To test the affinity of a new F(ab′)2 monoclonal antibody (TRF1) against human fragment D dimer of cross-linked fibrin for atherosclerotic plaques free of detectable thrombi, 6 atherosclerotic segments of carotid and femoral artery, and as a control 5 segments of atherosclerosis-free internal mammary artery, were drawn from 11 male patients undergoing bypass surgery. All segments were carefully washed in order to remove possible endoluminal thrombi, and cut to obtain pairs of intimal fragments of similar weight, containing either plaques (n = 16), or fatty streaks (n = 12), or normal endothelium (n = 20). Each fragment underwent a direct binding test to TRFI, or to a non-specific antibody, both labeled with 125I. The activity in each fragment was measured after 3 h of incubation at 37°C, and after washing the fragments every hour for 3 h. TRF1 binding (as percentage of initial activity) was significantly higher (P < 0.001) in atherosclerotic than in normal fragments (26% ± 11.5%, vs. 9.2% ± 3.9% in fatty streaks, and 1.9% ± 0.6% in normal endothelium), and indirect immunofluorescence confirmed TRF1 uptake within the plaque wall. By contrast, the non-specific antibody did not show any significant binding. These preliminary results demonstrate the high specific affinity of TRF1 for atherosclerotic plaques, probably due to the hemorheologic phenomena that activate platelets and provoke the formation of fragment D dimers of cross-linked fibrin on the plaque surface. © 1993.

Immunodetection of human atherosclerotic plaque with 125I-labeled monoclonal antifibrin antibodies / Cesare, Greco; Mario Di, Loreto; Massimo, Ciavolella; Maria, Banci; Taurino, Maurizio; Elena, Cerquetani; Roberto, Chiavarelli; Naro, Fabio; Gabriella Cusella De, Angelis; Antonio, Mele. - In: ATHEROSCLEROSIS. - ISSN 0021-9150. - 100:2(1993), pp. 133-139. [10.1016/0021-9150(93)90199-5]

Immunodetection of human atherosclerotic plaque with 125I-labeled monoclonal antifibrin antibodies

Cesare Greco;TAURINO, Maurizio;NARO, Fabio;
1993

Abstract

To test the affinity of a new F(ab′)2 monoclonal antibody (TRF1) against human fragment D dimer of cross-linked fibrin for atherosclerotic plaques free of detectable thrombi, 6 atherosclerotic segments of carotid and femoral artery, and as a control 5 segments of atherosclerosis-free internal mammary artery, were drawn from 11 male patients undergoing bypass surgery. All segments were carefully washed in order to remove possible endoluminal thrombi, and cut to obtain pairs of intimal fragments of similar weight, containing either plaques (n = 16), or fatty streaks (n = 12), or normal endothelium (n = 20). Each fragment underwent a direct binding test to TRFI, or to a non-specific antibody, both labeled with 125I. The activity in each fragment was measured after 3 h of incubation at 37°C, and after washing the fragments every hour for 3 h. TRF1 binding (as percentage of initial activity) was significantly higher (P < 0.001) in atherosclerotic than in normal fragments (26% ± 11.5%, vs. 9.2% ± 3.9% in fatty streaks, and 1.9% ± 0.6% in normal endothelium), and indirect immunofluorescence confirmed TRF1 uptake within the plaque wall. By contrast, the non-specific antibody did not show any significant binding. These preliminary results demonstrate the high specific affinity of TRF1 for atherosclerotic plaques, probably due to the hemorheologic phenomena that activate platelets and provoke the formation of fragment D dimers of cross-linked fibrin on the plaque surface. © 1993.
1993
atherosclerotic plaque; monoclonal antifibrin antibodies; scintigraphy
01 Pubblicazione su rivista::01a Articolo in rivista
Immunodetection of human atherosclerotic plaque with 125I-labeled monoclonal antifibrin antibodies / Cesare, Greco; Mario Di, Loreto; Massimo, Ciavolella; Maria, Banci; Taurino, Maurizio; Elena, Cerquetani; Roberto, Chiavarelli; Naro, Fabio; Gabriella Cusella De, Angelis; Antonio, Mele. - In: ATHEROSCLEROSIS. - ISSN 0021-9150. - 100:2(1993), pp. 133-139. [10.1016/0021-9150(93)90199-5]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/103907
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