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Biomedical subjects

M Pierres

Publications and source records attributed to M Pierres.

122 records · Page 7Linked to original sources
PubMed1979

Fine specificity of antibodies to poly(Glu60Ala30Tyr10) produced by hybrid cell lines.

The polyethylene glycol-mediated cell fusion technique has been used to analyze the diversity of the antibody response to the terpolymer poly(Glu60Ala30Tyr10)(GAT). Nine stable clones (all producing IgM K anti-GAT antibodies) were isolated from a fusion between P3-X63-Ag8 myeloma cells and spleen cells from a DBA/2 mouse sensitized to GAT 5 days earlier. Seven other clones (producing IgG K anti-GAT antibodies) were derived from another fusion between NSI myeloma cells and spleen cells of (C57BL/6 X DBA/2)F1 hybrid mice hyperimmunized with GAT. These 16 anti-GAT antibodies were grouped according to their pattern of reactivity with GAT and the two related polymers of poly(Glu60Ala40) (GA) and poly(GLU50Tyr50) (GT). Two monoclonal anti-GAT antibodies (IgM F9-102.2 and IgG F17-148.3) demonstrated crossreactivity with GA but failed to crossreact with GT determinants. In contrast, the remaining 14 hybridoma antibodies demonstrated preferential reactivity with GAT but also exhibited crossreactive binding to GT and in some cases GA. There was a correlation between the fine specificity pattern and the presence of a common anti-GAT idiotype on these antibodies. Thus, the hybridoma anti-GAT antibodies which reacted with GT shared crossreactive idiotypic determinants (CGAT) present in mouse anti-GAT immune sera. In contrast, the monoclonal F9-102.2 and F17-148.3 antibodies that failed to bind to GT lacked the major CGAT idiotypic determinants.

Alanine↗
PubMed1979

Idiotypic analysis of monoclonal antibodies to poly(Glu60Ala30Tyr10).

Fifteen hybridoma anti-poly(Glu60Ala30Tyr10) (anti-GAT) antibodies were analyzed for the presence of a common set of idiotypic specificities associated with murine anti-GAT antibodies, termed CGAT idiotype, which are present on the anti-GAT antibodies of all mouse strains. Thirteen of these monoclonal anti-GAT antibodies expressed a major fraction of CGAT idiotypic specificities. However, the remaining fraction of CGAT idiotypic specificities were not detected in individual or pooled hybridoma anti-GAT antibodies. Anti-idiotypic antisera made against each of the 15 hybridoma anti-GAT antibodies preferentially bound homologous ligand and showed minimal binding activity to specifically purified serum anti-GAT antibodies. Furthermore, the diversity of the hybridoma anti-GAT antibodies was demonstrated by the presence of individual idiotypic specificities on each of the hybridoma anti-GAT antibodies. However, relatedness among some of the hybridoma antibodies was also apparent since idiotypic analysis revealed that some hybridoma anti-GAT antibodies shared cross-reactive idiotypic specificities not associated with CGAT idiotype. The genetic mechanisms which could account for the generation of such antibody diversity are discussed.

Alanine↗
PubMed1978

In vivo effects of anti-Ia alloantisera. I. Elimination of specific suppression by in vivo administration of antisera specific for I-J controlled determinants.

The in vivo effects of intravenous administration of alloantisera directed to I-J subregion coded determinants were investigated. In confirmation and extension of our previous results, anti-I-Jk [B10.A(3R) anti-B10.A(5R)] and anti-I-Js ([B10.A(3R) X B10.S(9R)]F1 anti-B10.HTT) antisera, when administered in 1 to 10 microliter amounts at the time of immunization, led to twofold increases in the IgM and IgG plaque-forming cells (PFC) responses to suboptimal doses of sheep erythrocytes in A/J (I-Jk) and SJL (I-Js) mice, respectively. To assess whether this immunopotentiation was due to a decrease in specific suppression, experiments were carried out using the polypeptide antigens random linear terpolymer of L-glutamic acid60, L-alanine30, and L-tyrosine10 (GAT) and random linear copolymer of L-glutamic acid50-L-tyrosine50 (GT), since administration of GAT to the nonresponder strain SJL, or GT to the nonresponder strain CBA fails to induce a primary PFC response and stimulates specific suppressor T cells able to prevent PFC responses to subsequent challenge with the immunogens GAT-methylated bovine serum albumin (MBSA) or GT-MBSA, respectively. The current study demonstrates that CBA (I-Jk) mice given 100 microgram GT in Maalox-pertussis adjuvant on day 0, and 10 microliter anti-I-Jk antiserum i.v. on days 0, 1, and 2, develop a significant primary specific PFC response on day 7. A similar responsiveness to 10 microgram GAT is found in SJL mice treated with 10 microliter anti-I-Js antiserum for 3 days. This same active anti-I-Js antiserum does not permit CBA mice to respond to GT, demonstrating the specificity of the anti-I-J effect. These data suggest that anti-I-J antiserum treatment at the time of antigen administration reduces suppressor responses to GAT or GT, permitting primary PFC responses. To directly demonstrate such an effect on suppressor activity, SJL or CBA mice treated, respectively, with GAT or GT to induce suppressor cells active on GAT-MBSA or GT-MBSA responses after adoptive transfer to normal syngeneic recipients were also given anti-I-J antisera (10 microliter/day) for 3 days, at which time their spleen cells were tested for suppressive activity upon transfer. Cells from such treated mice failed to show detectable suppressive activity upon transfer to syngeneic recipients challenged with GAT-MBSA or GT-MBSA, confirming the hypothesis of an in vivo effect of anti-I-J antiserum on suppressor activity.

