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Biomedical subjects

A Capurso

Publications and source records attributed to A Capurso.

At least 55 records · Page 3Linked to original sources
PubMed1988

Apolipoprotein C-II deficiency: detection of immunoreactive apolipoprotein C-II in the intestinal mucosa of two patients.

Recent data suggest that mutant immunoreactive forms of apolipoprotein C-II (apoC-II) can be detected in the plasma of patients with the apoC-II deficiency syndrome. We studied the possible presence of apoC-II mutants in the plasma of two patients with apoC-II deficiency by immunological means. The patients were hypertriglyceridemic, and apoC-II was undetectable in plasma as determined by radial immunodiffusion, electroimmunoassay, and immunonephelometry. Furthermore, apoC-II was undetectable either by electrophoresis or by immunoblotting in the plasma of the probands, while apoC-II was present in the plasma of their parents, although at less than half-normal concentration. Immunochemical localization of apoC-II, however, showed that the apoprotein could be detected within the enterocytes obtained from the intestinal mucosa of the patients. From these data we conclude that the patients synthesize apoC-II, at least in the intestine.

Apolipoprotein C-II↗
PubMed1988

Cell-mediated immune response in patients with type IIa, type IIb and type IV primary hyperlipoproteinaemia.

Plasma lipoproteins inhibit immune function. Polymorphonuclear cell (PMN) and monocyte activities, and pokeweed mitogen (PWM)-driven B cell differentiation in patients with type IIa, type IIb and type IV primary hyperlipoproteinaemia were evaluated. Evidence is provided for a selective impairment of these functional capacities in type IIa and type IIb hyperlipoproteinaemic patients, while immune responsiveness is unaffected in type IV primary hyperlipoproteinaemia. The data suggest a specific immune dysfunction in patients with type IIa and type IIb primary hyperlipoproteinaemia.

Adult↗
PubMed1985

Relationship of the phenotypic expression of the A-IMilano apoprotein with plasma lipid and lipoprotein patterns.

The plasma lipoprotein and apolipoprotein profile of 29 adult A-IMilano (A-IM) carriers and 29 age- and sex-matched non-affected subjects of the same kindred was examined, in order to investigate linkages between the lipid and apoprotein abnormalities and the phenotypic expression of the biochemical disorder. Carriers (A-IM+) showed a higher prevalence of hypertriglyceridemia (12 out of 29); they also had lower plasma total cholesterol, esterified cholesterol and phospholipids, compared to non-carriers. Lipoproteins were characterized by a significant enrichment of triglycerides in low and high density fractions (LDL and HDL), and by the expected striking reduction of HDL mass and cholesterolemia. Conversely, no significant alterations of the major circulating apolipoprotein levels, except for apo A-I and apo A-II, were noted in the A-IM+. The increased free cholesterol/esterified cholesterol ratio in plasma (most marked in HDL), was accompanied by a significant reduction of the lecithin cholesterol acyl transferase molar activity. Several correlations pertaining to lipids, lipoproteins and apoproteins were examined: cholesterol and triglycerides in HDL and, more remarkably, apoprotein A-I and C-III levels in plasma were significantly correlated in the A-IM+. While there was no significant prevalence of specific apo E phenotypes, plasma triglycerides and apo C-II levels were highly correlated in the carriers. The A-IM subjects, while in the presence of severe lipoprotein risk factors, may have alternative mechanisms of cholesterol disposal, potentially responsible for the apparently low prevalence of atherosclerosis.

Adolescent↗
PubMed1984

In vitro effects of human lipoproteins on the immune system in healthy donors: inhibition of plaque forming cell generation and decreased frequency of NK cells.

The effects of human high density lipoproteins, low density lipoproteins and very low density lipoproteins on spontaneous plaque forming cell (PFC) generation have been evaluated in healthy donors. Additionally, natural killer (NK) cytotoxicity using either 51Cr release assay or agarose single cell system has been studied under identical experimental conditions. A significant inhibition of spontaneous PFC capacity was observed. Furthermore, lipoprotein (LP) pre-treatment led to a reduced frequency of cells mediating NK cytotoxic activity as shown by the decreased binding capacity, even if the killing function was per se not affected. Taken together, these results suggest an inhibitory role for human LP on certain immune functions, likely related to the imbalance of lymphocyte metabolic pathway.

Adult↗
PubMed1984

Effect of procetofen on serum lipids and apoproteins.

The effect of procetofen (fenofibrate) on lipids and apoproteins was studied in ten patients affected with familial type II-A and II-B hyperlipoproteinemia. Following stabilization with an isocaloric diet for 2 months, the patients were given 300 mg/day of procetofen for 3 months, then placebo for 1 month. Plasma cholesterol and triglycerides were decreased by 15% and 46%, respectively. Plasma apo B was lowered by 17%. The predominant decrease in lipids and apoproteins occurred in VLDL, whereas in HDL cholesterol increased significantly but not its major apoprotein, apo A-I. A mechanism of action involving increased catabolism of VLDL and reduced synthesis of LDL and VLDL is proposed.

Adult↗
PubMed1983

Plasma lipids, lipoproteins and apoproteins in a case of apo C-II deficiency.

