Characterization of a Monoclonal Antibody (A12) that Defines a Human Acute Lymphoblastic Leukemia-Associated Differentiation Antigen

Carrel, Stefan; Heumann, Didier; Sékaly, Rafick Pierre; Zaech, P.; Buchegger, Franz; Girardet, Christophe

doi:10.1089/hyb.1983.2.149

Cited by 22 publications

(15 citation statements)

References 32 publications

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“…The following mAb were used in this study: D1-12, directed against a monomorphic determinant of the HLA-DR molecule [19]; B9, directed against a monomorphic determinant of the HLA-ABC molecule [20]; DC, directed against a monomorphic determinant of the HLA-DC molecule [21]; Pzm, directed against free P2m microglobulin [20]; A12, directed against the CALL antigen CALLA [22]; LAU-A1, directed against a "Pan-T-cell'' antigen (231; Mel-12, Me4-F8, Me14-Dl2, Mel4-El are mAb directed against melanoma-associated differentiation antigens [24,251. mAb Mel-5, Mel-14 and Me12-D2 react with different epitopes of a large molecular mass glycoprotein (220 kDa) probably identical to the antigen detected by mAb 225,28S of Ferrone [14] whereas the 4 other anti-melanoma mAb react with different antigens.…”

Section: Monoclonal Antibodies (Mab)mentioning

confidence: 99%

Recombinant interferon‐γ can induce the expression of HLA‐DR and ‐DC on DR‐negative melanoma cells and enhance the expression of HLA‐ABC and tumor‐associated antigens

Carrel¹,

Schmidt-Kessen²,

Giuffrè³

1985

Eur J Immunol

104

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Recombinant interferon-gamma (IFN-gamma) induced the expression of HLA-DR when added to the culture medium of HLA-DR- melanoma cell lines. In addition, IFN-gamma induced the expression of another class II antigen, HLA-DC, on a HLA-DR+ and -DC-melanoma cell line and to a lower level on a -DR- and -DC-melanoma line. IFN-gamma also enhanced the expression of HLA-ABC and beta 2-microglobulin, as well as HLA-DR on DR+ melanoma cells. In contrast, IFN-alpha gave no induction of expression of HLA-DR and DC on two DR- melanoma lines, while it did enhance the expression of HLA-ABC and of beta 2-microglobulin. The expression of 3 out of 6 melanoma-associated differentiation antigens was enhanced by IFN-gamma treatment. The modulation of antigens by IFN-gamma was both dose and time dependent. A minimum incubation time of 48 h was necessary for the appearance of HLA-DR on the two HLA-DR- melanoma lines, whereas HLA-ABC and beta 2-microglobulin were already increased after 24 h. A dose of 20 U/ml IFN-gamma started to induce the expression of HLA-DR and DC on melanoma cells GLL-19 and Me-43 and a plateau of maximum antigen expression was reached with 100 U/ml. Analyses of IFN-gamma-treated cells by flow microfluorometry showed a homogeneous distribution of increased staining intensity rather than the appearance of two cell populations. Immunoprecipitation experiments using detergent-solubilized 125I-labeled membrane proteins of IFN-gamma-treated melanoma cells and a monoclonal anti-HLA-DR antibody confirmed the presence of HLA-DR antigens. When IFN-gamma-treated cells were cultured without IFN the induced or enhanced expression of HLA antigens was reversible. Eight days after removal of IFN, the HLA-DR level was reduced by more than 90% and the level of HLA-ABC and beta 2-microglobulin by more than 50%. The demonstration of the ability of HLA-DR- melanoma cells to express HLA-DR after IFN-gamma treatment was extended to cells from other types of tumor such as gliomas, colon carcinomas and one cervical carcinoma cell line.

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Section: Monoclonal Antibodies (Mab)mentioning

confidence: 99%

Recombinant interferon‐γ can induce the expression of HLA‐DR and ‐DC on DR‐negative melanoma cells and enhance the expression of HLA‐ABC and tumor‐associated antigens

Carrel¹,

Schmidt-Kessen²,

Giuffrè³

1985

Eur J Immunol

104

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“…Human plasma kallikrein (9) and Ci inhibitor (20) were purified by using published procedures. The complex between kallikrein and Ci inhibitor was prepared by incubating kallikrein (1.5 Three days after the last injection, mouse spleen cells were removed, fused with NS2 myeloma cells, and distributed in five 96-well plates (Costar, Cambridge, MA), as previously described (23). Wells exhibiting growth of hybrid cells were examined for the production of mAbs, using an assay system detailed later in this section.…”

Section: Methodsmentioning

confidence: 99%

“…Wells exhibiting growth of hybrid cells were examined for the production of mAbs, using an assay system detailed later in this section. Selected hybridoma cells were cloned by limiting dilution (24), and cloned hybridoma cells were injected intraperitoneally into pristane-primed BALB/c mice for the production of ascites fluid (23).…”

Section: Methodsmentioning

confidence: 99%

Human plasma kallikrein and C1 inhibitor form a complex possessing an epitope that is not detectable on the parent molecules: demonstration using a monoclonal antibody.

