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Biomedical subjects

L Vitale

Publications and source records attributed to L Vitale.

At least 55 records · Page 3Linked to original sources
PubMed1991

The fate of human polymorphonuclear leukocyte aminopeptidases upon cell stimulation with phagocytic and chemical stimuli.

1. After being treated with nonopsonized zymosan A or phorbol-12-myristate-13-acetate, human polymorphonuclear leukocytes release aminopeptidases together with granules marker-enzymes and vitamin B12-binding protein. 2. Chemotactic peptide, fMet-Leu-Phe and its analogs, fMet-Phe, fMet-Ala and fMet-Leu-Phe-Lys have a similar effect. 3. By their isoelectric point determinations the released aminopeptidases correspond to the enzymes from granules. Among aminopeptidases released the highest activities were those toward methionine- and alanine-2-naphthylamide and the lowest one toward arginine-2-naphthylamide.

Aminopeptidases↗
PubMed1991

Types and localization of aminopeptidases in different human blood cells.

1. Erythrocytes, polymorphonuclears, monocytes and lymphocytes isolated from human peripheral blood, were shown to possess in their cytosols, granules and microsomal fractions, aminopeptidases capable of hydrolysing arginyl-, leucyl-, methionyl-, phenylalanyl- and alanyl-2-naphthylamide. 2. In different cell compartments enzymes of different pI were responsible for these activities. 3. Chloride activated arginine aminopeptidase, broad specificity aminopeptidase and dipeptidyl peptidase III were found in cytosols of all examined cells. 4. In granules at least two aminopeptidases, a basic or neutral one, and an acidic one inactive at pH 4.4, could be discerned, whereas in microsomal fractions a broad specificity aminopeptidase preferring methionine was detected. 5. There is a considerable degree of similarity in the pattern of aminopeptidases within different blood cells. This may suggest that their functions are correlated to the physiological role of a particular cell compartment, rather than to that of a distinct cell type.

Aminopeptidases↗
PubMed1991

Immunosuppressive effects of Prevotella intermedia on in vitro human lymphocyte activation.

In this study, we have assessed four strains of Prevotella intermedia, isolated from periodontally involved lesions, for their ability to inhibit lymphocyte functions. All four strains were found to cause a dose-dependent inhibition of B- and T-cell proliferation in response to mitogens and antigens. This was reflected in altered DNA, RNA, and protein syntheses. Furthermore, P. intermedia appeared to affect the early stages of cell activation. This was ascertained by kinetic analysis in which it was determined that the extract had to be present during the first 24 h of incubation to cause suppression. Moreover, direct assessment of the early stages of cell activation indicated that release of cytokines and expression of the interleukin 2 receptor and CD69 on T cells were inhibited by P. intermedia sonic extracts. Finally, preliminary characterization of the immunosuppressive agent indicates that it has a molecular mass of approximately 50 kDa and is heat labile. It has been proposed that impaired host defense may play a pivotal role in the pathogenesis of many infections. The data presented in this paper suggest that microbially mediated immunosuppression may contribute to the pathogenesis of periodontal disease by altering the nature and consequences of host-parasite interactions.

Bacteroides↗
PubMed1990

[Endoscopic resolutions of volvulus of the sigmoid colon].

The flexible colonoscope has brought considerable advantages to the diagnosis and nonsurgical treatment of volvulus. In the case of repeated recurrences that make surgery vital because of the onset of signs of vascular trouble on the twisted ansa, preoperative resolution permits correction of hydroelectrolytic imbalances and the preparation of the colon with the possibility of operating with no need for protective colostomy. It also allows resolution of the acute situation in the presence of contraindications to intervention.

Adult↗
PubMed1990

Purification and properties of glutamyl aminopeptidase from chicken egg-white.

Hydrolytic activities characteristic for different aminopeptidases were detected in the egg-white of unfertilized chicken eggs, and one aminopeptidase was isolated in an electrophoretically homogeneous form. The isolated aminopeptidase preferentially hydrolyzed bonds of alpha-glutamyl residue at the NH(2)-end of synthetic substrates and peptides. The enzyme is a dimer with an M(r) of 320,000 and pI of 4.2. Its optimal pH and temperature are 7.6 and 60 degrees C, respectively. EDTA, amastatin, and N-bromosuccinimide are inhibitors, while Ca2++ and Mn2+ are activators of the enzyme Ca2+ also stabilizes the enzyme. According to the observed properties, the isolated chicken egg-white aminopeptidase belongs to the glutamyl aminopeptidases.

Aminopeptidases↗
PubMed1990

[La Peyronie's disease. Our experience].

Following an aetiopathogenetic review of I.P.P., diagnostic and therapeutic possibilities are assessed. Medically, stress is laid on the value of orgotein, an SOD which, used in time, reduces pain and penis curving and permits satisfactory sexual activity. In the case of inveterate forms or of large plaques, the use of a silastic prosthesis is proposed. This support enables a normal sex life to be continued, so resolving psychological and family stress.

Adult↗
PubMed1989

[Use of intraoperative transcystic choledoscopy in calculosis of the main bile duct].

