[Separation, by means of electrofocusing, of some phosphorylase B derivatives].
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Catalysis↗
Biomedical subjects
E Castigli
Publications and source records attributed to E Castigli.
The activity of silybin on phospholipid metabolism of normal and fatty liver in vivo.
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Animals↗
The effect of silybin on liver phospholipid synthesis in the rat in vivo.
Female Wistar rats have been injected intravenously for seven days with various different doses of silybin, the main component of the drug silymarin, and the in vitro synthesis of phosphatidylethanolamine and phosphatidylcholine from their respective precursors, CDP-ethanolamine and CDP-choline has been examined in liver microsomal membranes. Appreciable inhibition of the incorporation rates of precursors into lipids has been noticed at dosage of 15-20 mg/100 g body wt., daily. No evident effect is exerted by similar silybin treatment on choline and ethanolamine incorporation respectively into liver phosphatidylcholine and phosphatidylethanolamine in vivo.
Animals↗
[Changes in some enzyme levels of the gastrocnemius muscle of patients with chronic obliterating arteriopathy of the lower limbs].
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Acid Phosphatase↗
CD40 ligand/CD40 deficiency.
CD40 is a surface antigen expressed on B cells. The CD40 ligand (CD40L) is expressed on activated T cells. Interaction between CD40 and CD40L is critical for proliferation and isotype switching in the context of a response to a T-cell-dependent antigen. Patients with X-linked hyper-IgM syndrome (HIGMX-1) in their CD40L gene are unable to switch from IgM to IgG, IgA and IgE. Mice with a disrupted CD40 gene fail to undergo isotype switching to T-cell-dependent antigens but respond normally to T-independent antigens.
Animals↗
Changes in enzyme levels in human skeletal muscle during obstructive arteriopathy of the lower limbs.
Some enzymatic activities have been assayed in the gastrocnemius muscle of patients with obstructive arteriopathy of the lower limbs. The specific activities of all the examined glycolytic enzymes, of malate dehydrogenase and of glycerol-3-phosphate dehydrogenase are significantly decreased while the specific activities of two lysosomal enzymes, beta-glucuronidase and cathepsin A, are significantly higher than in the controls. Therefore it may be inferred that the metabolic capacity of glycolysis and of Krebs cycle are lowered. On the other hand the increased specific activity of lysosomal enzymes suggests the hypothesis that the above mentioned modifications and the morphologic alterations of the muscle and of the small blood vessels might be ascribed, at least partly, to a release of lysosomal hydrolases in active form.
Adult↗
[Lysosomal lesions during a course of acute experimental muscular ischemia. Protective effect of a polypetitide proteinase inhibitor].
Three groups of rabbits were used: a) with acute ischaemia in a rear limb; b) with acute ischaemia in a rear limb and treated with i.v. 100,000 KIU of a proteinase-inhibitor polypeptide extracted from ox lung; c) normal controls. Acute ischaemia was obtained by ligature of the ipsilateral common iliac, external iliac, inferior epigastric and femoral arteries. Soluble and total activity of 3 lysosomal enzymes (cathepsin, acid phosphatase and N-acetyl-glucosaminidase) were determined in gastrocnemius muscle from all 3 groups. The mean ratio between bound and soluble activity for all 3 enzymes in normal gastrocnemius muscle was higher than in ischaemic muscle, but not significantly different from that in ischemic muscle of animals treated with the polypeptide. Furthermore, this ratio in ischemic muscle was significantly lower than that of ischemic muscle of the rabbits treated with the polypeptide. These data suggest that the polypeptide offers protection against lysosomal lesion in the course of experimental ischaemia of the skeletal muscle.
Acetylglucosaminidase↗
Activation of phosphatidylserine synthesis: a possible mechanism of regulation of the base-exchange enzymic system.
The possible relationship between phosphatidyl serine synthesis by base-exchange and nervous activity has been investigated in the rat caudate nucleus. The rate of incorporation of L-serine into the phosphatidyl serine of slices from caudate nucleus is not affected by dopamine nor is it affected by the addition to dopamine of a cyclic phosphodiesterase inhibitor which would increase the endogenous cyclic-AMP levels. However, imidazole, a phosphodiesterase activator, clearly stimulates by more than 100% the phosphatidyl serine synthesis in the slices. The activation is not due to interaction at the catalytic site(s) of the base-exchange system, since it is neither observed in homogenates of caudate nucleus nor in cerebral microsomes at various pH values.
3',5'-Cyclic-AMP Phosphodiesterases↗