Agostini¹,

Schapira²,

Wachtfogel³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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The inactivation of human plasma kallikrein (EC 3.4.21.8) by the inhibitor of activated complement component 1 (Ci inhibitor) induces the formation of a 1:1 stoichiometric kallikrein-Ci inhibitor complex and a proteolytically modified form of Ci inhibitor. We have produced a monoclonal antibody that recognizes the kallikrein-Cl inhibitor complex as well as modified C1 inhibitor but fails to react with virgin Ci inhibitor or native plasma kallikrein. This observation constitutes an unequivocal demonstration that the reaction between plasma kallikrein and Ci inhibitor leads to the emergence of an epitope that is undetectable on the parent enzyme and inhibitor molecules.Complexes formed between serine proteases and protease inhibitors of the a1-protease inhibitor class seem to possess a specific domain that is not present on the parent enzyme and inhibitor molecules. This suggestion is based on the following: (i) immunochemical studies showing that neoantigenic determinants are formed during the inactivation of thrombin and factor Xa by antithrombin III, or when plasmin reacts with a2-antiplasmin (1-4); and (ii) in vivo investigations indicating that the complexes between thrombin and antithrombin III, trypsin and a1-protease inhibitor, or involving a2-antiplasmin are rapidly cleared from the circulation by receptor-mediated pathways, whereas this is not the case for the respective virgin inhibitor molecules (5-7).Plasma kallikrein (EC 3.4.21.8) is a serine protease that results from proteolytic cleavage of the zymogen prekallikrein (8-10). Kallikrein plays a central role in the activation of the contact system of blood coagulation, fibrinolysis, and inflammation (11,12). Once formed in the plasma milieu, kallikrein reacts with its substrates, as well as with plasma protease inhibitors. In normal plasma, the predominant inhibitors of kallikrein are the inhibitor of activated complement component 1 (Ci inhibitor) and a2-macroglobulin (13,14). The mechanism by which kallikrein is inactivated by Ci inhibitor has been examined in purified systems. Kallikrein and Ci inhibitor form stable 1:1 stoichiometric enzyme-inhibitor complexes, which do not exhibit enzymatic or inhibitory activity (15-18). Thus, Ci inhibitor inactivates kallikrein by the same mechanism as that reported for the reaction of a1-protease inhibitor, antithrombin III, or a2-antiplasmin with their respective target serine proteases (19). Because of these mechanistic similarities, the reaction between kallikrein and Ci inhibitor may also induce the formation of a complex-specific domain. In this study, we have examined the feasibility of producing monoclonal antibodies (mAbs) that would specifically react with such a domain but would fail to detect the parent kallikrein and Ci inhibitor molecules. This attempt was successful, and relevant mAbs will be made available to other investigators for research purposes. MATERIALS AND METHODSProteins. Human plasma kallikrein (9) and Ci inhibitor (20) were purified by using published procedures. The complex ...

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“…The rat monoclonal antibodies, that labelled brightly CALLA+ leukaemic cells, differed strikingly from J5 (Ritz et al, 1980) and 24.1 (Braun et al, 1983) only f5% of normal blood granulocytes, which was corroborated by the immunoprecipitation data; the rat antibodies also reacted weakly with normal bone marrow lymphoid cells and with foetal liver cells. The reasons for this discrepancy are still unclear, but it is worth mentioning that two other anti-CALLA mono-1982) and A12 (Carrel et al, 1983) …”

Section: Relative Fluorescence Intensity-mentioning

confidence: 99%

Rat AL2, AL3, AL4 and AL5 monoclonal antibodies bind to the common acute lymphoblastic leukaemia antigen (CALLA gp 100)

Lebacq-Verheyden¹,

Ravoet²,

Bazin³

et al. 1983

Intl Journal of Cancer

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Four distinct rat monoclonal antibodies against the common ALL antigen (CALLA, gp 100) were obtained in a single fusion. Rat AL2, AL3, AL4, AL5 and the previously reported mouse J5 monoclonal antibodies identified the same subsets of leukaemic cells. AL2 and AL3 reacted weakly with terminal transferase-positive cells in normal bone marrow and foetal liver, as well as with a minority of mature granulocytes in blood. Immunoprecipitation experiments and competitive binding assays demonstrated that the four rat antibodies and J5 bound to the same glycoprotein of approximately 100,000 mol. wt. This set of rat monoclonal antibodies directed against CALLA has not only a diagnostic usefulness but may also be of therapeutic value.

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Characterization of a Monoclonal Antibody (A12) that Defines a Human Acute Lymphoblastic Leukemia-Associated Differentiation Antigen

Cited by 22 publications

References 32 publications

Recombinant interferon‐γ can induce the expression of HLA‐DR and ‐DC on DR‐negative melanoma cells and enhance the expression of HLA‐ABC and tumor‐associated antigens

Recombinant interferon‐γ can induce the expression of HLA‐DR and ‐DC on DR‐negative melanoma cells and enhance the expression of HLA‐ABC and tumor‐associated antigens

Human plasma kallikrein and C1 inhibitor form a complex possessing an epitope that is not detectable on the parent molecules: demonstration using a monoclonal antibody.

Rat AL2, AL3, AL4 and AL5 monoclonal antibodies bind to the common acute lymphoblastic leukaemia antigen (CALLA gp 100)

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