Animals↗
PubMed1977

Reduction of syngeneic tumor growth by an anti-I-J-alloantiserum.

Highly significant suppression of the growth of S1509a and Sa-I syngeneic sarcomas was observed in A/J mice following daily intravenous injections of 2 microliter of anti-I-Jk alloantiserum. This effect persisted as long as the anti-I-Jk serum was administered (day 15), In contrast, a control anti-I-Js serum had no discernible effect on the growth of the S1509a tumor. The inhibitory activity of the anti-I-Jk serum on the growth of the tumor was absorbed specifically by B10-BR spleen cells bearing I-Jk determinants. In other experiments, we established that A/J mice treated with anti-I-Jk serum, according to the protocol described above, are no longer a source of tumor-specific suppressor cells for adoptive transfer into immune tumor-bearing recipient mice. We conclude that anti-I-Jk serum inhibits tumor growth in A/J mice by abolishing tumor-specific suppressor activity.

Animals↗
PubMed1977

Potentiation of a primary in vivo antibody response by alloantisera against gene products of the I region of the H-2 complex.

Mice were immunized intravenously with suboptimal numbers (3.5-5 X 10(5)) of sheep erythrocytes together with various anti-Ia antisera or with sheep erythrocytes alone, and the primary IgM and IgG plaque-forming cell responses were assayed 6 days later9 A/J (H-2a) mice given 5 X 10(5) sheep erythrocytes together with as little as 0.4 mul of a (129 X A.TH)F1 anti-A.TL (anti-Iak) antiserum developed 2-3 times as many IgM and IGG plaque-forming cells as mice injected with antigen alone or together with various antisera not containing anti-Ia antibodies. Similar results were obtained with BALB/c (H-2d) mice and a (C3H X LG/Ckc)F1 anti-C3H. OH (anti-Iad) antiserum plus sheep erythrocytes. In the case of the anti-Iad antiserum, the potentiating activity could be absorbed with C3H. OH (Id) but not C3H(Ik) spleen cells, demonstrating that the active antibodies were specific for the Id region. Antiserum to I-Jk subregion-coded determinants was tested in A/J (I-Jk) mice and found to also potentiate 2- to 3-fold the plaque-forming cell response to suboptimal erythrocyte immunization. This antiserum [(BIO.A(3R) X DBA/2)F1 anti-B10.(5R)] failed to potentiate responses in BALB/c (I-Jd) mice, as expected on a genetic basis. The potentiating antibodies could be removed by absorption with B10.BR (I-Jk) but not B10 (I-Jb) spleen cells, also confirming the I-J specificity of the activity. The interference of anti-I-J antibodies with T lymphocyte suppressor mechanisms is prposed as a possible explanation for this phenomenon.

Animals↗
PubMed1976

Molecular heterogeneity of rabbit heart phosphorylase kinase.

Phosphorylase kinase (ATP: phosphorylase-b phosphotransferase, EC 2.7.1.38) from rabbit heart, when submitted to electrophoresis on Pevikon, separates into two discrete peaks A and B. The two peaks have been analyzed using reelectrophoresis, chromatography on DEAE-cellulose, thermal stability, inactivation by EGTA (ethyleneglycol-bis(beta-aminoethyl ether)-N,N'-tetraacetic acid) and reaction with an anti-muscle phosphorylase kinase antiserum. It can be concluded that rabbit heart extracts contain two isozymes of phosphorylase kinase. The more negatively charged isozyme seems to be identical with the muscle enzyme. The other isozyme resembles the liver enzyme but differs from the major fraction of the latter by its charge. It is likely that there exist at least three molecular types of phosphorylase kinase.

