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Biomedical subjects

J C Monier

Publications and source records attributed to J C Monier.

At least 55 records · Page 3Linked to original sources
PubMed1988

Use of immunoblotting to characterize the mitochondrial antigens recognized by anti-mitochondrial autoantibodies.

Sera with anti-mitochondrial autoantibodies detected by indirect immunofluorescence and/or enzyme-linked immunosorbent assay (ELISA) were examined by immunoblotting against pig heart mitochondria. Seven types of reactions were defined, according to the pattern of the labelled bands. Type I sera reacted with 12 bands located within four zones. The most intensively labelled bands were located at 70, 67, 58, 63 and 43 kDa. Other types gave decreasing band numbers. When beef heart mitochondria were used, sera belonging to each of the above types had a profile of labelled bands which sometimes differed from those obtained with pig heart mitochondria. When the chloroform extracted F1-ATPase from beef heart mitochondria was used to prepare the immunoblots, primary biliary cirrhosis (PBC) sera with anti-mitochondria antibodies reacted with all the bands although zone A bands were less labelled. Rat liver mitochondria gave seven bands with type I sera among which the 57 and 35 kDa bands were specific for rat liver mitochondria, as shown by absorption tests. Sera of PBC patients were also tested in immunoblotting against rat liver subcellular fractions including mitoplasts, submitochondrial particles, inner membrane, outer membrane, matrix proteins and inter-membrane proteins. Antigenic bands of A and B zones were localized in the inner membrane and/or in the matrix proteins and the 35 kDa band in inter-membrane proteins. The outer membrane gave no reaction. The most frequent anti-mitochondrial autoantibody types in PBC were type II, then I, whilst for chronic active hepatitis type III was the most common. Type V was only seen in a patient suffering from a typical PBC. Some sera from patients with syphilis, collagenous colitis or progressive systemic sclerosis labelled one or two bands distinct from those labelled by the PBC sera. Sera from patients with drug-induced hepatitis with endoplasmic reticulum antibodies and with systemic lupus erythematosus were generally found negative by immunoblotting.

Animals↗
PubMed1988

Spontaneous familial systemic lupus erythematosus in a canine breeding colony.

A colony of German shepherd dogs was studied in which a high proportion of antinuclear antibody (ANAb) carriers and dogs with systemic lupus erythematosus (SLE)-like signs were found. The titre of serum thymulin and the percentage of circulating T lymphocytes were both low. The incidence of disease decreased down the generations through the introduction of outside sires, thus suggesting a genetic origin for the disease.

Animals↗
PubMed1988

Immunomodulation induced by immunoglobulins. I. Action of placental immunoglobulin on in vitro spontaneous synthesis of IgE in man.

The IgE contents of various therapeutic immunoglobulin (Ig) preparations of placental or plasmatic origin were measured. Their effects on spontaneous IgE synthesis by lymphocytes from healthy and atopic subjects were also studied. Whatever their origin, Igs contained IgE in varying amounts, depending on the batch. Only Igs of placental origin inhibited spontaneous IgE synthesis; this effect appeared linked to IgE content.

Adjuvants, Immunologic↗
PubMed1988

Systemic lupus erythematosus in a colony of dogs.

A colony of dogs was obtained by the mating of a female German Shepherd Dog crossbred and a male Belgian Shepherd Dog crossbred, both with systemic lupus erythematosus (SLE). The colony also contained 16 dogs representing F1, F2, and F3 generations. Ten colony dogs had circulating antinuclear antibodies, and 5 of the 10 had clinical signs of SLE. Two F3-generation females had signs of severe SLE. Two dogs had antibodies to extractable nuclear antigen, notably 1 dog had antibodies to Smith (Sm) antigen and 1 had antibodies to Sjogren syndrome A (SSA) antigen. Thymulin (serum thymic factor associated with zinc) titers were generally low in the descendants, but fluctuations were detected within the same dog. In vitro response of lymphocytes from these colony dogs to concanavalin A was maximal for lower mitogenic concentrations, compared with response of lymphocytes from 10 healthy dogs. The suppressive lymphocyte activity in 6 autoimmune colony dogs was diminished in comparison with the activity in 5 nonautoimmune colony dogs and 6 healthy dogs.

Animals↗
PubMed1988

Anti-histone antibodies (ELISA and immunoblot) in canine lupus erythematosus.

