TY  - JOUR
A1  - Carregari, Victor Corasolla
A1  - Floriano, Rafael Stuani
A1  - Rodrigues-Simioni, Lea
A1  - Winck, Flavia V.
A1  - Baldasso, Paulo Aparecido
A1  - Ponce-Soto, Luis Alberto
A1  - Marangoni, Sergio
T1  - Biochemical, Pharmacological, and Structural Characterization of New Basic PLA(2) Bbil-TX from Bothriopsis bilineata Snake Venom
JF  - BioMed research international
N2  - Bbil-TX, a PLA(2), was purified from Bothriopsis bilineata snake venom after only one chromatographic step using RP-HPLC on mu-Bondapak C-18 column. A molecular mass of 14243.8 Da was confirmed by -Tof ltima API ESI/ MS (TOF MS mode) mass spectrometry. The partial protein sequence obtained was then submitted to BLASTp, with the search restricted to PLA(2) from snakes and shows high identity values when compared to other PLA(2)s. PLA(2) activity was presented in the presence of a synthetic substrate and showed a minimum sigmoidal behavior, reaching its maximal activity at pH 8.0 and 25-37 degrees C. Maximum PLA(2) activity required Ca2+ and in the presence of Cd2+, Zn2+, Mn2+, and Mg2+ it was reduced in the presence or absence of Ca2+. Crotapotin from Crotalus durissus cascavella rattlesnake venom and antihemorrhagic factor DA2-II from Didelphis albiventris opossum sera under optimal conditions significantly inhibit the enzymatic activity. Bbil-TX induces myonecrosis in mice. The fraction does not show a significant cytotoxic activity in myotubes and myoblasts (C2C12). The infiammatory events induced in the serum of mice by Bbil-TX isolated from Bothriopsis bilineata snake venom were investigated. An increase in vascular permeability and in the levels of TNF-a, IL-6, and IL-1 was was induced. Since Bbil-TX exerts a stronger proinfiammatory effect, the phospholipid hydrolysis may be relevant for these phenomena.
Y1  - 2013
U6  - https://doi.org/10.1155/2013/612649
SN  - 2314-6133
SN  - 2314-6141
PB  - Hindawi Publishing Corp.
CY  - New York
ER  - 
TY  - JOUR
A1  - Winck, Flavia V.
A1  - Riano-Pachon, Diego M.
A1  - Sommer, Frederik
A1  - Rupprecht, Jens
A1  - Müller-Röber, Bernd
T1  - The nuclear proteome of the green alga Chlamydomonas reinhardtii
JF  - Proteomics
N2  - Nuclear proteins play a central role in regulating gene expression. Their identification is important for understanding how the nuclear repertoire changes over time under different conditions. Nuclear proteins are often underrepresented in proteomic studies due to the frequently low abundance of proteins involved in regulatory processes. So far, only few studies describing the nuclear proteome of plant species have been published. Recently, the genome sequence of the unicellular green alga Chlamydomonas reinhardtii has been obtained and annotated, allowing the development of further detailed studies for this organism. However, a detailed description of its nuclear proteome has not been reported so far. Here, we present an analysis of the nuclear proteome of the sequenced Chlamydomonas strain cc503. Using LC-MS/MS, we identified 672 proteins from nuclei isolates with a maximum 1% peptide spectrum false discovery rate. Besides well-known proteins (e.g. histones), transcription factors and other transcriptional regulators (e.g. tubby and HMG) were identified. The presence of protein motifs in nuclear proteins was investigated by computational tools, and specific over-represented protein motifs were identified. This study provides new insights into the complexity of the nuclear environment and reveals novel putative protein targets for further studies of nuclear mechanisms.
KW  - Nuclear proteomics
KW  - Plant proteomics
KW  - Systems biology
KW  - Transcription factor
Y1  - 2012
U6  - https://doi.org/10.1002/pmic.201000782
SN  - 1615-9853
VL  - 12
IS  - 1
SP  - 95
EP  - 100
PB  - Wiley-Blackwell
CY  - Malden
ER  -