Fluoride Exposure Attenuates Expression of Streptococcus pyogenes Virulence Factors

Thongboonkerd, Visith; Luengpailin, Jiraporn; Cao, Junkai; Pierce, William M.; Cai, Jian; Klein, Jon B.; Doyle, R.J.

doi:10.1074/jbc.m200746200

Cited by 97 publications

(69 citation statements)

References 47 publications

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“…After carboxymethylation of the purified enzyme and digestion with trypsin, the peptide fragments were identified on the basis of the deduced amino acid sequence of the cDNA using electron spray ionization mass spectrometry (ESI-MS) according to previously described methods [24].…”

Section: Mass Spectrometrymentioning

confidence: 99%

Purification and characterization of glutathione peroxidase 1 in the red muscle of Pacific bluefin tuna Thunnus orientalis

et al. 2012

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Glutathione peroxidase GPx1 was purified from the red muscle of Pacific bluefin tuna Thunnus orientalis and its enzymatic properties were characterized. The enzyme was optimally active at pH 7.4 with a specific activity for hydrogen peroxide and a K m of 6.7 lM. cDNA was also isolated and it contained a predicted open reading frame (ORF) encoding a 188 amino acid protein. The phylogenetic tree shows that fish including Pacific bluefin tuna, pufferfish, and zebrafish, but not mammals, possess two genetically distinct types of GPx1, i.e., GPx1a and GPx1b. The purified enzyme was classified as a fish GPx-1b enzyme on the basis of the phylogenetic tree of the GPx1 family.

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Section: Mass Spectrometrymentioning

confidence: 99%

Purification and characterization of glutathione peroxidase 1 in the red muscle of Pacific bluefin tuna Thunnus orientalis

et al. 2012

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“…Trypsin-generated peptides were applied by a thin film-spotting procedure for MALDI-MS analysis using ␣-cyanohydroxycinnamic acid as the matrix on stainless steel targets, as described previously (45). Mass spectral data were obtained using a TOF-Spec 2E (Micromass) and a 337-nm N 2 laser at 20 -35% power in the reflector mode.…”

Section: Phosphorylation Of Wild Type and Mutant Vcp Proteins By Activementioning

confidence: 99%

Akt-mediated Valosin-containing Protein 97 Phosphorylation Regulates Its Association with Ubiquitinated Proteins

Klein

Barati

et al. 2005

Journal of Biological Chemistry

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Hypoxia is a common environmental stress that influences signaling pathways and cell function. Previous studies from our laboratory have identified significant differences in cellular responses to sustained or intermittent hypoxia with the latter proving more cytotoxic. We hypothesized that differences in susceptibility of neurons to intermittent (IH) and sustained hypoxia (SH) are mediated by altered Akt signaling. SH, but not IH, induced a significant increase in Akt activation in rat CA1 hippocampal region extracts compared with room air controls. Most mammalian neurons are sensitive to hypoxia to a varying degree. However, the mechanisms underlying this heterogeneous sensitivity are not well understood. Heterotopic differences in hypoxic sensitivity are now well established in the brain during conditions of oxygen deprivation such as hypoxic ischemia and the oxidant stress that follows reperfusion or malonate-induced mitochondrial metabolic disruption (1-4). Previous studies from our laboratory have identified significant differences in the hypoxic susceptibility of the CA1 and CA3 hippocampal regions, with CA1 vulnerability being particularly prominent in response to intermittent mild hypoxic episodes (5-7). These findings suggest that the CA3 region is relatively resistant to hypoxia when compared with the CA1 region, and CA1 regional vulnerability to hypoxia varies depending on the mode, severity, and duration of the hypoxic insult (8 -10). The mechanisms underlying the greater susceptibility of the CA1 region to intermittent hypoxia (IH) 1 than to sustained hypoxia (SH) are unknown. We have recently shown in PC-12 cells that different signaling pathways are involved in sustained and intermittent hypoxia-induced cell death. Identifying these pathways may contribute to our understanding of differential brain susceptibility to sustained and intermittent hypoxia (11). In the present study, we found that in rat CA1, SH but not IH induces significant increase in Akt activation compared with room air (RA) control, suggesting that differences in Akt signaling maybe implicated in the differences in hypoxia sensitivity in IH versus SH. Proteomic analysis of Akt immunoprecipitates from RA, SH, and IH CA1 samples was performed to identify differences in the assembly of Akt-binding partners among different conditions. These studies demonstrated that SH but not IH increased expression and association of endoplasmic reticulum (ER)-proteasome interacting protein, velosin-containing protein 97 (VCP) with Akt, compared with RA-exposed animals. Additionally, VCP was identified as an Akt substrate in vitro and in vivo thereby potentially implicating the VCP-Akt complex in the regulation of protein quality control during SH.VCP is a member of the AAA (ATPases associated with various cellular activities) family and is divided into N (residues 1-187), D1 (residues 209 -460), D2 (residues 481-761), and C (residues 742-806) domains, and two linkers, N-D1 linker (residues 188 -208) and D1-D2 linker (residues 461-

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“…In-gel tryptic digestion and MALDI-TOF MS were performed using the techniques described previously [18]. Peptide mass fingerprinting was performed using the "ProFound" search engine (http://129.85.19.192/ profound_bin/WebProFound.exe).…”

Section: In-gel Tryptic Digestion Maldi-tof Ms and Peptide Mass Finmentioning

confidence: 99%

Proteomic Identification and Immunolocalization of Increased Renal Calbindin-D28k Expression in OVE26 Diabetic Mice

Thongboonkerd¹,

Zheng²,

McLeish³

et al. 2005

Rev Diab Stud

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■ AbstractDiabetic nephropathy is a common diabetic complication that is associated with alterations in the expression of several renal proteins and abnormal calcium homeostasis. We performed proteomic analysis to screen for global changes of renal protein expression in diabetic kidney. Proteins extracted from the whole kidney of 120-day-old OVE26 (a transgenic model of Type 1 diabetes) and FVB (non-diabetic background strain) mice were separated by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) and visualized by SYPRO Ruby staining (n = 5 in each group). Quantitative intensity analysis revealed 41 differentially expressed proteins, of which 30 were identified by matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS) followed by peptide mass fingerprinting. One of the altered proteins with the greatest magnitude of change was the calcium-binding protein, calbindin-D28k, whose expression was increased 6.7-fold in diabetic kidney. We confirmed the increase in calbindin-D28k expression in diabetic kidney by Western blot analysis. Immunohistochemical study demonstrated that calbindin-D28k expression was markedly increased in tubular epithelial cells of distal convoluted tubules (DCT), collecting ducts (CD), and proximal convoluted tubules (PCT) in diabetic kidney. Calbindin-D28k plays a critical role in maintaining calcium homeostasis. The elevation in renal calbindin-D28k expression in our model may indicate a compensatory mechanism to overcome hypercalciuria in diabetes.

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Fluoride Exposure Attenuates Expression of Streptococcus pyogenes Virulence Factors

Cited by 97 publications

References 47 publications

Purification and characterization of glutathione peroxidase 1 in the red muscle of Pacific bluefin tuna Thunnus orientalis

Purification and characterization of glutathione peroxidase 1 in the red muscle of Pacific bluefin tuna Thunnus orientalis

Akt-mediated Valosin-containing Protein 97 Phosphorylation Regulates Its Association with Ubiquitinated Proteins

Proteomic Identification and Immunolocalization of Increased Renal Calbindin-D28k Expression in OVE26 Diabetic Mice

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