Comparative effects of high-intensity interval training and moderate-intensity continuous training on soleus muscle fibronectin type III domain-containing protein 5, myonectin and glucose transporter type 4 gene expressions: a study on the diabetic rat model

Molecular Biology Reports - The increase in fibronectin type-III domain-containing protein 5 (FNDC5), myonectin, and glucose transporter 4 (GLUT4) leads to a decrease in diabetes; meanwhile,...     

Diversity of the rotifer Brachionus plicatilis species complex (Rotifera: Monogononta) in Iran through integrative taxonomy

Faunistic survey using a DNA taxonomy approach may provide different results from morphological methods, especially for small and understudied animals. In this study, we report the results from morphometric analyses (linear measurements of the lorica) and DNA taxonomy (generalized mixed Yule coalescent model on the barcoding mtDNA locus cytochrome c oxidase subunit I) performed on 15 clonal lineages of the rotifer Brachionus plicatilis species complex from six Iranian inland saltwaters. The DNA taxonomy approach found more units of diversity (four) than the morphometric approach (two) in the studied rotifers. Three of the taxa identified in this study are already known as described valid species or as‐yet unnamed lineages, but a new, additional lineage is also identified from Iran. © 2014 The Linnean Society of London     

The amino-terminal peptide of HIV-1 glycoprotein 41 lyses human erythrocytes and CD4+ lymphocytes.

Functional studies assessed the cytolytic activity of the amino terminal peptide (FP-I; 23 residues 519-541) of the glycoprotein 41,000 (gp41) of the Human Immunodeficiency Virus Type-1 (HIV-1). Synthetically prepared FP-I efficiently hemolyzed human red blood cells at 37 degrees C, with 40% lysis at 32 microM. Kinetic studies indicated that FP-I induced maximal hemolysis in 30 min, probably through tight binding of the peptide with the red cell membrane. The Phe-Leu-Gly-Phe-Leu-Gly (residues 526-531) motif in FP-I apparently plays a critical role in lysis of red cells, since no hemolytic activity was observed for an amino-acid-substituted FP-I in which the unique Phe-Leu-Gly-Phe-Leu-Gly was converted to Ala-Leu-Gly-Ala-Leu-Gly. As neither smaller constituent peptides (e.g., residues 519-524 and residues 526-536) nor a N-terminal flanking peptide (e.g., residues 512-523) induced red cell hemolysis, the entire 23-residue (519-541) sequence of FP-I may be required for hemolytic activity. FP-I was also cytolytic with CD4(+)-bearing Hut-78 cells, with 40% lysis at approx. 150 microM. These results are consistent with an earlier hypothesis that the N-terminal peptide of gp41 may partially contribute to the in vivo cytopathic actions of HIV-1 infection (Gallaher, W.R. (1987) Cell 50, 327-328).