Search PubMed⌕ Search

Biomedical subjects

R Mayer

Publications and source records attributed to R Mayer.

At least 199 records · Page 11Linked to original sources

Concomitant osteitis fibrosa cystica and ameloblastoma of the mandible.

A patient with a multiloculated cystic lesion of the mandible, and clinical as well as biological features of hyperparathyroidism is presented. This association suggesting the diagnosis of brown tumor was actually due to an ameloblastoma of the mandible. Such a concomitant association of an ameloblastoma with symptomatic hyperparathyroidism has never been reported to our knowledge.

Adenoma↗

[Facial malformations and asymmetries caused by the first and second branchial arch syndrome].

The first and second branchial arch syndrome is a congenital affection, among whom one can range as well hereditary as non-hereditary entities. They always cause a badly mutilating facial asymmetry. In this article, the first and second branchial arch syndrome were divided in hemifacial and bilateral dysostoses. We pointed out the hemifacial microsomia, the most occurring entity in these series. From two case reports, we attempt to give a treatment synopsis of this syndrome, which is always done by a multi-disciplinary team, including dentists, orthodontists, maxillofacial surgeons and plastic surgeons.

Adult↗

Biased usage of certain Vk gene families by autoantibodies and their polymorphism in autoimmune mice.

Of 79 hybridomas derived from stimulated or unstimulated autoimmune disease prone mouse strains, secreting autoantibodies of various specificities more than 65% use V genes from five Vk families, namely, Vk1, Vk4, Vk8, Vk10 and Vk19. Restriction fragment length polymorphism (RFLP) analysis of genomic DNAs from autoimmune prone mouse strains, tight skin, NZB and SJL show marked differences in the polymorphism of the Vk1, Vk10 and Vk19 gene families.

Animals↗

Neutral proteases involved in the reinvasion of erythrocytes by Plasmodium merozoites.

Neutral proteases of Plasmodium sp erythrocytic stages were studied by means of a sensitive fluorogenic method and gelatin-SDS-PAGE. The substrates gluconoyl-Val-Leu-Gly-Lys(or Arg)-3-amido-9-ethylcarbazole were selectively hydrolyzed by an endopeptidase from rodent Plasmodium berghei (Pb) and Plasmodium chabaudi (Pc) and from human Plasmodium falciparum (Pf) parasites. These endopeptidases were purified from 100,000-g soluble schizont extract by high pressure liquid chromatography; they have a similar Mr of 68,000 in SDS-PAGE, and an optimal activity at pH 7.4. The Pb 68 and Pf 68 endopeptidases were localized in schizonts and also in merozoites as shown by indirect immunofluorescence on Pb merozoites and by the identification of the Pf 68 endopeptidase activity in free viable merozoites. The Pb 68 and Pf 68 endopeptidases belong to the class of cysteine proteases. Analysis by gelatin-SDS-PAGE of a Pb 68 endopeptidase-enriched fraction showed a reproducible 95,000 proteolytic band. The initial extracts showed a similar 95,000 proteolytic band, and also 2 other 90,000 and 85,000 major bands. During reinvasion experiments, it was possible to recover a 95,000 and a 40,000 protease band from supernates of cultures grown in a semidefined medium without serum. Hydrophilic peptide derivatives related to the substrate of Pf 68 endopeptidase are shown to be potential inhibitors of the Pf reinvasion process in vitro.

Animals↗

Is serum fructosamine assay specific for determination of glycated serum protein?

We compared the fructosamine activity in sera from healthy and diabetic subjects with the degree of protein glycation detected by a liquid-chromatographic method. The latter technique measures furosine as a specific product after hydrolysis of epsilon-amino-fructose-lysine. Our results indicate that the fructosamine assay measures the extent of glycation of purified human serum albumin correctly. On the other hand, we found no correlation between the two methods for sera from healthy subjects, although for diabetics' sera the values obtained with both methods were related. However, only about half of the reducing activity (fructosamine) was due to specific nonenzymatic glycation of proteins in healthy subjects and well-controlled diabetics. The remaining unspecific activity varied from serum to serum. It was not reducible with NaBH4 and was independent of the glycation of albumin, which normally accounts for about 80% of glycated serum proteins. The fructosamine assay is therefore of limited specificity for the exact measurement of glycated proteins in serum.

Blood Proteins↗