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Biomedical subjects

C Lapresle

Publications and source records attributed to C Lapresle.

At least 37 records · Page 2Linked to original sources

Study of the antigenic structure of human serum albumin with monoclonal antibodies.

Analysis of the antigenic structure of human serum albumin was undertaken using monoclonal antibodies. Nineteen antibodies were prepared and their specificities were studied using fragments which encompass the whole sequence of the albumin molecule. These antibodies recognized 13 different epitopes which are different from the one previously identified with two other monoclonal antibodies [Doyen et al., Immun. Lett. 3, 365-370 (1981)]. Among those 13 different epitopes, six were overlapping. Four epitopes were located on the N-terminal half of the albumin molecule. One of these required integrity of methionine 87 and the other three were overlapping and located around methionine 123. Eight epitopes were located on the C-terminal half of the albumin. Two of them were within the sequence, 330-422 and 299-496 respectively; the other six appeared to be topographic determinants which were altered or lost in the albumin fragments. A last epitope could not be located on any region of albumin. Four monoclonal antibodies directed against a given portion of the albumin molecule reacted slightly with another part of albumin, thus confirming the existence of an intramolecular cross-reactivity between the different domains of human albumin.

Animals↗

[8 cases of drug-resistant Plasmodium falciparum malaria contracted in Mozambique].

Between April and June 1984, eight chloroquine-resistant P. falciparum malaria cases were observed in non-immune patients after their emergency sanitary return from NE Mozambique. In vivo resistance to amodiaquine and pyrimethamine were demonstrated from two isolates. Radical cure was obtained with mefloquine in all cases. These patients came from an expatriate community of 35 adult men among which six other chloroquine-resistant malarial cases were probable. The epidemic pattern of this chloroquine-resistant focus is underlined.

Adult↗

[Digital tenosynovitis caused by non-tuberculous mycobacteria. Apropos of the 4th case caused by Mycobacterium terrae].

A 75 year old man developed chronic flexor tenosynovitis in a finger, caused by Mycobacterium terrae. He had a history of diabetes mellitus and arteritis, but not of local trauma. However, triamcinolone had been injected into the tendon sheath on 3 occasions. Chemotherapy was instituted, but after 3 months amputation became mandatory. This is the fourth case reported in which M. terrae was involved, and it supports the responsibility of this organism as a human pathogen. Attention is drawn to the hazards of corticosteroid injections into tendon sheaths.

Aged↗

[Major intolerance to carbamazepine. Acquired immunodepression or allergy?].

The authors report the case of an eight-year-old boy who developed erythroderma under carbamazepine. Other findings were enlarged lymph nodes, slight hepatic cytolysis, leuconeutropenia and decrease in the three classes of immunoglobulins. The immunosuppressive effect of the drug is recalled. Respective responsibility of immunosuppression and allergy is discussed.

Carbamazepine↗

Study of an antigenic site of human serum albumin with monoclonal antibodies.

Two monoclonal anti-HSA antibodies, HA1 and HA2, have been shown to be specific for a univalent fragment of 6000 mol. wt, F1, located near the C-terminus of HSA (Doven, Pesce & Lapresle, Immunology Letters 3, 365-370, 1981). Both monoclonal antibodies have been shown to react with the same site, which includes the following components: the last small loop of HSA (558-567) the disulfide bridge 514-559 and the residue 570. This site is as available on HSA and F1, but partially masked on the 'Inhibitor' fragment from which F1 derives. Polyclonal anti-F1 antibodies, purified from rabbit sera or mouse ascites by affinity chromatography, react with the same site as HA1 and HA2. However, polyclonal antibodies are heterogenous, most probably because they consist of anti-F1 specific antibodies and of antibodies specific against other parts of the albumin molecule which cross-react with F1. In addition, monoclonal antibodies can recognize the mutation of a single amino acid residue in the albumin molecule.

Albumins↗

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↗

[Prevention of inter-human rabies transmission after corneal graft].

