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Biomedical subjects

S Ferrone

Publications and source records attributed to S Ferrone.

At least 379 records · Page 21Linked to original sources
PubMed1981

Humoral immunity in renal transplantation Detection of cytotoxic antibodies to lymphocyte antigens other than HLA-A,B,C and Ia-like antigens in patients with vascular graft rejection.

By using a Fab2 fragment blocking assay with cultured human B lymphoid cells and peripheral lymphocytes as targets, cytotoxic antibodies to Ia-like antigens, to HLA-A,B,C antigens, and to lymphocyte structures other than these two types of histocompatibility antigens were identified in serial post-transplant sera from 18 renal allograft recipients. Multiple combinations of these three types of antibodies were seen in 78% of the sera. A higher reactivity as well as higher titers of antibodies were found in patients with graft failure from rejection. The occurrence of anti HLA-A,B,C or anti Ia-like antibodies did not show any relationship to graft outcome. However, cytotoxic antibodies to other antigens (referred to as non-HLA antibodies) were detected in five of the six patients with graft failure and in only one patient with graft survival. In this latter patient, non-HLA antibodies occurred with a chronic rejection episode and were no longer detectable when the rejection ceased. This study shows that the Fab2 fragment blocking assay is a useful method to identify antibodies to multiple specificities in sera from kidney graft recipients, and suggests that non-HLA cytotoxic antibodies may be associated with graft rejection.

Antibody Formation↗
PubMed1981

Lysis of cultured human melanoma M10 cells by polyclonal xenoantibodies to melanoma-associated antigens.

Cultured human melanoma cells M10 harvested from cultures in different phases of their growth show significant changes in the expression of melanoma-associated antigens (MAA), but they do not vary in susceptibility to lysis mediated by anti-MAA xenoantisera and effected by complement or lymphoid cells. Furthermore, melanoma cells M10 showed a significant increase in susceptibility to immune lysis following treatment with puromycin at doses that do not effect the expression of MAA. The lack of correlation between MAA density and susceptibility to immune lysis supports the contention that, under the experimental conditions used, cellular properties play a major role in the outcome of immune attack.

Antibodies, Neoplasm↗
PubMed1981

Tumor-associated antigens in spent medium of human melanoma cells: immunochemical characterization with xenoantisera.

Xenoantisera to human melanoma cells and to partially purified melanoma-associated antigens were coupled to protein A-bearing Staphylococcus Aureus or protein A-Sepharose and used as immunoadsorbents for the indirect immunoprecipitation of intrinsically radiolabeled proteins released into culture medium from various cultured human tumor and nontumor cell lines. These radiolabeled immunoprecipitates when analyzed by SDS-PAGE revealed highly reproducible molecular profiles of proteins and glycoproteins released by various cultured tumor lines and control cells into their spent culture media. A comparison of molecular profiles together with data indicating the binding specificity of known xenoantisera produced against human melanoma cells or their extracts led to the discovery of 2 macromolecules that are associated with human melanoma cells; a glycoprotein with a subunit m.w. of 240,000 (240K) and a single-chain glycoprotein of 94,000 (94K) m.w. also found in association with human carcinoma cells are described in this report.

Animals↗
PubMed1981

Molecular profiles of human melanoma-associated antigens.

Melanoma-associated antigens (MAA) shed into spent culture medium of intrinsically radiolabeled melanoma cells react specifically with monoclonal and polyclonal anti-melanoma xenoantiserums and are represented by two glycoproteins with molecular weights of 240,000 (240K) and 94,000 (94K): 240K is present only on melanoma cells whereas 94k is also found on carcinoma cells and on fetal melanocytes. Both 240K and 94K have been obtained radiochemically pure by utilizing cellulose ion-exchange and antibody affinity chromatography. The two antigens have different charge properties, as 240K binds to CM-cellulose while 94K does not. A difference in carbohydrate moieties is also indicated since 240K binds selectively to lentil lectin and 94K to ricin lectin. Two-dimensional gel electrophoresis an tryptic peptide maps of the two antigens reveal distinct and characteristics profiles. Subunit structure determination of both antigens suggests 94K to be a single chain whereas 240K appears to be a subunit of a larger molecular structure.

Antibodies, Neoplasm↗
PubMed1980

Lymphocytotoxic antibodies in systemic lupus erythematosus patients and their relatives: reactivity with the HLA antigenic molecular complex.

Lymphocytotoxic activity of sera from systemic lupus erythematosus (SLE) patients and their families was inhibited by 50% or more by preincubation of target cells with Fab2 fragments of xenoantisera against beta 2 microglobulin or the heavy chain of the HLA-A,B,C antigenic molecular complex. An antiHLA-DR xenoantiserum had less blocking effect on peripheral blood mononuclear cells but was effective at blocking reactivity of these sera against cultured B lymphoid cell lines. The repertoire of specificities in family members' sera differed from each other and their respective proband with respect to their reactions with cultured lymphoid cell lines. These data indicate that lymphocytotoxic antibodies (LCA) found in most patients with SLE and some of their relatives include a subpopulation with specificity for determinants present on major histocompatibility gene products. They also suggest that LCA in relatives represent a defect in immune regulation which allows expression of existing autoimmune potentials rather than immunization with a single "lupus" antigen.

Antibody Specificity↗
PubMed1980

Lymphoid cell line identification and the detection of cross contamination.