In the canine systemic lupus erythematosus (SLE), anti-double stranded DNA (ds-DNA) antibodies (enzyme linked immunosorbent assay (ELISA) or indirect immunofluorescence on Crithidia luciliae) are rare whereas anti-histone antibodies are often found: 61.7% with ELISA and 74% with immunoblot. In canine SLE the pattern of anti-histone antibodies on immunoblot is different from anti-histone antibodies in human SLE. Indeed, histone fractions which are most often recognized by the canine antibodies are by order of frequency H3, H4 and H2A, whereas in man this order is H1, H2B then H3. In the diagnostic criteria of canine SLE, we suggest replacing the anti-ds-DNA antibodies by the anti-histone antibodies detected by immunoblot.

Animals↗
PubMed1988

Immunolocalization of thymosin alpha 1, thymopoietin and thymulin in mouse thymic epithelial cells at different stages of culture: a light and electron microscopic study.

The secretory evolution of the thymic hormones (thymulin, thymosin alpha 1 and thymopoietin) in cultured thymic reticuloepithelial cells (TREC) was studied by immunocytochemical techniques using monoclonal anti-thymulin or anti-thymosin alpha 1 and polyclonal anti-thymopoietin antibodies (Ab). The culture of TREC was performed with a medium where L-valine was replaced by D-valine, thus ensuring rapid and selective development of these cells. The number of thymulin, thymosin alpha 1 or thymopoietin-containing cells increased progressively from Day 6 to Day 12 of the culture. The localization of the three thymic hormones within the TREC also varied according to the age of the culture. By light microscopy the staining of the three hormones was localized in some cytoplasmic granules at the beginning of the culture and at Day 90, while at Day 12 it was throughout the cytoplasm. In electron microscopy these localizations corresponded respectively to vacuoles of different sizes and to cytosol. All these results show that the synthesis and excretion of thymulin, thymosin alpha 1 and thymopoietin evolve during the development of TREC in culture.

Animals↗
PubMed1988

Discrepancies between two procedures for ds-DNA antibody detection: Farr test and indirect immunofluorescence on Crithidia luciliae.

Of the 54,911 sera routinely tested for anti-double stranded-DNA antibodies (Ab), 2,297 gave a positive reaction with both indirect immunofluorescence (IIF) on Crithidia luciliae (CL) and the Farr test, or with only one of the two tests. Of the sera giving positive reactions, only 1,499 (65.3% of the positive sera) were positive with both reactions. Among the remaining 798 sera (34.7% of positive sera), 48.25% gave a positive reaction with the Farr test and 51.75% with the IIF reaction. Of the discrepant Farr test(+), IIF-CL(-) sera, slightly fewer than half corresponded to a false positive reaction of the Farr test due to the presence in the serum of proteins other than Ab which were able to bind to the labelled ds-DNA to form a complex precipitable by 50% saturated ammonium sulfate solution. Slightly more than half of the other Farr test(+) IIF-C'(-) sera corresponded to a defect in the IIF-CL reaction. Among the discrepant Farr test(-) IIF-CL(+) sera, 1/3 corresponded to false positive reactions IIF-CL and 2/3 of the remaining sera contained weakly avid anti-ds-DNA antibodies undetectable using the Farr test.

Animals↗
PubMed1988

Immunoreactivity of aqueous extracts of rat and mouse tissue with anti-thymosin alpha 1, anti-bovine thymopoietin and anti-thymulin antibodies. Studies using immunoblotting.

Anti-thymosin alpha 1 monoclonal antibodies recognized, on immunoblots, 1 to 2 bands corresponding to molecules of 34 and 35 Kd when using aqueous extracts of thymus, spleen, kidney, liver, brain, pituitary and adrenal glands from rats or mice. Anti-bovine thymopoietin polyclonal antibodies, in the same conditions, labelled analogous 34, 35 and 35.5 Kd molecules in brain and thymus extracts but also a 40 Kd molecules in thymus and a 90 Kd in brain extracts. Anti-synthetic thymulin monoclonal antibodies recognized irregularly and poorly a 52 Kd molecule from thymus and brain extracts. These results suggest that thymopoietin, thymulin and specially Thymosin alpha 1 are first synthesized in large precursors. Finally, other organs seem capable of synthesizing thymosin alpha 1 and probably thymopoietin, but for thymulin, the results are too irregular to conclude.