Transplantation, to a normal recipient, of a cornea taken from a donor who died of rabies encephalitis constitutes an extremely serious exposure. Four cases, up to now are known of human to human transmission of rabies virus. In these four cases, the diagnosis of rabies in the donor has been made afterwards when to the recipient developed fatal rabies. We report here the first case of this type of exposure where the diagnosis of rabies in the donor could be made on the day following the transplantation thus allowing application, without delay, the recipient of a prophylactic therapy for inactivated rabies vaccine administered. No signs or symptoms of rabies appeared and, more than three months after the transplantation, the recipient is well and alive.

Adult↗

[Comparative study of quantitative changes in serum proteins in human pathology (author's transl)].

Five proteins (albumin, orosomucoid, IgG, IgM and IgA) were assayed by simple radial immunodiffusion method in the sera of 345 healthy subjects and 5 000 patients suffering from some 200 different diseases. The results were analyzed by computer, and from concomitant changes in individual protein levels it was possible to divide the subjects into eleven groups, each group having a distinctive protein profile. These profiles are characteristic of either a disease (e.g. group VI for virus hepatitis, group VII for trypanosomiasis) or of a physiopathological process (e.g. group II for inflammation, group V for liver damage, group VIII for hypogammaglobulinaemia due to anabolic deficiency and group IX for the same condition due to passage of serum proteins into the extravascular compartment), or they have a prognostic value (e.g. group I).

Adolescent↗

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↗

[Trypanosomiasis presenting with trypanids and complicated by myopericarditis (author's transl)].

In a 26-year-old man who had spent time in a trypanosome endemic zone, lesions of erythema marginatum progressing by acute exacerbations for 2 years despite various forms of treatment led to the discovery of a multiple lymphadenopathy and a greatly accelerated sedimentation rate. These findings suggested a diagnosis which was confirmed by the discovery of Trypanosoma gambiense in the blood and lymph node aspirate. In addition, there was an albumino-lymphocytic reaction in the cerebrospinal fluid. Finally, an atrioventricular block was discovered. All these symptoms and signs responsed to treatment with melarsoprol but a pericardial reaction developed, possibly of immunoallergic origin.

Adult↗

Partial non-cleavage by cyanogen bromide of a methionine--cystine bond from human serum albumin and bovine alpha-lactalbumin.

When human albumin was treated with CNBr, a fragment designated D was obtained and attributed to the absence from some of the albumin molecules of methionine at position 123 [Lapresle & Doyen (1975) Biochem. J. 151, 637-643]. The present study shows that methionine-123 is converted into homoserine without cleavage of the subsequent methionine-cystine bond. With bovine alpha-lactalbumin, a further example of non-cleavage of a methionine-cystine bond with conversion of methionine into homoserine is reported.

Amino Acids↗

Chemical structure of two fragments of human serum albumin and their location in the albumin molecule.

1. 'Inhibitor fragment' isolated from human serum albumin degraded by rabbit cathepsin D is composed of one peptide chain with two intrachain disulphide bonds. There are two kinds of inhibitor molecules having different N-terminal amino acids: one is threonine and the other glutamine. 2. Fragment F1, isolated from inhibitor degraded by trypsin, is composed of two chains linked by a disulphide bond. There are three kinds of fragment F1. All have one alpha chain in common, which has an intrachain disulphide bond. They differ by the nature of the chain, which is linked to the alpha chain by a disulphide bond. The epsilon chain is present in trace amounts. The two other chains, beta and gamma, differ by their C-terminal amino acid, which is respectively arginine and lysine. 3. Inhibitor is composed of the last 92 or 89 residues of the human albumin molecule and fragment F1 is composed of two parts of this C-terminal portion of the albumin molecule.

Alkylation↗

Isolation and properties of a fragment of human serum albumin demonstrating the absence of a methionine residue from some of the albumin molecules.

1. A fragment designated D was isolated from human serum albumin degraded by CNBr. Its properties show that it is made up of the B and C fragments isolated by McMenamy et al. (1971) (J. Biol. Chem., 246, 4744-4750). 2. Reduction of fragment D gives rise to two chains, one of which consists of the second subfragment of reduced fragment B linked to fragment C by an amino acid different from methionine. It thus demonstrates the existence of albumin molecules from which the second methionine residue located between fragments B and C is missing.

Amino Acids↗