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Biomedical subjects

A J Pesce

Publications and source records attributed to A J Pesce.

At least 73 records · Page 4Linked to original sources
PubMed1984

Kinetics of oral tolerance: study of variables affecting tolerance induced by oral administration of antigen.

The induction of antigen-specific tolerance by oral administration of hen egg albumin (OVA) was shown to be time- and dose-dependent. The IgE response was the most effectively suppressed by antigen feeding prior to or after parenteral immunization. The effect on IgG response paralleled that observed on the IgE response, but the magnitude of suppression was less pronounced. The IgA response was enhanced rather than suppressed if the interval between feeding and parenteral immunization was short or if the animals were antigen-fed after the intraperitoneal priming.

Administration, Oral↗
PubMed1984

Expression of normal and tumor-associated antigens in human breast carcinoma.

The expression of six cytoplasmic/membrane antigens (beta 2-microglobulin, HLA, HLA-DR, carcinoembryonic antigen, and two breast tumor-associated antigens (TAAs), B6.2 and B72.3) was investigated in serial sections of 28 human breast carcinomas using monoclonal antibodies and the avidin-biotin complex immunoperoxidase technique. The frequency of expression and linkage between these antigens was determined, and antigenic expression was related to patient age, morphologic differentiation, cytologic grade, and estrogen receptor/progesterone receptor content of the tumor. The expression of beta 2-microglobulin and HLA correlated with morphologic differentiation, well-differentiated and moderately well-differentiated tumors expressing these antigens more often than poorly differentiated tumors. Expression of the TAAs, however, was not related to differentiation. There was no linkage between beta 2-microglobulin/HLA and the TAAs. Carcinoembryonic antigen was found to be linked to the TAA, B6.2. Expression of the TAA, B72.3, correlated with patient age. Eighty percent (23 of 28) of the tumors were positive for carcinoembryonic antigen or at least one of the TAAs. The estrogen receptor/progesterone receptor status of the tumor was not statistically related to the expression of any of the antigens studied. Analysis of tumor antigen profiles may provide important information relevant to prognosis, therapy, and early detection of cancer, as well as insights into the nature of the neoplastic process.

Adult↗
PubMed1983

Immunoregulatory properties of antigenic fragments from bovine serum albumin.

Regulation of the immune response to bovine serum albumin (BSA) by defined substructures of the protein was investigated. The fragments consisted of 41 to 307 amino acids each bearing unique serologic determinants. When administered intravenously the fragments were capable of suppressing the immune response to the entire BSA molecule. The suppression was T-cell mediated and affected the determinants that were linked. The fragments also primed for a secondary anti-BSA response when given in adjuvant; however, the ability to prime was restricted to determinants on the immunizing fragment. The data demonstrate that immune responses to a large protein molecule can be regulated by a relatively small component of its structure and that the ability of a fragment to induce help is more restricted than is its suppressive potential.

Amino Acids↗
PubMed1983

Induction of oral tolerance in mice unresponsive to bacterial lipopolysaccharide.

C3H/HeJ lipopolysaccharide (LPS)-unresponsive and closely related C3H/HeSn LPS-responsive mice were rendered tolerant to hen albumin by antigen feeding before parenteral immunization. Both single and multiple feedings of antigen were effective in inducing tolerance to hen albumin in LPS-responsive and -unresponsive strains of mice. Our data demonstrate that ability to respond to LPS is not a prerequisite for induction of oral tolerance to a soluble protein antigen.

Albumins↗
PubMed1983

Pitfalls and errors in drug monitoring: analytical aspects.

Drug analyses, whether for purposes of evaluating new drug products or as part of clinical monitoring programs, have become frequently requested tests in both clinical and industrial laboratories. From the time of phlebotomy, throughout the transportation, processing and storage of the specimen, during the actual analytical procedure and throughout the clerical reporting of the data, certain potential errors and limitations in the system exist which should be fully recognized for proper evaluation of the laboratory data.

Humans↗
PubMed1982

Immunochemical cross-reactivity between cyanogen bromide fragments of human serum albumin.

