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Biomedical subjects

A Mauron

Publications and source records attributed to A Mauron.

At least 19 recordsLinked to original sources
PubMed2006

[Neuroethics].

Explore the source record for details and available documents.

Humans↗
PubMed2002

'He found me very well; for me, I was still feeling sick': the strange worlds of physicians and patients in the 18th and 21st centuries.

It is commonplace today to deplore the dissatisfaction of patients with the physician-patient relationship. Furthermore, historical investigation shows that this problem is not really new. We investigated an important source of patients' views in the 18th century, namely the letters of patients received by the famous Swiss physician, Samuel Tissot, and noted remarkably similar feelings of frustration. Yet the medical paradigms of today and of Tissot's times are considerably different. We propose that the persisting problems in the physician-patient relationship are due to a basic dissonance between the patient's ordinary modes of perception and the systematic way of perceiving reality characteristic of the physician. In addition, they reflect the unavoidable chasm between the ultimately private and singular nature of the illness experience, and the general and anonymous stance of medical theory. This chasm is therefore a permanent feature of the patient-physician relationship, predating the advent of scientific medicine, even if the latter reinforced it. In line with the current medical humanities movement, we believe that the engagement of physicians and medical students with literature and the arts helps them explore, and to some extent overcome, the existential divide between the patient's experiential self knowledge and the systematic, impersonal knowledge that plays a central role in medicine. We suggest a few examples of contemporary fiction that may be relevant and useful in this respect.

Communication↗
PubMed1999

[The new molecular physician: engineer, soothsayer or health advisor?].

The label of molecular medicine stands for a variety of scientific, diagnostic and therapeutic developments. While these aspects of modern medicine have relatively little in common in terms of the ethical tissues they raise, they change the overall philosophy of medicine in characteristic ways. These changes are analysed in terms of three somewhat non-traditional dimensions of medical practice: the engineering's deal, the predictive dimension, and the role of the doctor as personal health advisor.

Bioethics↗
PubMed1991

Germ-line engineering: a few European voices.

We have surveyed various recent European opinions on germ-line engineering. The majority express more or less severe reservations about any interventions on the human germ-line, including therapeutic ones. However, they are divided over the pragmatic, or categorical-ethical nature of the relevant arguments. This split reflects two competing views of technology. The 'pessimistic' one is deeply concerned by the slippery slope leading from bona fide therapeutic applications of genetic engineering to eugenic practices. It insists that, if anything can defend us against these evils, it must be a set of strong, ethically-based prohibitions. The other, 'optimist' view is more confident in the discriminating powers of societal regulation. We argue for the latter view and suggest that the pragmatic arguments brought to this debate are less problematic than the ethical ones.

Advisory Committees↗
PubMed1989

Autoimmune T lymphocytes in myasthenia gravis. Determination of target epitopes using T lines and recombinant products of the mouse nicotinic acetylcholine receptor gene.

Oligoclonal and cloned T lines from peripheral blood or thymuses of patients with myasthenia gravis (MG) were selected for reactivity against nicotinic acetylcholine receptors (AChR) from Torpedo california, or against a recombinant fusion peptide, X4, representing the extracellular portion of the mouse AChR alpha-chain. All cell lines expressed the CD4 membrane phenotype, and their antigen reactivity was blocked by antibodies against monomorphic HLA DR/DP determinants. Using a panel of fusion proteins of different, overlapping mouse AChR alpha-chain sequences, a major T cell epitope was localized between amino acid positions 85 and 142. This determinant was distinct from the humoral main immunogenic region, which has been identified on the sequence 61-76. The response pattern of uncloned T lines from three patients with different HLA haplotypes suggests, however, that in any one MG patient T lymphocytes may recognize more than one autoantigenic epitope on the AChR alpha-chain, and that the T lymphocyte response profiles vary among individual patients.

Adult↗
PubMed1988

Monoclonal antibodies to the main immunogenic region of the nicotinic acetylcholine receptor bind to residues 61-76 of the alpha subunit.

Monoclonal antibodies (mAbs) to the main immunogenic region (MIR) bind to fusion proteins containing region 37-200 of the alpha chain of Torpedo, mouse, and chicken nicotinic acetylcholine receptor. In the case of the mouse alpha chain, these mAbs react with sequence 61-216 but not with 74-216. A synthetic peptide M1, containing residues 61-76 of the mouse alpha chain, also binds these anti-MIR mAbs, showing that all or part of their binding site is included in this region. The conformational dependence and epitope specificity of the mAbs are discussed.

Amino Acid Sequence↗
PubMed1987

Mapping the main immunogenic region and toxin-binding site of the nicotinic acetylcholine receptor.

The alpha-chain of the nicotinic acetylcholine receptor carries the binding sites both for cholinergic ligands and for most experimentally induced or naturally occurring antibodies to the native receptor. By means of expression cloning in Escherichia coli, fusion proteins were derived from specific fragments of a complementary DNA encoding the mouse alpha-chain, allowing the mapping of the toxin-binding site to residues 160-216 and the main immunogenic region to residues 6-85. This approach permits the independent study of different functional domains of a complex receptor molecule and should be generally applicable to other proteins for which complementary DNA clones are available.

Amino Acid Sequence↗
PubMed1985

Constitutively expressed rat mRNA encoding a 70-kilodalton heat-shock-like protein.

A nearly full-length cDNA clone isolated from the rat pheochromocytoma cell line, PC12, revealed extensive nucleotide sequence similarity between the rat cDNA and the Drosophila melanogaster hsp70 gene. The rat recombinant clone encodes a 71,000-dalton protein that is 70% identical with the dipteran hsp70 protein. Remarkably, a truncated segment of this cDNA clone was originally isolated by immunoreactivity with antisera raised to catecholamine-synthesizing enzymes, suggesting that this heat shock protein and these catecholamine enzymes shared antigenic determinants. The rat hsp70-related mRNA is responsible for the production of a constitutive hsp70 protein, because it is present in abundant amounts in various tissues at normal growth temperatures and is only minimally induced by hyperthermia. The rat hsp70-related sequence is part of a multigene family that extends across species to mice and humans.

Animals↗
PubMed1984

Structure linkage, and sequence of the two genes encoding the delta and gamma subunits of the nicotinic acetylcholine receptor.

We have cloned and sequenced a fragment of the chicken genome approximately 9 kilobases in length that comprises the genes encoding the delta and gamma subunits of the nicotinic acetylcholine receptor. The two genes are homologous and have identical structures: both consist of 12 exons, some of which precisely correspond to predicted structural domains of the receptor subunits. The delta and gamma subunit genes are encoded by the same DNA strand and are very closely linked, there being only 740 base pairs between the last codon of delta and the initiator codon of gamma. Blot analysis demonstrates that the genes we describe are unique in the genome. Comparison of the predicted protein sequence for the corresponding subunits of chicken and of the elasmobranch Torpedo reveals a high degree of conservation in some but not all of the protein domains.

Amino Acid Sequence↗