Habitat deterioration promotes the evolution of direct development in metamorphosing species

Although metamorphosis is widespread in the animal kingdom, several species have evolved life-cycle modifications to avoid complete metamorphosis. Some species, for example, many salamanders and newts, have deleted the adult stage via a process called paedomorphosis. Others, for example, some frog species and marine invertebrates, no longer have a distinct larval stage and reach maturation via direct development. Here we study which ecological conditions can lead to the loss of metamorphosis via the evolution of direct development. To do so, we use size-structured consumer-resource models in conjunction with the adaptive-dynamics approach. In case the larval habitat deteriorates, individuals will produce larger offspring and in concert accelerate metamorphosis. Although this leads to the evolutionary transition from metamorphosis to direct development when the adult habitat is highly favorable, the population will go extinct in case the adult habitat does not provide sufficient food to escape metamorphosis. With a phylogenetic approach we furthermore show that among amphibians the transition of metamorphosis to direct development is indeed, in line with model predictions, conditional on and preceded by the evolution of larger egg sizes.     

Familial breast/ovarian cancer and BRCA1/2 genetic screening: the role of immunohistochemistry as an additional method in the selection of patients.

Only 20-25% of families screened for BRCA1/2 mutations are found positive. Because only a positive result is informative, we studied the role of BRCA1/2 immunohistochemistry as an additional method for patient selection. From 53 high-risk-affected probands, 18 (34%) had available paraffin blocks of their tumors and were selected for this study. Mutation screening was done by conformation-sensitive gel electrophoresis and multiplex ligation-dependent probe amplification. For immunohistochemistry, 21 neoplastic specimens (15 breast carcinomas, 5 ovary neoplasms, and 1 rectal adenocarcinoma) were analyzed with BRCA1 (monoclonal antibody, Ab-1, oncogene) and BRCA2 (polyclonal antibody, Ab-2, oncogene) antibodies. Absence of the BRCA1 protein was confirmed in negative tumors by Western blotting. Seven patients were positive for BRCA1/2 mutations: 5 for BRCA1 and 2 for BRCA2. Four out of five positive patients had tumors negative for BRCA1 immunostaining, and the remaining 13 BRCA1-negative patients had positive BRCA1 immunostaining in all tumor samples. Sensitivity to predict for BRCA1 mutation carriers was 80%, and specificity was 100%, with a positive predictive value of 100% and a negative predictive value of 93%. This correlation was statistically significant (p=0.001). No correlation was observed for BRCA2. If larger studies confirm these results, high-risk patients with BRCA1-negative tumors should be screened first for this gene.     

Calcium-dependent binding of EDTA-extractable proteins to calf lens fiber membrane structures

Calf lens fiber membranes and fractions enriched in junction-like structures have been isolated in the absence and presence of EDTA. Their biochemical features have been studied. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and immunoblotting experiments have provided evidence that a distinct group of EDTA-extractable proteins, being one of the main protein components of calf lens fiber membranes and very likely also of junction-like structures, is bound to these membranes via calcium ions. In addition to these proteins, four polypeptides with apparent molecular weights between 14 000 and 17 000 are characteristic for detergent-insoluble lens fiber structures prepared in calcium-rich medium. The absence of EDTA-extractable proteins in the urea-soluble calcium-containing fraction implies that they are not components of the cytoskeleton and that the calcium-dependent binding of these proteins to the membrane is urea-resistant. The use of EDTA throughout the whole membrane isolation procedure results in their complete removal from the membranes which already starts during buffer washing. This indicates that EDTA-extractable proteins exclusively consist of extrinsic membrane proteins which probably are not involved in cytoskeleton binding.     

Allylic palladium(II) triazenido complexes: synthesis and spectroscopic studies

Reaction of [Pd(1-3-η-allyl)Cl]₂ with lithium triazenide (triazenide = p-XC₆H₄NN-NC₆H₄X-p; X = Cl, H, CH₃) affords dimeric complexes of the type [Pd(1-3-η-allyl)(triazenide)]₂. In the solid state the triazenido ligands are bridging two palladium atoms with their terminal nitrogen atoms, as shown by a preliminary X-ray determination of the complex with X = CH₃. The allyl groups are stereochemically equivalent. ¹H NMR spectra demonstrate the presence of two conformers in solution. The major component has the same configuration found in the solid. The other conformer has stereochemically non equivalent allyl groups. The concentration ratio of the two conformers is independent of the temperature, suggesting the absence of intramolecular processes and of palladium- triazenido bond breaking. This point is discussed also by comparing the (1-3-η-allyl)(triazenide)palladium (II) dimers with the closely related(1-3-η-allyl)(acetate)palladium(II) complexes.