P Soubiran

Natural and induced antitubulin antibodies were compared for their epitope recognition on alpha- and beta-tubulin subunits by immunoenzymatic assays and Western blot techniques on partially digested tubulin molecules. Our results indicated that natural autoantibodies recognized different epitopes from those recognized by induced antibodies, because: 1) all polyspecific natural autoantibodies tested so far recognized the same or very overlapping epitopes in the central part of both alpha- and beta-subunits (between positions 100 and 300 on the tubulin amino acid sequence) and that this epitope differed from the various epitopes recognized by induced antitubulin antibodies on the amino-terminal or carboxy-terminal parts of the tubulin subunits; 2) one human myeloma protein (monoclonal (m)IgA, kappa) with a monospecific antitubulin activity bound to an epitope around position 310 on both alpha- and beta-subunits and a second human mIg (mIgM, kappa) with a monospecific anti-beta activity bound to an epitope on the carboxy-terminal part of the subunit around amino acid position 350. Both epitopes differed from epitopes recognized by induced antitubulin antibodies. These results thus confirmed our previous findings indicating that natural and induced antitubulin antibodies do not share cross-reactive idiotopes.

Journal Article Vitiligo: peripheral T‐cell subset imbalance as defined by monoclonal antibodies Get access P. SOUBIRAN, P. SOUBIRAN INSERM U 210, Laboratoire d'Immunoiogie, Faculté de Médecine, Nice Dr P. Soubiran, U 210 INSERM, Faculté de Médecine, 06034 Nice Cédex, France. Search for other works by this author on: Oxford Academic Google Scholar S. BENZAKEN, S. BENZAKEN INSERM U 210, Laboratoire d'Immunoiogie, Faculté de Médecine, Nice Search for other works by this author on: Oxford Academic Google Scholar C. BELLET, C. BELLET INSERM U 210, Laboratoire d'Immunoiogie, Faculté de Médecine, Nice Search for other works by this author on: Oxford Academic Google Scholar J. P. LACOUR, J. P. LACOUR Service de Dermatologie, Hôpital Pasteur, CHU de Nice, France Search for other works by this author on: Oxford Academic Google Scholar J. P. ORTONNE J. P. ORTONNE Service de Dermatologie, Hôpital Pasteur, CHU de Nice, France Search for other works by this author on: Oxford Academic Google Scholar British Journal of Dermatology, Volume 113, Issue s28, 1 July 1985, Pages 124–127, https://doi.org/10.1111/j.1365-2133.1985.tb15640.x Published: 01 July 1985

Recent experiments suggested that alpha‐protein (AFP) may have immunoregulatory properties and play a role in protecting the fetus from rejection by the mother. The present study was performed to determine whether purified human AFP, its molecular variants separated on Lens culinaris agglutinin, and fetal serum albumin showed immunoregulatory activiiy on in vitro transformation of normal human lymphocytes by mitogens or by allogeneic cells. Human AFP and fetal serum albumin were purified from human whole fetuses by immunoabsorption, followed by acid elution. AFP variants (HLI, HL2, HL3, HL4) were separated by lectin affinity chromatography. The proteins were tested in lymphocyte cultures stimulated by concanavalin A, phytohaemagglutinin and pokeweed mitogen and in mixed lymphocyte cultures. Four batches of AFP and one batch of fetal albumin, in the concentration range of 0‐100 μg/ml and in one experiment up to 2 mg/ml, had a stimulatory effect on lymphocytes. One batch of human AFP showed inhibitory effect with low reproducibility. The variants had a stimulatory effect except for HL3, which was found to be slightly inhibitory in phytohaemagglutinin stimulated cultures when compared with cultures without AFP, but there was no significant difference when compared with cultures in which AFP was replaced by its dialysate. Thus, the results reported here are not consistent with the conclusion that human AFP has a significant immunosuppressive effect on man. Hypotheses about causes of discrepancies are analysed.