A new species of Mycterothrips Trybom (Thysanoptera: Thripidae) from India with new record of the genus Paithrips Nonaka & Jangvitaya

Mycterothrips nainiae sp. n. (Thripinae) is described and illustrated from India, and one genus and species, Paithrips circularis Nonaka and Jangvitaya, is newly recorded from India. A key to species of Mycterothrips from India is also provided. The DNA barcode data using partial mitochondrial cytochrome c oxidase subunit I (mtCOI) from the holotype also five sequences of Paithrips circularis were generated.

A new species of Homatula (Teleostei: Cobitoidea: Nemacheilidae) from the Pearl River, China

Analyses of morphological and molecular data from specimens of Homatula from China reveal an undescribed species which lives in the Nanpanjiang River, the upper Pearl River, and indicate that H. acuticephala is a synonym of H. anguillioides. The new species is collected from Yunnan, China. It differs from its congeners by having a naked and robust body, developed adipose crests (depth of caudal peduncle in the percent of its length:70.53–78.48), a median notch on the lower jaw, a median gap on the lower lip, short barbels with maxillary barbels extend posteriorly reaching the anterior edge of eyes, vertebrae 37–38, completed lateral line. New species differs from other species of Homatula by 0.05–0.11 in K2P distance of mitochondrial cytochrome c oxidase subunit 1. Phylogenetic analysis based on mitochondrial cytochrome c oxidase subunit 1 indicate that new species formed a sister group to co-drainage species. Based on both morphological and molecular results, we confirm that the validation of this undescribed species named H. robusta sp. nov. and describe it.

Saussurea lappa Exhibits Anti-Oncogenic Effect in Hepatocellular Carcinoma, HepG2 Cancer Cell Line by Bcl-2 Mediated Apoptotic Pathway and Mitochondrial Cytochrome C Release

Background and Objectives: Saussurea lappa (S. lappa) is an important species of the Asteraceae family with several purposes in traditional medicine. This study intended to explore the cytotoxic effect of S. lappa on HepG2 cancer cell proliferation. Materials and Methods: The effects of an S. lappa n-butanol extract on the induction of apoptosis were investigated by flow cytometry and mitochondrial cytochrome C-releasing apoptosis assay. Additionally, real-time PCR was employed to confirm apoptosis initiation. Further, qualitative estimation of the active constituent of S. lappa was done by gas chromatography–mass spectroscopy (GC–MS). Results: The cell viability study revealed that the n-butanol extract of S. lappa demonstrated potent cytotoxicity against HepG2 cancer cells, with an IC50 value of 56.76 μg/mL. Cell morphology with dual staining of acridine orange (AO)-ethidium bromide (EB) showed an increase in orange/red nuclei due to cell death by S. lappa n-butanol extract compared to control cells. Apoptosis, as the mode of cell death, was also confirmed by the higher release of cytochrome C from mitochondria, the increased expression of caspase-3 and bax, along with down regulation of Bcl-2. Conclusion: These findings conclude that S. lappa is a cause of hepatic cancer cell death through apoptosis and a potential natural source suggesting furthermore investigation of its active compounds that are responsible for these observed activities.

Amino Acid Substitutions in the Non-Ordered Ω-Loop 70–85 Affect Electron Transfer Function and Secondary Structure of Mitochondrial Cytochrome c

The secondary structure of horse cytochrome c with mutations in the P76GTKMIFA83 site of the Ω-loop, exhibiting reduced efficiency of electron transfer, were studied. CD spectroscopy studies showed that the ordering of mutant structure increases by 3–6% compared to that of the WT molecules due to the higher content of β-structural elements. The IR spectroscopy data are consistent with the CD results and demonstrate that some α-helical elements change into β-structures, and the amount of the non-structured elements is decreased. The analysis of the 1H-NMR spectra demonstrated that cytochrome c mutants have a well-determined secondary structure with some specific features related to changes in the heme microenvironment. The observed changes in the structure of cytochrome c mutants are likely to be responsible for the decrease in the conformational mobility of the P76GTKMIFA83 sequence carrying mutations and for the decline in succinate:cytochrome c-reductase and cytochrome c-oxidase activities in the mitoplast system in the presence of these cytochromes c. We suggest that the decreased efficiency of the electron transfer of the studied cytochromes c may arise due to: (1) the change in the protein conformation in sites responsible for the interaction of cytochrome c with complexes III and IV and (2) the change in the heme conformation that deteriorates its optimal orientation towards donor and acceptor in complexes III and IV therefore slows down electron transfer. The results obtained are consistent with the previously proposed model of mitochondrial cytochrome c functioning associated with the deterministic mobility of protein globule parts.