Choledochoscopy is complementary to peroperative cholangiography in exploration of the main biliary way. Transcystic access is proposed in choledocholithiasis. The cystic duct, in fact, is frequently transitable owing to the dilatation produced by the migration of gallstones and because of the increasing miniaturisation of instruments. This examination of the MBW is less traumatic and risky than transcholedochotomic choledochoscopy.

Endoscopy↗
PubMed1989

New chloride-activated aminopeptidase from human erythrocytes.

A new Cl- -activated aminopeptidase was purified from the cytosol of human erythrocytes as a single chain protein of an approx. Mr of 70,000 and pI of 5.1. The enzyme hydrolysed 2-naphthylamides of aliphatic, aromatic and basic L-amino acids, with a preference for the alanyl residue. It also hydrolysed di-, tri-, and some hydrophobic tetrapeptides. The inhibitors were bestatin, amastatin, Co2+, Zn2+, Mn2+, 4-hydroxymercuribenzoate and 1,10-phenanthroline. The activity of the enzyme, inhibited by 4-hydroxymercuribenzoate, was partially restored by the addition of sulfhydryl compounds. The presence of 0.2 M Cl- (Br-,F-) caused a several-fold increase in the isolated aminopeptidase activity.

Aminopeptidases↗
PubMed1989

Differential activity of saporin 6 on normal and leukemic hemopoietic cells.

The antiproliferative effect of saporin 6 (SO6), a ribosome-inactivating protein (RIP) purified from the seeds of Saponaria officinalis has been tested on three leukemic cell lines (K562, U937, and HL60), human normal bone marrow, and peripheral blood hemopoietic progenitor cells from normal subjects. In leukemic cell lines, SO6 appeared much more effective against erythrocytic than against monocytic and promyelocytic leukemic cells, as shown by protein synthesis assays carried out after up to 72 h of culture. Among the normal hemopoietic progenitor cells, erythroid burst-forming units were the most affected, with results similar to those observed in the erythroid leukemic cell line, both in treated and in pretreated cultures, with strong damage after 24 h of exposure to SO6. On the other hand, granulocyte-macrophage colony-forming units (CFU-GM) from bone marrow were significantly more affected than the myeloid leukemic cell lines after permanent treatment with the inhibitor, the damage being significantly lower after an exposure of 24 h. CFU-GM from peripheral blood and megakaryocyte CFU showed an intermediate sensitivity after 24 h of exposure to SO6, similar to that of the other normal precursors after permanent treatment with the drug.

Bone Marrow Cells↗
PubMed1988

Dipeptidyl peptidase III from human erythrocytes.

Purification procedure for dipeptidyl peptidase III (DPP III) from human erythrocytes cytosol, entailing separations on DEAE-cellulose, hydroxylapatite and Sephacryl S-200 column, which gave homogeneous preparation in 35% yield, is described. The enzyme was shown to be a monomeric acidic protein (Mr approximately 82,000, pI approximately 4.5-4.6), sensitive to freezing and temperatures above 40 degrees C. It was inhibited by metallo-chelators and sulphydryl reagents, the activity being restored by divalent cations and thiol compounds. Co2 and Zn2 at low concentrations activated the enzyme, most probably by binding at the same site. Co2 prevented DPP III inactivation by di(4-pyridyl)disulfide, indicating that it is a metallo-peptidase with essential SH-groups which might be near or at the binding site for the metal. Among various naphthylamides Arg-Arg-2-naphthylamide was the best substrate (Km = 7.7 microM, kcat = 28 s-1) of the enzyme. DPP III from human erythrocytes hydrolysed also tri- to decapeptides of different composition, provided they did not have proline at P1 or P'1 position. A hydrophobic residue at P'1 was preferred. Among substrates were angiotensins and Leu-enkephalin. The enzyme showed particularly high affinity for angiotensin III.

Catalysis↗
PubMed1986

A specific nuclear protein and poly(ADPribose)transferase activity in lizard oviduct during the reproductive cycle.

A specific nuclear protein (SNP) appears in the oviduct of the lizard, Podarcis s. sicula Raf., during the recovery phase of the breeding cycle. The protein has a low molecular weight (9.9 kDa), a high electrophoretic mobility and a peculiar amino acid composition. It seems to be regulated by estradiol which, in this species, is involved in oviduct stimulation. Nuclear poly(ADPribose)transferase activity increases in the oviduct as the organ grows, and it peaks upon morphological maturation. Thereafter, as the oviduct becomes secretory, the enzyme returns to basal level. A transient increase of poly(ADPribose)transferase precedes the appearance of SNP, which suggests that the two phenomena are related.

Animals↗
PubMed1986

Human polymorphonuclear leukocytes aminopeptidases.

In human polymorphonuclear leukocytes a methionine, leucine, arginine, phenylalanine and alanine aminopeptidase activities were detected, both in cytosol and secondary granules. All activities were EDTA sensitive and their pH optima were in the range of pH 6.5 to 8.6. In the cytosol two enzymes could be distinguished, broad substrate specificity aminopeptidase of pH 4.7-4.9 and a chloride dependent arginine aminopeptidase of pI 5.3-5.5. The granules contain aminopeptidase of pI 4.0-4.6 and of pI 9.8-10.2, different from those in the cytosol. Among them broad specificity aminopeptidases and possibly specific methionine and leucine aminopeptidases could be discerned.

Alanine↗