Monoclonal Antibodies Against Human Placental Glutathione Transferase (Class п )

Massoud, Renato; Bello, Mario Lo; Stefano, Ester De; Molino, Anna; Zelaschi, Daniela; Federici, Giorgio

doi:10.1089/hyb.1991.10.89

Cited by 3 publications

(2 citation statements)

References 14 publications

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“…Unfortunately, the GST antibody study did not provide further information (it did not influence catalytic activity). However, this lack of inhibition is consistent with observations made by others [17]. Since CDNB is a substrate for all three GST families, some further clarification of the data is necessary.…”

Section: Discussionsupporting

confidence: 91%

Glutathione S-Transferase in Human Endometrium: Quantitation and Interindividual Variability in Isoform Content

Barnette

Sarkar²,

Glover³

et al. 1999

Gynecol Obstet Invest

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Objectives: The goals of the present study were to determine whether human endometrium contains glutathione S-transferases (GSTs), to identify the isoforms present (if any) and to assess the causes of any intersubject variability which was observed. Method: Hysterectomy patients (n = 32, 13 with endometrial carcinoma) were examined in the core study. The ability of cytosol from these endometria to conjugate 1-chloro-2,4-dinitrobenzene was measured. Additional studies with chemical inhibitors and monoclonal antibodies to GSTπ were also performed. Results: The pattern of inhibition caused by ethacrynic acid and cibacron blue strongly suggests substantial interindividual variability in type (α and π dominant) and amount (∼10-fold) of this important group of enzymes. Significantly lower GST activity was seen in cancer patients who were smokers when compared with all other subjects (p < 0.05). Conclusion: There are substantial interindividual differences in the GST content of human endometrium. Furthermore, lower GST activity in tissues from endometrial carcinoma patients with a history of smoking may have contributed to the neoplastic transformation of this tissue.

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Section: Discussionsupporting

confidence: 91%

Glutathione S-Transferase in Human Endometrium: Quantitation and Interindividual Variability in Isoform Content

Barnette

Sarkar²,

Glover³

et al. 1999

Gynecol Obstet Invest

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“…Z-Val-Ala-DL-Asp-fluoromethylketone (Z-VAD) was obtained from Calbiochem (San Diego, Calif.). Cell culture media were from GIBCO Life Technologies Ltd. (Paisley, U.K.) and plastic was from Nunc (Roskilde, Denmark); mAb anti-tTG was obtained from Neo-Markers (Fremont, Calif.); mAb antiglutathione S transferase (GST) P1-1 was produced as described by Massoud et al (18). All electrophoresis reagents and secondary antibodies were from Bio-Rad (Richmond, Va.).…”

Section: Reagentsmentioning

confidence: 99%

Identification of ‘tissue’ transglutaminase binding proteins in neural cells committed to apoptosis

et al. 1999

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Overexpression of 'tissue' transglutaminase (tTG) in the human neuroblastoma cells increases spontaneous apoptosis and renders these cells highly susceptible to death induced by various stimuli. We used immunoprecipitation to identify cellular proteins that interact specifically with tTG in SK-N-BE(2) -derived stable transfectants. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed that tTG binding proteins have molecular masses of 110, 50, 22, 14, and 12 kDa. Microsequencing and computer search analyses allowed us to identify these polypeptides as the beta-tubulin (50 kDa), the histone H2B (14 kDa), and two GST P1-1-truncated forms (22 and 12 kDa). The specificity of the interaction between tTG and these proteins was confirmed by competing tTG binding with purified enzyme and by detecting tTG in immunoprecipitates obtained using beta-tubulin or GST P1-1 mAb's. Here we demonstrate that the GST P1-1 acts as an efficient acyl donor as well as acceptor tTG substrate both in cells and in vitro. The tTG-catalyzed polymerization of GST P1-1 leads to its functional inactivation and is competitively inhibited by GSH. By contrast, the tTG-beta-tubulin interaction does not result in the cross-linking of this cytoskeletal protein, which suggests that microtubules act as the anchorage site for tTG and GST P1-1 interaction.

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Allele-Specific Monoclonal Antibodies Against GlutathioneS-transferase Mul-1

Juronen¹,

Tasa²,

Uusküla³

et al. 1994

Hybridoma

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IgG1 class mouse monoclonal antibodies (MAbs) were produced against human glutathione S-transferase Mu1-1 (GSTMu1-1). Eight MAbs of 16 are able to recognize only the native form of the enzyme; 4 MAbs bind to native and denaturated enzyme, and the remaining 4 can bind only to partially denatured antigen in direct ELISA or Western blot. The antibodies recognizing the native form of the enzyme bind to six different epitopes. Three overlapping epitopes are responsible for specific binding of MAbs to different allelic variants of GSTMu1-1. Three allele-specific antibodies, 2E1, 11F12, and 7D11, bind to GSTM1a monomer and the other two, 1H8 and 3H10, recognize GSTM1b monomer.

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Monoclonal Antibodies Against Human Placental Glutathione Transferase (Class п )

Cited by 3 publications

References 14 publications

Glutathione S-Transferase in Human Endometrium: Quantitation and Interindividual Variability in Isoform Content

Glutathione S-Transferase in Human Endometrium: Quantitation and Interindividual Variability in Isoform Content

Identification of ‘tissue’ transglutaminase binding proteins in neural cells committed to apoptosis

Allele-Specific Monoclonal Antibodies Against GlutathioneS-transferase Mul-1

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