The antigenic structure of human albumin was investigated in order to establish whether or not there was any similarity between its antigenic sites. Using immunoadsorbent columns prepared with cyanogen bromide fragments of human serum albumin, antibodies directed against different portions of the albumin molecules were isolated. Measurement of the amount of the antibodies isolated and study of their specificity by inhibition techniques show that these subpopulations of antibodies reacted not only with the fragment used for their isolation (homologous) but also with the other fragments (heterologous). Heterologous fragments were inhibiting only at a very high concentration with regard to the homologous ones. These results show that there is a weak cross-reactivity between different portions of the albumin molecule. This reaction is most probably due to the homology existing in the sequence of the human albumin molecule which has arisen by gene duplication. The same type of behavior can be predicted to extent to other molecules which have evolved by similar mechanisms.

Cross Reactions↗
PubMed1982

Evaluation of the peroxidase-antiperoxidase method for demonstrating cell membrane B2-microglobulin.

The peroxidase-antiperoxidase (PAP) immunohistochemical technic was evaluated for its usefulness in studying B2-microglobulin (B2m) expression in the cell membrane of human tumor lines grown in athymic mice. Eleven human tumor xenograft lines expressing various amounts of B2m were used. B2m was assessed by three methods: PAP technic on formalin-fixed, paraffin-embedded tissue; indirect immunofluorescence on frozen sections; and radioimmunoassay on soluble tumor extracts. The three technics gave comparable results, and the PAP technic proved to be useful in evaluating B2m.

Animals↗
PubMed1981

Specificity of two anti-human albumin monoclonal antibodies.

We have studied the reaction of two monoclonal anti-human albumin antibodies with various fragments of albumin comprising the entire molecule. Using solid phase assay, inhibition of enzyme immunoassay and of passive hemagglutination, they were shown to be specific for a fragment F1, of 6000 dalton, located near the C terminus of human albumin. In addition, these antibodies reacted weakly with fragment D which corresponds to the N terminal half of the molecule.

Antibodies, Monoclonal↗
PubMed1981

Heterogeneity of beta 2-microglobulin in human breast carcinoma.

beta 2-microglobulin (beta 2m) content and distribution in human benign and malignant breast tissues have been investigated by immunohistologic means, and wide differences in the expression of this protein have been observed. The distribution of beta 2m as determined by indirect immunofluorescence was uniform throughout normal human and benign breast tumor tissues, as well as in human tumor xenografts grown in athymic mice, but marked difference in beta 2m content was demonstrated between individual tumors. In breast carcinomas, heterogeneity in beta 2m expression was found to exist within individual tumors. This heterogeneity was evident mainly in moderately well-differentiated tumors; the majority of poorly differentiated tumors did not express beta 2m at all. It is suggested that the expression of surface beta 2m is an indicator of tumor cell differentiation or maturation.

Animals↗
PubMed1981

Immunoenzymometric assays for simultaneous quantitation and distribution of erythrocyte antigen.

We describe an adaptation and modification of the enzyme-labeled immunosorbent assay (ELISA), which yields information on the quantity and distribution of surface antigens on erythrocytes. The distribution assay, named "ELADA" (for Enzyme-Linked Antigen Distribution Assay), involves use of an alkaline phosphatase-immunoglobulin conjugate with alpha-naphthol phosphate and a diazonium salt as substrate. The insoluble reaction product forms a complex on the cell surface at the location of the antigen. Antigens in aliquots from the same enzyme-immunoglobulin conjugate are quantified with the soluble substrate p-nitrophenyl phosphate. One can thus establish whether the distribution of erythrocyte antigens is random by examining the ELADA-stained cells with a scanning electron microscope. Combining the quantitative ELISA with measurements of cell numbers makes it possible to estimate the number of antibody molecules-and thus the number of antigenic sites per cell. By using various modified antisera, substituted naphthol phosphates with higher avidities, and reaction conditions designed to optimize the kinetic reaction, we have been able to resolve the enzyme product deposited on the antigenic site to within 20 nm. It is not always possible to decide whether each deposit represents a cluster of antigenic determinants or a single determinant; however, if the number of antibody sites is known from ELISA quantitation, information about the number of antibody sites per deposit can be ascertained.

Adult↗