Animals↗
PubMed1975

Third HL-A segregant series: genetic analysis and molecular independence on lymphocyte surface.

Five sera which detect two alleles of the third HL-A locus (T2 and T4) are described. Statistical analysis of a panel of 220 donors gave gene frequencies in a French Parisian population which are comparable to the results of Scandinavian authors. Segregation observed in 50 families emphasized the linkage disequilibrium with SD2 alleles. T1 was found to be associated with one part of W22 (Da30) and T3 with the other part non-Da30). No recombination was observed between SD2 and SD3, and the distance between these two loci can be estimated at less than 0.0042 U. Differential capping experiments showed that redistribution of SD3 antigens did not affect the SD2 or SD1 products, indicating that they are borne on the cell surface by independent structures. Moreover, capping of SD1, SD2 and SD3 antigens did not provoke complete redistribution of beta2microglobulin which suggests that not all beta2M molecules are linked to HL-A antigens.

Adult↗
PubMedDate not supplied

Interrelationships among distinct idiotypic specificities.

The fine idiotypic properties of a hybridoma (H51.85.2) anti-GAT antibody which lacks both CGAT and GA-1 idiotypes are described. We identified another idiotype, termed GA-2 idiotype, on H51.85.2 hybridoma antibody. The GA-2 idiotype is present in all mouse strains tested and is induced by GA-related antigenic determinants. An interesting relationship between GA-1 and GA-2 idiotype on hybridoma anti-GA antibodies was observed. All GA-1+ hybridomas also express GA-2 idiotype. In contrast, GA-2+ hybridomas can express a full set, a fraction, or none of the GA-1 idiotypic determinants. The data together with previous amino acid sequence studies strongly suggest that H51.85.2 hybridoma antibody was derived from the same VH and VL genes encoding the GA-1+ hybridoma antibodies.

Amino Acid Sequence↗
PubMedDate not supplied

Thy-1 solubilization from mouse T cells by phosphatidylinositol-specific phospholipase C: biochemical and antigenic characterization.

Membrane anchorage of mouse and rat Thy-1 antigens results from the post-translational attachment of a non-proteic tail terminated by a phosphatidylinositol group. In order to determine the biochemical and antigenic properties of the material released by phosphatidylinositol-specific phospholipase C (PI-PLC), we studied, by one-(1-D) and two-dimensional (2-D) gel electrophoresis and by immunoprecipitation, the supernatant of surface-labelled mouse T cells treated with purified Staphylococcus aureus PI-PLC. The major protein released by this enzymatic treatment showed an apparent molecular weight (MW) and an isoelectric focusing (IEF) pattern identical to those of detergent-solubilized, immunoprecipitated Thy-1. In addition, a sandwich radioimmunoassay (RIA) utilizing two Thy-1-specific monoclonal antibodies (mAb) was used to quantitate the amounts of PI-PLC-released and spontaneously shed Thy-1. Considerable differences in susceptibility to enzymatic cleavage and in spontaneous shedding were observed for a variety of mouse T-cell populations, including thymocytes and hybridoma, helper and cytotoxic cloned T cells, even though time-course experiments demonstrated that excess enzyme was used. It might be useful to consider these differences in the cell biology of Thy-1 and the occurrence of other PI-linked proteins of the lymphocyte surface in terms of their implications in the transduction of activation signals.

Animals↗
PubMedDate not supplied

Expression of I-Ak class II genes in mouse L cells after DNA-mediated gene transfer.

The I-region of the mouse H-2 complex encodes I-region-associated or Ia antigens which are involved in lymphocyte interactions and in the regulation of immune responsiveness. Two Ia antigens, termed I-A and I-E, have been identified; both are cell-surface integral membrane glycoproteins which consist of two noncovalently linked polypeptide chains designated alpha (molecular weight (MW) approximately 34,000) and beta(approximately 28,000 MW). Their expression is restricted to B lymphocytes and to antigen-presenting cells such as macrophages. Inside the cell, these alpha beta dimers are associated noncovalently with a nonpolymorphic chain of 31,000 MW designated the invariant (Ii) chain. Cloning of 200 kilobases (kb) of the I-region from mice of the H-2d and H-2k haplotypes was accomplished recently in our laboratory, and the genes encoding the four polypeptide chains, A alpha, A beta, E alpha and E beta, were identified. We now describe the successful expression of I-Ak molecules in transfected mouse L cells.

Animals↗