A new case of apo C-II deficiency is described. The patient had plasma triglyceride levels ranging from 10.2-30.5 mmol/l. Apo C-II deficiency was confirmed by gel electrophoresis, isoelectric focusing and immunochemistry. In this patient plasma lipoproteins were mainly chylomicrons and very low density lipoproteins, LDL and HDL levels being very low. Infusion of normal plasma effectively reduced plasma triglycerides and enhanced low density and high density lipoproteins cholesterol levels. These data suggest that in vivo a precursor-product relationship exists between triglyceride rich lipoproteins and LDL and HDL, and further stress the role of the lipoprotein lipase-apo C-II system in modulating these metabolic interconversions.

Apolipoprotein C-II↗
PubMed1981

In vitro catabolism of human very low density lipoproteins: fate of apoproteins B and C.

The fate of apo C-II, apo C-III and apo B during the in vitro catabolism of human very low density lipoproteins (VLDL) by the action of purified lipoprotein lipase was studied. Up to 58 percent of triglyceride apo C-II and C-III was released from VLDL during hydrolysis and at a similar rate. The amount of C apoproteins lost was proportional to triglyceride hydrolysis. The apo B content of VLDL remained constant. From these studies we conclude that during the hydrolysis of human VLDL, lipoprotein lipase, while including a net loss of apo C, is not responsible for major changes in the apo C-II/C-III ratio.

Apolipoprotein C-II↗
PubMed1980

A-IMilano apoprotein. Decreased high density lipoprotein cholesterol levels with significant lipoprotein modifications and without clinical atherosclerosis in an Italian family.

Significant hypertriglyceridemia with a very marked decrease of high density lipoproteins (HDL)-cholesterol levels (7-14 mg/dl) was detected in three members (father, son, and daughter) of an Italian family. The three affected individuals did not show any clinical signs of atherosclerosis, nor was the atherosclerotic disease significantly present in the family. Lipoprotein lipase and lecithin:cholesterol acyltransferase activites were normal or slightly reduced. Morphological and compositional studies of HDL in the subjects showed a significant enlargement of the lipoprotein particles (approximately 120 vs. approximately 94 A for control HDL) and a concomitant increase in the triglyceride content. Analytical isoelectric focusing of HDL apoproteins provided evidence for multiple isoproteins in the apoprotein(apo)-A-I range, with nine different bands being detected instead of the usual four bands observed in normal subjects. Two-dimensional immunoelectrophoresis against apo-A antiserum indicated a clear reduction of apo-A in the alpha electrophoretic region, with splitting of the protein "peak." The observation in otherwise clinically healthy subjects of hypertriglyceridemia, reduced HDL-cholesterol, and marked apoprotein abnormalities, without a significant incidence of atherosclerotic disease in the family suggests this is a new disease entity in the field of lipoprotein pathology, very probably related to an altered amino acid composition of the apo-A-I protein (see Weisgraber et al. 1980. J. Clin. Invest. 66: 901-907).

Adolescent↗
PubMed1979

Demonstration of human apolipoprotien A in isolated mucosal cells from small intestine and isolated hepatocytes.

Isolated mucosal cells from the human jejunum and stomach, cryostat sections from the jejunum, isolated parenchymal liver cells and lymphocytes were investigated for the presence of apolipoprotien A (apoA). Antisera against purified human apoA-I and apoA-II were raised in rabbits and conjugated with fluorescein-isothiocyanate (FITC). Mucosal cells from jejunum and stomach were isolated with pronase from tissue obtained from operated patients. ApoA-I and apoA-II could be demonstrated in isolated mucosal cells as well as in cryostat sections from the jejunum. The fluorescence pattern in isolated jejunal cells was coarse granular. In the radial gel diffusion test the homogenate from mucosal cells of jejunum showed a single precipitation line with anti-apoA-I and with anti-apoA-II, respectively. The reaction was more intensive with anti-apoA-I than with anti-apoA-II. Isolated gastric cells were negative for apoA. Hepatocytes incubated with FITC anti-apoA-I showed a fine granular fluorescence pattern in the cytoplasm. Anti-apoA-II did not react with hepatocytes. There was no evidence for an in vivo fixation of serum-apoA at the surface of isolated mucosal cells from jejunum or isolated hepatocytes. The results support the hypotheses that in man apoA is synthesised in the epithelial cells of the small intestine and in parenchymal liver cells.

Apolipoproteins↗
PubMed1977

The lipoprotein abnormality in Tangier disease: quantitation of A apoproteins.

In this study we have determined by radioimmunoassay and double immunoelectrophoresis the total quantities and distributions of A apoproteins in three adult patients affected with Tangier disease (hereditary alpha-lipoprotein deficiency). Compared with normal plasma, the total quantities of apoproteins A-I and A-II in Tangier plasma were determined to be less than 1% and 5-7%, respectively. In Tangier patients, approximately 90% of the apoprotein A-I sedimented when ultracentrifugations of plasma were carried out at density 1.21 g/ml KBr. By contrast, more than 95% of the apoprotein A-II floated under those conditions. In normal plasma, approximately 90% of both apoproteins A-I and A-II is found in the 1.063-1.21-g/ml KBr density fraction. These findings suggest that complete dissociation of A apoproteins occurs in Tangier plasma. This dissociation of apoproteins was confirmed by double immunoelectrophoresis with monospecific antisera. Immunochemical and electrophoretic experiments did not provide evidence for a structural abnormality of apoprotein A-I in these patients, The results taken together strongly suggest that normal high-density lipoproteins are absent from Tangier plasma.

Adult↗