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Biomedical subjects

S Ferrone

Publications and source records attributed to S Ferrone.

At least 343 records · Page 19Linked to original sources
PubMed1981

Immunochemical analysis of anti-HLA-A2, HLA-A3, and HLA-B27 xenoantisera elicited with hybrids between human and murine cells.

Rabbits were immunized with hybrids constructed with human and murine cells. Serological and immunochemical studies showed that xenoantiserum 1595 is operationally specific for HLA-A2, xenoantisera 0806 and 0746 for HLA-A3 and xenoantiserum 0745 for HLA-B27. The Fab2 blocking assay suggests a spatial relationship between allotypic determinants recognized by the xenoantisera and those reacting with the HLA-A, B-specific monoclonal antibodies (MoAb) Q1/28, 6/31, Q6/64, and CR-1 and the anti-beta 2-microglobulin (beta 2-mu) MoAb NAMB-1.

Animals↗
PubMed1981

The free and the beta 2-microglobulin-associated heavy chains of HLA-A, B alloantigens share the antigenic determinant recognized by the monoclonal antibody Q1/28.

Serological and immunochemical assays have shown that the monoclonal antibody Q1/28 recognizes an antigenic determinant which is expressed on the heavy chain of subsets of HLA-A, B antigens and is distinct from those defining the serological polymorphism of this system. Association of the HLA-A, B heavy chain with beta 2-microglobulin is not required for expression of the antigenic determinant recognized by the monoclonal antibody Q1/28, since this antibody can immunoprecipitate a 45 000 m.w. component from radiolabeled lymphoid-cell glycoproteins immunodepleted with either an anti-human beta 2-microglobulin xenoantiserum or the MoAb W6/32 to framework determinants of HLA-A, B, C antigens. Furthermore, the MoAb Q1/28 can immunoprecipitate a 45 000 m.w. component from an NP40 lysate of radiolabeled Daudi cells, which lack the genetic information for beta 2-microglobulin. The determinant recognized by the MoAb Q1/28 is relatively resistant to denaturing treatments and does not appear to be carbohydrate in nature. The MoAb Q1/28 is the first example of an antibody which recognizes an antigenic determinant expressed on both the beta 2-microglobulin-associated and free HLA-A, B heavy chains.

Antibodies, Monoclonal↗
PubMed1981

Cross-reactivity between human and murine lymphocyte antigens. IV. Reactivity of H-2 alloantisera with HLA-A, B antigens.

The anti-H-2 alloantiserum D-32 [(B10.A(2R) x C3H.SW) anti-C3H] is cytolytic to human lymphocytes. Fab2 blocking assays, indirect immunoprecipitation and sequential immunoprecipitation experiments showed that the anti-H-2 alloantiserum D-32 recognizes antigenic determinants which are expressed on the heavy chain of subpopulations of HLA-A, B antigens. These determinants are different from those defining the serological polymorphism of the HLA-A, B, C system, are the same as or spatially close to those recognized by the anti-HLA-A, B monoclonal antibody Q6/64 and are expressed on rabbit, rat or guinea pig lymphocytes.

Animals↗
PubMed1981

The monoclonal xenoantibody Q6/64 recognizes a determinant expressed by certain gene products of the A and B loci of the HLA region.

A combination of serological (cytotoxicity, binding assay, lysostrip) and immunochemical (indirect immunoprecipitation, sequential immunoprecipitation, two-dimensional gel electrophoresis) assays have shown that the monoclonal antibodies Q6/64 recognizes an antigenic determinant which is expressed by certain gene products of the A and b loci of the HLA region. The determinant identified by Q6/64 is spatially close to those which define the serological polymorphism of the HLA-A, B, C antigenic system. The results presented in this study in conjunction which those recently published by other investigators indicate that sharing of determinants among HLA-A and -B allospecificities is more frequent than originally assumed on the basis of the cross-reactivity pattern obtained with alloantisera. This conclusion is in agreement with the high degree of homology in the primary amino-acid sequence of A and B allospecificities.

Amino Acid Sequence↗
PubMed1981

Distribution of antigenic determinants recognized by three monoclonal antibodies (Q2/70, Q5/6 and Q5/13) on human Ia-like alloantigens and on their subunits.

The distribution of antigenic determinants recognized by the anti-Ia-like antigen monoclonal antibodies (MoAb) Q2/70, Q5/6 and Q5/13 on molecules coded for by the DR locus and by non-DR loci was investigated using a binding assay with 125I-labeled Ia-like antigens isolated from four B lymphoid cell lines. The determinants reacting with the MoAb Q2/70 and Q5/13 are expressed on all DR alloantigens tested and on BR4X7 specificities, while those reacting with the MoAb Q5/6 are not detectable on DRw7 and BR4X7 molecules. None of the monoclonal antibodies reacted with DC1 molecules. The MoAb Q5/6 and Q5/13 reacted with the isolated beta subunit of the Ia-like antigenic complex, while the MoAb Q2/70 did not react with the isolated chains.

Animals↗
PubMed1981

Stimulation of human T lymphocytes by PHA-activated autologous T lymphocytes: analysis of the role of Ia-like antigens with monoclonal antibodies.

Human T lymphocytes activated with PHA express Ia-like antigens and acquire the ability to stimulate autologous T lymphocytes in mixed lymphocyte reaction. This reaction is immunological in nature since it has specificity and memory. Ia-like antigens play a role in the stimulation of T lymphocytes by autologous PHA-T lymphocytes since monoclonal antibodies to Ia-like antigens can significantly, although not completely, inhibit the stimulation.