Animals↗
PubMed1987

Lack of reactivity of anti-human immunodeficiency virus (HIV) P17/18 antibodies against alpha 1 thymosin and of anti-alpha 1 thymosin monoclonal antibody against P17/18 protein.

The blood rate of alpha 1 thymosin is increased during HIV infection, despite the thymus involution. Anti-alpha 1 thymosin antibodies inhibit HIV replication in vitro. A homology between alpha 1 thymosin and the HIV P17/18 core protein exists and would explain a cross-antigenicity. We have studied the interaction between anti P17/18 antibodies from HIV patients and alpha 1 thymosin and between an anti-alpha 1 thymosin monoclonal antibody and the P17/18 protein. We were unable to confirm any cross-reactivity. During acquired immune deficiency syndrome, a major involution of the thymus appears with a severe depletion of thymocytes and epithelial cells. Certain thymic functions are missing, as corroborated by the reduction of the hormone thymulin in the blood. At the same time, the blood rate of the 2 other hormones (partly of thymic origin), alpha 1 thymosin and beta 4 thymosin is increased. One of the theories explaining this discordance is that patients with acquired immunodeficiency syndrome produce molecules which have a cross antigenicity with these thymic hormones. Sarin et al. have recorded a 50% homology between the C-terminal part (last 18 aminoacids) of alpha 1 thymosin and the part between the 92nd and the 109th aminoacids of the HIV P17/18 protein. The cross reactivity between this P17/18 protein and alpha 1 thymosin would explain the high rates of alpha 1 thymosin found in the radio-immunoassay of sera from patients infected with HIV. Another result of this cross-reactivity is the ability of alpha 1 thymosin antibodies to inhibit HIV replication in the H9 permissive cell line.(ABSTRACT TRUNCATED AT 250 WORDS)

Antibodies, Monoclonal↗
PubMed1987

IgM rheumatoid factor (RF), IgA RF, IgE RF, and IgG RF detected by ELISA in rheumatoid arthritis.

One hundred patients with rheumatoid arthritis (RA), of whom 73 were seropositive by latex or Waaler-Rose (WR) assays, or both, 100 healthy subjects, and 102 diseased controls (22 patients with systemic lupus erythematosus (SLE) and 80 with bronchial asthma) were evaluated for the presence of IgM rheumatoid factor (RF), IgA RF, IgE RF, and IgG RF by an enzyme linked immunosorbent assay (ELISA). Ninety two per cent, 65%, 68%, and 66% of the patients with RA were found to be positive for IgM, IgA, IgE, and IgG respectively. A positive correlation existed between the levels of IgM RF and IgA RF on the one hand and disease activity on the other, and the levels of IgM RF and IgA RF correlated with the levels of circulating immune complexes as measured by a C1q binding assay. The presence of extra-articular features also correlated positively with the levels of IgA RF and IgE RF. Five out of six patients with Sjögren's syndrome had very high levels of IgA RF. Of 47 patients typed for HLA-DR, DR1 and DR2 were significantly more frequent in those with the highest levels of IgM RF. Conversely, DR3 was associated with low levels or absence of IgA RF and IgE RF. These results suggest that immune response genes may regulate the level of different RF isotypes. The frequencies of IgM, IgA, IgE, and IgG RF were 59%, 36%, 9%, and 27% respectively in SLE and 25%, 2.5%, 70%, and 59% in bronchial asthma.

Adult↗
PubMed1987

Intracellular localization of thymosin alpha 1 by immunoelectron microscopy using a monoclonal antibody.

Distribution of thymosin alpha 1 in normal mice (OF1) or autoimmune mice (NZB) was investigated using immunocytochemical techniques on sections of GMA- and Epon-embedded mouse thymuses. A monoclonal antibody directed against synthetic thymosin alpha 1 was used. With the immunofluorescence assay, patchy staining of thymosin alpha 1 was found in the cytoplasm of epithelial cells of the subcapsullary and medullary zones of OF1 thymus. In NZB thymus, the fluorescent pattern was less precisely localized. At the electron microscopic level, immunolabeling of Epon-embedded ultra-thin sections revealed ferritin in some vacuoles of epithelial cells. Ferritin labeling in OF1 thymus was found in several small vacuoles of the same cell, but was present in large, dense vacuoles in NZB thymus. These differences might reflect differences in the secretory process of thymic hormone.

