombocytopenia, anemia, an

Simultaneous detection of Gaucher's disease and renal involvement of non-Hodgkin's lymphoma: the first Asian case report and a review of literature.

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Gaucher's disease (GD) is a rare autosomal recessive (AR) disorder characterized by a deficiency of glucocerebrosidase (glucosylceramidase, acid β-glucosidase). This enzyme deficiency results in an accumulation of sphingolipids in the cells of GD patients, which may contribute to the dysregulation

Studies on the nephrotoxicity of p-nitrophenylarsonic acid: changes in rat kidney and urinary enzyme activities following the administration of p-nitrophenylarsonic acid.

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Histological studies showed that the administration of p-nitrophenylarsonic acid to rats resulted in renal tubular necrosis. The nephrotoxin was administered intraperitoneally and doses greater than 30 mg/kg were found to be fatal. The severity of the renal lesion depended on the amount of the

[Bone changes in Gaucher disease].

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Among Ashkenazi-Jews, Gaucher' disease, an autosomal-recessive hereditary genetic defect of sphingolipid metabolism, occurs more frequently than in the general population. Because of lack of the specific b-glucosidase, glucocerebrosidase, there is increased deposition of glucocerebrosides in the

Intrafamilial clinical variability of type 1 Gaucher disease in a French-Canadian family.

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Glucocerebroside beta-glucosidase (glucocerebrosidase) activity was determined from peripheral blood lymphocytes and cultured skin fibroblasts of eight full sibs in a French-Canadian family at risk for Gaucher disease, an autosomal recessive sphingolipidosis resulting from deficient

Use of plain radiography to optimize skeletal outcomes in children with type 1 Gaucher disease in Brazil.

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BACKGROUND Gaucher disease is the most common lysosomal storage disease and is caused by deficient production and activity of the lysosomal enzyme beta-glucosidase (glucocerebrosidase), resulting in progressive accumulation of glucosylceramide (glucocerebroside) in lysosomes of cells of the

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