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Biomedical subjects

R Creyssel

Publications and source records attributed to R Creyssel.

At least 19 recordsLinked to original sources
PubMed1984

Immunoelectrophoretic investigations in 55 patients with systemic amyloidosis.

Among 55 amyloidoses, the detection of a monoclonal protein (MP) led to the selection of 15 primary and 3 myeloma-associated types of amyloidosis. Therefore the presence of a MP gives evidence for an immunocytic amyloidosis. The lambda-light-chain nature of MP and the abundant production of free light-chains are two of the factors predisposing to the production of amyloid deposits (AL) in the course of immunocyte dyscrasias.

Amyloid↗
PubMed1982

Coexistence of multiple monoclonal immunoglobulins with identical constant regions in one patient.

Two populations of IgG molecules, designated F-IgG3(chi) and S-IgG3(chi), were isolated from a patient with multiple myeloma. The constant regions of the two molecules appear to be identical, since the heavy chains of both belong to the gamma 3 subclass and both molecules are positive for G3m(5), G3m(10), and G3m(11) but negative for G3m(21), Km(1) and Km(2) allotypes. In contrast, the two molecules have different variable regions, since (a) they do not share idiotypic determinant(s); (b) their light chains have different NH2 terminal amino acid sequences, and (c) both their heavy and light chains have different peptide maps and amino acid compositions. SDS-polyacrylamide gel electrophoresis showed that the F-IgG3(chi) molecules have two kinds of light chains. One, designated, chi n, has a normal molecular weight (approximately 23,000); the other, designated chi h, has a molecular weight of approximately 28,000.

Aged↗
PubMed1982

Laser nephelometry and radial immunodiffusion compared for immunoglobulin quantification in pathological sera.

We evaluated nephelometers from Behring, Hyland, and Beckman for IgG, IgA, and IgM quantitation in sera from patients with monoclonal gammopathies. The intra-batch precision of each instrument for each immunoglobulin class and for different concentrations of the same immunoglobulin was compared to the one obtained with the radial immunodiffusion method. No nephelometer showed a clearly better precision. The correlation with cellulose acetate electrophoresis was good for each of the three nephelometers. The mean value by the radial immunodiffusion method was higher than corresponding determinations by nephelometry.

Humans↗
PubMed1981

A sensitive method for characterization of oligoclonal immunoglobulins in unconcentrated cerebrospinal fluid.

Although isoelectric focusing has been used to demonstrate the presence of oligoclonal IgG in the CSF, the technique has not allowed detection of oligoclonal IgG in unconcentrated CSF. A new technique is reported, by which unconcentrated CSF is separated by isoelectric focusing, and the IgG bands are then detected by radioimmunofixation. Samples as small as 20 microliters may be used.

Autoradiography↗
PubMed1978

Monoclonal IgM cryoglobulinemia associated with gamma-3 heavy chain disease: immunochemical and biochemical studies.

A patient (Mia) with a monoclonal IgM(kappa) cryoglobulin (cryo IgM) developed additional heavy chain disease proteins of the gamma3 subclass 8 years later. Biochemical studies of the cryo IgM indicated that the heavy chain was VHI, but the NH2-terminal amino acid sequence of the light chain did not permit a definite assignment of its Vkappa subgroup. Two major fragments of the gamma3 chain were distinguishable by electrophoresis in sodium dodecyl sulfate polyacrylamide gel. The smaller component (designated Mia F) had a molecular weight of approximately 30 000 and the larger component (designated Mia S) 35 000. Both fragments had G3m(21) and G3m(27) allotypic determinants. These data and the NH2-terminal amino acid sequence of the gamma chain fragments suggested that Mia S consists of the major part of the gamma3 hinge region plus the CH2 and CH3 domains of the gamma3 chain, whereas Mia F may be derived from the former as a result of postsynthetic cleavage. The partial amino acid sequence of the Mia S fragment is homologous to the hinge region amino acid sequence of human gamma3 chains reported in the literature, with only one amino acid difference out of the 11 residues compared. This difference may represent an allotypic difference within the gamma3 subclass. Alternatively, the production of Mia S may have resulted from the accidental derepression of a "silent" constant region gene not expressed in normal individuals.

Amino Acid Sequence↗
PubMed1977

Alpha-1-antitrypsin phenotypes in Lyon, France.

Alpha-1-antitrypsin Pi phenotyping was performed by thin-layer isoelectric focusing on samples from 1653 healthy white blood donors. The variants were confirmed by the acid-starch gel technique and crossed immunoelectrophoresis, with complete agreement between the two methods. The allele frequencies in this population were PiM, 0.9019; PiS, 0.0713;PiZ,0.0142; PiI, 0.0036; PiF, 0.0036; PiV, 0.0024. In addition, some rare phenotypes (MX, IS, LM) were noted. No difference was noted in the distribution of the variant alleles between males and females. The significance of the high frequency of the S allele is related to the ethnic origin of this population. The agreement of the results obtained by our technique and by acid-starch gel electrophoresis confirms the validity of Pi determination by thin-layer isoelectric focusing.

Adolescent↗
PubMed1976

[Neurological manifestations in monoclonal gammapathies. Pure neurological manifestations. Immunofluorescence study].

Analysis of 105 peripheral and central nervous system complications in 1062 monoclonal gammapathies draws attention to two types of phenomena. The possibility of pure neurological manifestations of IgM monoclonal gammapathies with macroglobulinorachia leads to discussion of their nosological position in relation to Waldenström's disease, Burkitt's lymphoma and Marek's disease. It is suggested that these cases should be reclassified under the heading "secreting neurolymphomatosis". Immunofluorescence and electron microscopy of 10 biopsies of the peripheral nerve showed deposits of monoclonal immunoglobulin whose function in determining peripheral neuropathies is discussed. The simultaneous presence of lymphoid infiltration, amyloid deposits and the monoclonal immunoglobulin (M component) suggests that this immunoglobulin could be the link between the cellular infiltrate secreting it and amyloid infiltration which would be the visible manifestation of it.

Amyotrophic Lateral Sclerosis↗