Animals↗
PubMed1986

Antihistone antibodies detected by micro-ELISA and immunoblotting in mice with lupus-like syndrome (MRL/1, MRL/n, PN, and NZB strains).

Antihistone antibodies were searched for in autoimmune prone strains of mice: MRL/1, MRL/n, PN, and NZB by micro-enzyme-linked immunosorbent assay (micro-ELISA with total histones or H1 fraction as antigen) and immunoblotting using a solution of total histones containing H1, H2A, H2B, H3, and H4. In addition, we specified the localization of H1 fraction epitopes recognized by mouse anti-H1 autoantibodies using immunoblotting with H1 digested by alpha-1-chymotrypsin. All strains of autoimmune mice synthesize antihistone antibodies, principally MRL/1, then MRL/n and PN, and finally NZB. Among MRL/1 mice, the histone fractions best recognized by antihistone antibodies, are, in decreasing order: H1, H3, H4, H2B, and H2A. With MRL/n and, even more strikingly with PN mice, the antihistone antibodies recognize preferentially H1 and H2B as they do in human lupus. Finally, the binding of antihistone antibodies from NZB mice is slightly stronger for H2B than for the other histone fractions. The anti-H1 autoantibodies from MRL/1, MRL/n, and PN mice are mainly directed at epitopes located on the C terminal of the histone molecule.

Animals↗
PubMed1986

Comparative studies on naturally occurring antikeratin antibodies in human sera.

Comparative studies on the specificity of the so-called antiepidermal antibodies (Abs) found in human sera were performed by immunoblotting, enzyme-linked immunosorbent assay (ELISA), and immunoelectron microscopy (IEM). After a screening test by indirect immunofluorescence (IF), sera obtained from patients with various diseases and controls could be classified in 5 different groups according to the IF patterns on the epidermis: sera reactive with: (1) the stratum corneum (SC); (2) the upper layer (U-Cyt); (3) the whole epidermis (G-Cyt); (4) basal cells (B-Cyt); and (5) negative ones. By immunoblotting, all the 23 IF-positive sera were found to bind to one or more keratin bands, and did not show any reactivity with epidermal Nonidet P-40 soluble proteins. SC-Abs were mainly directed against a 67 kD Keratin band, whereas U-Cyt- and G-Cyt-Abs bound to both 58-56 kD and 67-63 kD keratins. B-Cyt-Abs reacted strongly with 63 kD Keratins and slightly with a 50 kD band. Antikeratin Abs were detected by immunoblotting even in the IF-negative sera. The ELISA study showed that sera with high IF titers contained high levels of antikeratin Abs. In the IEM study using sera containing U-Cyt- or B-Cyt-Abs, 2 distinct reaction patterns were demonstrated: U-Cyt-Abs stained tonofilaments of suprabasal keratinocytes, while B-Cyt-Abs characteristically reacted with those of basal cells. Moreover, SC-, U-Cyt-, and G-Cyt-Abs were absorbed out by insoluble epidermal proteins, and B-Cyt-Abs were decreased in titer after the absorption test. The present study provides strong evidence that most, though not all, human antiepidermal Abs are directed against different keratin polypeptides, and that antikeratin Abs commonly occur in almost all human sera.

Antibody Specificity↗
PubMed1986

Anti-H1 histone antibodies in systemic lupus erythematosus: epitope localization after immunoblotting of chymotrypsin-digested H1.

Using micro enzyme-linked immunosorbent assay (micro-ELISA) anti-H1 antibodies are most frequently seen in systemic lupus erythematosus (SLE) (61.4% of patients). Positive anti-H1 ELISA reactions are rare in rheumatoid arthritis (RA) (5.8% of cases), melanomas (16.7%), leukaemias (13.6%) and other cancers (5.6%). In SLE, the immunoglobulins (Ig) which constitute anti-H1 antibodies are, by order of importance, IgM, IgG and IgA. By means of immunoblotting using H1 solutions digested by alpha-1-chymotrypsin fixed on collagen membranes, we have shown that all the SLE sera containing anti-H1 antibodies recognize the sequential epitopes that are found on the carboxy terminal tail and, for 28% of anti-H1 sera, also the epitopes present on the aminoterminal half. The technique used did not make it possible to determine with certainty whether anti-H1 autoantibodies are also directed against the conformational epitopes of the globular part of the molecule.

Antibodies, Neoplasm↗