Antibodies↗
PubMed1981

Expression of Ia-like antigens in normal human nonlymphoid tissues.

Recent results have demonstrated that Ia-like antigen expression in animal tissues is not restricted to cells associated with immune functions. Whether this phenomenon occurs in normal human tissues has been investigated in this study by indirect immunofluorescence on cryostat sections using monoclonal antibodies to framework determinants of Ia-like antigens. The results of this study show that Ia-like antigens are expressed on several normal human tissues of different embryonic origin. These include the epithelium of the gastrointestinal tract, urinary bladder, bronchial glands, thymic reticuloepithelial cells (entodermic origin), epithelium of mammary gland, acinar cells of parotid, astrocytes (ectodermic origin), alveolar macrophages, Kupffer cells, glomerular and peritubular renal endothelium, endometrium, and Langerhans cells (mesodermic origin).

Cell Line↗
PubMed1981

Analysis of the expression of I-Ak-like antigens in murine fetal and adult tissues with the monoclonal antibody 10-2.16.

The expression of I-Ak antigens in normal C3H/FeJ adult and 15-day embryonic mice has been investigated by indirect immunofluorescence staining of tissue cryostat sections with the anti I-Ak antigen monoclonal antibody 10-2.16. In adult mice I-Ak antigens were expressed in Langerhans-like cells in the skin, epithelium of the gastrointestinal tract, endometrium, thymic reticuloepithelial cells, and several capillary endothelia. On the other hand, these antigens were not detected in Kupffer cells, alveolar macrophages, brain or mammary gland. In 15-day-old embryos the expression of Ia-like antigens was restricted to thymic reticuloepithelial cells, isolated spleen cells, and capillaries of the gastrointestinal tract.

Animals↗
PubMed1981

Effect of tunicamycin on the assembly and antigenicity of HLA antigens: analysis with monoclonal antibodies.

The effect of glycosylation on the assembly and antigenicity of HLA antigens was investigated by examining HLA antigens synthesized in the presence of the antibiotic tunicamycin, an inhibitor of asparagine-linked oligosaccharide addition, with monoclonal antibodies specific for a variety of antigenic determinants. The monoclonal antibody Q5/13 reactive with a determinant expressed on the beta chain of human Ia-like antigens immunoprecipitated alpha and beta subunits with reduced apparent molecular weights from tunicamycin-treated cells, indicating that glycosylation is not required for association of the Ia-like antigen alpha and beta subunits. Immunoprecipitation of HLA-A,B,C antigens from tunicamycin-treated cells with four monoclonal antibodies specific for the heavy chain and one specific for beta 2-microglobulin showed that the heavy-chain determinant detected by the antibody Q6/64 is absent from the non-glycosylated molecule. This is the first demonstration that carbohydrate addition during biosynthesis affects the protein conformation of the HLA-A,B,C heavy chain.

Antibodies, Monoclonal↗
PubMed1981

Characterization of human null cells isolated from peripheral lymphocytes by a simultaneous double-rosetting procedure.

Human null cells were isolated from peripheral blood lymphocytes (PBL) by differential centrifugation on a Ficoll-Hypaque gradient of the PBL following simultaneous rosetting with erythrocyte indicators specific for B and T lymphocytes. Specifically, the T lymphocytes were rosetted with 2-aminoethylisothiuronium bromide-treated sheep erythrocytes (ShE), whereas the B lymphocytes were either rosetted with ShE coated with xenoantibodies against human gamma globulin or first sensitized with monoclonal antibodies to human Ig-like antigens and then rosetted with ShE coated with xenoantibodies against mouse gamma globulin. Approximately 90% of the lymphocytes isolated were null cells that did not bear detectable B-cell markers-that is, surface immunoglobulin and/or Ia-like antigens-or T-cell markers-that is, ShE receptors. The large majority of the null cells expressed receptors for the IgG Fc fragment (53-93%), C3 component (65-92%) and monkey erythrocytes (60-91%) but lacked receptors for the IgM Fc fragment and murine erythrocytes. The null cells exhibited high natural killer cell activity and antibody-dependent cellular cytotoxicity and were two- to four-fold active than the total PBL and the T-enriched cell fractions. The null cells, however, did not respond to stimulation with phytohaemagglutinin and failed to function as either stimulators or responders in an unidirectional mixed lymphocyte reaction.

Antibody-Dependent Cell Cytotoxicity↗
PubMed1981

ADCC of cultured human melanoma cells: analysis with monoclonal antibodies to human melanoma-associated antigens.

Four monoclonal antibodies to human melanoma-associated antigens (MAA) were found to be able to mediate specific cell-dependent lysis (ADCC) of cultured human melanoma cells. The extent of specific lysis of melanoma cells was influenced by the effector to target cell ratio, the amount of antibody added to the reaction mixture, and the incubation time. Cultured melanoma cells treated for 16 h with puromycin or cycloheximide (final concentration, 1.0 micrograms/ml) displayed increased susceptibility to ADCC even though the cell surface expression of MAA was not changed. On the other hand, treatment of melanoma cells with tunicamycin (final concentration, 1.0 microgram/ml) reduced the expression of MAA but did not affect susceptibility to ADCC. These findings suggest that other properties of the target cell membrane besides antigen density play a role in the outcome of ADCC reaction.

Antibodies, Monoclonal↗