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J Sire

Publications and source records attributed to J Sire.

45 records · Page 3Linked to original sources

[beta2-Microglobulin and experimental nephropathies in macacus monkey (author's transl)].

In the monkey, the action of four renal toxics : lead acetate, sodium maleate, cadmium chloride and sodium chromate was compared. Tubulopathies were obtained only with cadmium chloride and sodium chromate with in the best cases about 16 mg/l of beta2-microglobulin (beta2m) in the urine. Monkey and human beta2m have the same molecular weight and are antigenically similar. However, they differed in electrophoretic mobility, the monkey beta2m being slightly more cathodic.

Animals↗

[beta2-Microglobulin in human seminal fluid (author's transl)].

The expression of human beta2-microglobulin (beta2m) on human spermatozoa cell surface was investigated by cytotoxicity and immunofluorescence tests. beta2m was also found in human seminal fluid by use of immunochemical techniques. Seminal fluids obtained from couples with infertility problems were tested for beta2m, albumin and total proteins concentration. A higher level of beta-2m was found in azoospermia compared with that of normal sperms.

Adult↗

The different electrophoretic forms of post gamma-globulin their antigenic identity and their structural variability.

Post gamma-globulin, first described as a constant component of protein of cerebrospinal fluid and urine from patients with tubular disorders has also been found in other biological fluids. Post gamma-globulin from a single individual always migrated as several bands after storage. Three electrophoretic forms, immunochemically identical, have been isolated by gel chromatography, preparative continuous flow electrophoresis and ion-exchange chromatography. Their molecular weight was found to be approximately between 11 000 to 12 000. No difference between the three forms could be detected. The N-terminal amino acids were found to be Lys, Arg and Leu respectively for the three forms of post gamma-globulin. The "slow" and "fast" forms of post gamma-globulin seemed to differ by elimination of small basic peptides or amino acids from the N-terminal end of the protein. No enzymatic activity of post gamma-globulin was found, but this requires further investigations.

Amino Acids↗

A rapid and sensitive method using immunological nephelometric analysis to evaluate the gel-filtration method. (Application to the diagnosis of rubella).

Immunological nephelometric analysis has been shown to be a more sensitive method than either immunoelectrophoresis or gel-diffusion for testing the gel-filtration method of human immunoglobulins sera. This method has the advantages of facility, rapidity and sensitivity. We have compared this method to radial immunodiffusion. This method can be applied to locate with precision any antigens after gel-filtration or ion-exchange chromatography.

Antibodies, Anti-Idiotypic↗

HIV1 infection of human monocytes and macrophages promotes induction or translocation of NF-KB-related factors.

In 1991, we demonstrated, using electrophoretic mobility shift assays, that 3 different factors (termed B1, B2 and B3) with affinity for the KB-enhancer target sequence were specifically detected in nuclear extracts from HIV1-infected monocytes and macrophages. The B2 factor was induced in the nuclei of these cells only upon HIV1 infection. The B3 factor was only slightly evident in nuclei of uninfected cells but was readily detectable in nuclei of infected monocytes. Its expression remained very low in nuclei of HIV1-infected macrophages. In this paper, we demonstrate that the B2 factor is expressed in the cytosol of monocytes and macrophages as a DNA-binding protein, indicating that it is not associated with an inhibitor (IKB). This factor remained clustered in the cytosol and was translocated to the nuclei only after HIV1 infection. The B3 factor is detected in the cytosol only when cells are HIV1-infected. The role of HIV1 infection in the expression and the translocation of these factors is discussed.

Base Sequence↗

Serological and structural analysis of HLA class I molecules: beta 2-microglobulin interacts with the two external domains of the HLA class I heavy chain.

The serological reactivities of HLA class I molecules were studied in relation to structural modifications of these molecules, including shuffling of external exons and exchange of human beta 2-microglobulin for beta 2-microglobulin from different species. Two major clusters (I and II) of monomorphic and polymorphic antigenic determinants could be delineated. beta 2-Microglobulin participates in the formation of the two clusters, indicating that the light chain interacts tightly with the two external domains of the HLA class I heavy chain. However, external molecules can modify these interactions and alter the antigenic structure of the overall molecule. Thus, fixation on HLA class I molecules of the Fab fragment of a monoclonal antibody directed at antigenic determinants associated with cluster II resulted in enhanced fixation of a monoclonal antibody (B10.6) related to cluster I. The structural and functional implications of these results are discussed.

Antibodies, Monoclonal↗

Recognition of hybrid HLA molecules expressed on murine P815 cells using human alloreactive cytotoxic T lymphocytes.

The HLA-A2 and -A3 genes were used to construct intra-exon hybrids in which part of the third exon (corresponding to the second domain) was of one type and the rest of the other. Murine P815 cells expressing these hybrid constructs were assayed with human alloreactive cytotoxic T-lymphocyte lines specific for either HLA-A2 or HLA-A3. Specific recognition patterns were obtained which indicate that, in some cases, a small portion of the HLA-A2 sequence in an HLA-A3 background is sufficient for recognition by HLA-A2-specific cytotoxic T cells.

Cell Line↗