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Your search keyword '"PONTIERI GM"' showing total 3 results
Start Over Author "PONTIERI GM" Publisher thieme
3 results on '"PONTIERI GM"'

1. Anti-prothrombin but not "pure" anti-cardiolipin antibodies are associated with the clinical features of the antiphospholipid antibody syndrome.

Author

Sorice M, Pittoni V, Circella A, Misasi R, Conti F, Longo A, Pontieri GM, and Valesini G

Subjects
Adolescent, Adult, Aged, Antibodies, Anticardiolipin blood, Antiphospholipid Syndrome blood, Antiphospholipid Syndrome physiopathology, Autoantibodies blood, Autoantibodies immunology, Child, Female, Humans, Male, Middle Aged, Antibodies, Anticardiolipin immunology, Antiphospholipid Syndrome immunology, Prothrombin immunology
Published
1998

2. Ganglioside content of human platelets--differences in resting and activated platelets.

Author

Ferroni P, Lenti L, Martini F, Ciatti F, Pontieri GM, and Gazzaniga PP

Subjects
Chromatography, Thin Layer, Flow Cytometry, G(M3) Ganglioside analysis, Gangliosides analysis, Humans, Immunoenzyme Techniques, N-Acetylneuraminic Acid analysis, Spectrometry, Fluorescence, Blood Platelets metabolism, Gangliosides metabolism, Platelet Activation physiology
Abstract

Gangliosides may play functional roles in platelet physiology, therefore this study has been designed to evaluate whether changes in ganglioside composition may occur as a consequence of platelet activation. The results obtained indicate that lactosylceramide and GM3 are the major glycosphingolipids of human platelets. The lipid-bound sialic acid (LBSA) content was 1.27 +/- 0.04 micrograms/mg of protein. Resting platelets did not express GD3; GD3 was synthesized upon platelet activation (24 +/- 8 ng/mg of protein). The stimulation of platelets with adenosine diphosphate showed the appearance of GD3 even in the absence of degranulation. Finally, incorporation of pyrene-labeled GM3 into platelet membranes, followed by stimulation with adenosine diphosphate, resulted in the appearance of a fluorescent band comigrating with GD3. The present studies indicate that sialytransferase activation may occur as an early event following platelet stimulation, leading to GD3 synthesis mainly from the GM3 pool.

Published
1997

3. Anticardiolipin and anti-beta 2-GPI are two distinct populations of autoantibodies.

Author

Sorice M, Circella A, Griggi T, Garofalo T, Nicodemo G, Pittoni V, Pontieri GM, Lenti L, and Valesini G

Subjects
Adult, Aged, Antibodies, Anticardiolipin blood, Antiphospholipid Syndrome blood, Autoantibodies blood, Autoimmune Diseases blood, Binding Sites, Child, Enzyme-Linked Immunosorbent Assay, Epitopes immunology, Epitopes metabolism, Female, Glycoproteins metabolism, Humans, Immunoglobulin G blood, Immunoglobulin G classification, Immunoglobulin G immunology, Lupus Erythematosus, Systemic blood, Male, Middle Aged, Phospholipids metabolism, beta 2-Glycoprotein I, Antibodies, Anticardiolipin classification, Antiphospholipid Syndrome immunology, Autoantibodies classification, Autoimmune Diseases immunology, Cardiolipins immunology, Glycoproteins immunology, Lupus Erythematosus, Systemic immunology
Abstract

This study has been undertaken to assess whether anticardiolipin and anti-beta 2-GPI are two distinct populations of (auto)antibodies, and to clarify whether the beta 2-GPI region critical for phospholipid binding is also crucial for anti-beta 2-GPI reactivity. Fourteen of the 62 anticardiolipin (aCL) ELISA positive sera (22.6%) were positive for anti-beta 2-GPI by immunoblotting, 42 (67.7%) for aCL using TLC immunostaining. IgG fractions from 5 sera gave the same anticardiolipin reactivity detected by TLC immunostaining in the corresponding sera. All anti-beta 2-GPI-positive sera were reactive with the phenylthiocarbamyl derivative of the protein, indicating that binding of phenylisothiocyanate with lysine residues does not modify the molecule antigenicity. In addition, incubation of IgG fractions with the phospholipid binding site did not modify reactivity with beta 2-GPI. These findings demonstrate that: a) "true" antiphospholipid antibodies are detectable in patients' sera; b) aCL and anti-beta 2-GPI have a different immunological profile; c) the beta 2-GPI phospholipid-binding site is not the region recognized by the antibodies.

Published
1996

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