Four lymphoid cell lines, presumably recent derivatives from non-neoplastic human tonsils, were identified in actuality as established Burkitt lymphoma and lymphoblastoid cell lines (LCL) when tested by chromosome banding and typing for HLA antigens. Additionally, the morphology, growth characteristics, tumorigenicity, expression of Epstein-Barr virus antigens and surface membrane immunoglobulins (SmIg) of the four lymphoid cell lines confirmed the correct identifications. In determining the possibility of cross contamination, the most reliable criteria for the identification of lymphoid cell lines were found to be HLA antigenic profile, karyotype, cellular morphology, and growth characteristics.

Antigens, Viral↗
PubMed1980

Isolation of human T lymphocytes: comparison between nylon wool filtration and rosetting with neuraminidase (VCN) and 2-aminoethylisothiouronium bromide (AET)-treated sheep red blood cells (SRBC).

Isolation of human T lymphocytes by rosetting with SRBC, centrifugation on Ficoll-Hypaque gradients and lysis of SRBC, which reportedly affects the functional activities of lymphocytes, was compared to isolation of T lymphocytes by filtration through a nylon wool column. The two methods were similar in yields and purity of T lymphocytes. No selective loss of T cell subpopulations was found in T lymphocytes isolated by filtration through a nylon wool column as judged by the percentage of T gamma and T micron and the suppressor and helper activity in functional assays. Therefore, filtration through a nylon wool column is a useful method to purify T lymphocytes and has the advantage of being comparatively simple and quick to perform and of avoiding manipulations which may affect the functional activity of T lymphocytes.

Animals↗
PubMed1980

Serological, functional, and immunochemical characterization of a monoclonal antibody (MoAb Q2/70) to human Ia-like antigens.

Serological and immunochemical studies showed that monoclonal antibody Q2/70 (MoAb Q2/70), produced by the hybridoma technique, is specific for human Ia-like antigens. This antibody recognizes an antigenic determinant which is different from those defining the serologic polymorphism of Ia-like antigens, and is expressed on subsets of human Ia-like molecules and on lymphoid cells from other species. MoAb Q2/70 inhibits unidirectional MLRs* between allogenic human lymphocytes, but not between murine and human lymphocytes. In ADCC* assays. MoAb Q2/70 mediates lysis of cultured human B lymphoid cells RPMI 4098, effected by murine splenocytes. The antibody is suitable to isolate immunologically functional B lymphocytes from human peripheral blood.

Animals↗
PubMed1980

Cell cycle and the differential expression of HLA-A,B and HLA-DR antigens on human B lymphoid cells.

Monoclonal antibodies specific to HLA antigens and the fluorescence-activated cell sorter were used to analyze the changes in the density of human histocompatibility antigens HLA-A,B and HLA-DR on the surface of synchronously growing WI-L2 cells (a human B cell line) progressing through the cell cycle. The WI-L2 cells were synchronized by density-dependent arrest in G1, and samples from G0, G1, late S and late G2 phases were used to determine the frequency distribution of cell volume, DNA content, and the relative amounts of cell surface HLA antigens; the observed density changes were calculated from these values. The HLA-A,B density remained nearly constant throughout the cell cycle, whereas the HLA-DR density increased sharply at the G2-M stage. These results suggest a cell cycle-dependent differential control of the expression of these two sets of histocompatibility antigens on B cells.

B-Lymphocytes↗
PubMed1980

Lack of association of serologically detectable human melanoma-associated antigens with beta 2 microglobulin: serologic and immunochemical evidence.

Serologic and immunochemical assays showed that human melanoma-associated antigens (MAA) identified with operationally specific xenoantisera were neither spatially nor structurally associated with beta 2-microglobulin (beta 2-mu), the light chain of the HLA-A,B antigen molecular complex; i.e., cultured melanoma cells coated with a specific anti-beta 2-mu xenoantiserum maintained their reactivity with anti-MAA xenoantisera. Furthermore, soluble MAA were not bound by a beta 2-mu immunoadsorbent. Finally, MAA were shed into the culture medium of melanoma cells and then were immunoprecipitated with specific anti-MAA xenoantisera, analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, they appeared as two distinct structures with molecular weights of 240,000 and 94,000 but comprised no structure with the characteristic 12,000 molecular weight of beta 2-mu. Conversely immunoprecipitates obtained by the reaction of spent culture medium of [3H]valine-labeled melanoma cells with anti-beta 2-mu xenoantiserum had the 12,000-molecular-weight component but no structures with the molecular weights established for MAA. Thus the data refute the contention that serologically detectable MAA have a molecular structure similar to that of HLA antigens.

Antibodies, Neoplasm↗
PubMed1980

Cross-reacting xenoantibodies to the heavy chain of H-2 and HLA-A,B antigens: serologic and immunochemical characterization.

H-2 cross-reactive antibodies present in HLA xenoantisera were purified by absorption on and elution from murine cells. Antibodies isolated from one of these antisera, 78-E48, were found to mediate complement-dependent lysis of both human and murine lymphoid cells but not of Daudi cells or of human lymphoid cells coated with Fab2 fragments from a cow anti-human beta 2-microglobulin (beta 2 m) antiserum. In indirect immunoprecipitation analyses 78-E48 reacted only with proteins of approximately 45,000 and 12,000 MW present in NP-40 extracts of both human and murine lymphoid cells. Sequential precipitation experiments with rabbit anti-human beta 2 m and allo-anti-H-2Kk, Iak sera established that these proteins were in fact H-2 and HLA-A,B antigens. It was also found that 78-E48 reacted only with the heavy chain of HLA-A,b and H-2 antigens, since this eluate was unreactive with beta 2 m in a radioimmunoassay, and its capacity to immunoprecipitate the 45,000 and 12,000 MW proteins from human cell extracts was unaffected by prior reaction with purified human beta 2 m. These data show for the first time that H-2 and HLA-A,B antigens share properties that probably depend upon their teritary structure.

Absorption↗