Mitochondrial carrier homolog 2 (MTCH2): The recruitment and evolution of a mitochondrial carrier protein to a critical player in apoptosis.

Exp Cell Res . 2012 Feb 3; Robinson AJ, Kunji ER, Gross A Recent studies report mitochondrial carrier homolog 2 (MTCH2) as a novel and uncharacterized protein that acts as a receptor-like protein for the truncated BH3-interacting domain death agonist (tBID) protein in the outer membrane of mitochondria. These studies using mouse embryonic stem cells and fibroblasts, as well as mice with a conditional knockout of MTCH2 in the liver showed that deletion of MTCH2 hindered recruitment of tBID to the mitochondria with subsequent reductions in the activation of pro-apoptotic proteins, mitochondrial outer membrane permeabilization and apoptosis.

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Mitochondrial carrier homolog 2 (MTCH2): The recruitment and evolution of a mitochondrial carrier protein to a critical player in apoptosis.

Mitochondrial carrier homolog 2 (MTCH2): The recruitment and evolution of a mitochondrial carrier protein to a critical player in apoptosis.

Exp Cell Res . 2012 Feb 3; Robinson AJ, Kunji ER, Gross A Recent studies report mitochondrial carrier homolog 2 (MTCH2) as a novel and uncharacterized protein that acts as a receptor-like protein for the truncated BH3-interacting domain death agonist (tBID) protein in the outer membrane of mitochondria. These studies using mouse embryonic stem cells and fibroblasts, as well as mice with a conditional knockout of MTCH2 in the liver showed that deletion of MTCH2 hindered recruitment of tBID to the mitochondria with subsequent reductions in the activation of pro-apoptotic proteins, mitochondrial outer membrane permeabilization and apoptosis

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Mitochondrial carrier homolog 2 (MTCH2): The recruitment and evolution of a mitochondrial carrier protein to a critical player in apoptosis.

Analysis of multiple Leptospira vaccine proteomes and identification of LipL32 as a biomarker for potency.

Clin Vaccine Immunol . 2012 Feb 8; Humphryes PC, Weeks ME, Gielbert A, Thomson G, Coldham NG The current batch potency test for Leptospira interrogans serovar Canicola vaccines requires the use of a large number of hamsters and has severe effects (i.e. hepatic and renal failure resulting in death); whilst effective, a safer, cheaper, more ethical replacement is desired

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Analysis of multiple Leptospira vaccine proteomes and identification of LipL32 as a biomarker for potency.

The Arabidopsis voltage-dependent anion channel 2 is required for plant growth.

Plant Signal Behav. 2012 Jan 1; 7(1): 31-3
Tateda C, Kusano T, Takahashi Y

The voltage-dependent anion channels (VDACs) known as a major group of outer mitochondrial membrane proteins are present in all eukaryotic species. In mammalian cells, they have been established as a key player in mitochondrial metabolism and apoptosis regulation. By contrast, little is known about the function of plant VDACs. Recently, we performed functional analysis of all VDAC gene members in Arabidopsis thaliana, and revealed that each AtVDAC member has a specialized function. Especially, in spite of similar subcellular localization and expression profiling of AtVDAC2 and AtVDAC4, both the T-DNA insertion knockout mutants of them, vdac2-2 and vdac4-2, showed severe growth retardation. These results suggest that AtVDAC2 and AtVDAC4 proteins clearly have distinct functions. Here, we introduced the AtVDAC2 gene into the vdac2-2 mutant, and demonstrated that the miniature phenotype of vdac2-2 plant is abolished by AtVDAC2 expression.

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The Arabidopsis voltage-dependent anion channel 2 is required for plant growth.

Elucidation of the Involvement of p14, a Sperm Protein during Maturation, Capacitation and Acrosome Reaction of Caprine Spermatozoa.

PLoS One. 2012; 7(1): e30552
Nandi P, Ghosh S, Jana K, Sen PC

Mammalian sperm capacitation is an essential prerequisite to fertilization. Although progress is being made in understanding the physiology and biochemistry of capacitation, little has been yet explored about the potential role(s) of individual sperm cell protein during this process. Therefore elucidation of the role of different sperm proteins in the process of capacitation might be of great importance to understand the process of fertilization. The present work describes the partial characterization of a 14-kDa protein (p14) detected in goat spermatozoa using an antibody directed against the purified protein. Confocal microscopic analysis reveals that the protein is present in both the intracellular and extracellular regions of the acrosomal and postacrosomal portion of caudal sperm head. Though subcellular localization shows that p14 is mainly cytosolic, however it is also seen to be present in peripheral plasma membrane and soluble part of acrosome. Immuno-localization experiment shows change in the distribution pattern of this protein upon induction of capacitation in sperm cells. Increased immunolabeling in the anterior head region of live spermatozoa is also observed when these cells are incubated under capacitating conditions, whereas most sperm cells challenged with the calcium ionophore A23187 to acrosome react, lose their labeling almost completely. Intracellular distribution of p14 also changes significantly during acrosome reaction. Interestingly, on the other hand the antibody raised against this 14-kDa sperm protein enhances the forward motility of caprine sperm cells. Rose-Bengal staining method shows that this anti-p14 antibody also decreases the number of acrosome reacted cells if incubated with capacitated sperm cells before induction of acrosome reaction. All these results taken together clearly indicate that p14 is intimately involved and plays a critical role in the acrosomal membrane fusion event.

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Elucidation of the Involvement of p14, a Sperm Protein during Maturation, Capacitation and Acrosome Reaction of Caprine Spermatozoa.

Identification of differentially expressed proteins in the spinal cord of neuropathic pain models with PKCgamma silence by proteomic analysis.

Brain Res. 2012 Jan 2;
Zou W, Zhan X, Li M, Song Z, Liu C, Peng F, Guo Q

In order to elucidate the mechanisms that PKCγ regulates neuropathic pain (NP), and detect proteins that are associated with the function of PKCγ in NP, we exploited a chronic constriction injury (CCI)-induced neuropathic pain rat (CCI-NP rat) model in which PKCγ knockdown in the spinal cord was successfully carried out with stable RNA interference (RNAi). The spinal cords (L4-L5) were surgically obtained from CCI-NP rats with and without PKCγ knockdown, for comparative proteomic analysis. The total proteins from the spinal cords (L4-L5) were extracted and were separated with two-dimensional gel electrophoresis (2DGE). 2D gel images were analyzed with PDQuest software. Nineteen differential gel-spots were identified with spot-volume increased and 17 spots with spot-volume decreased. Among them, eighteen differentially expressed proteins (DEPs) were identified with matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF MS) between CCI-NP rats with and without PKCγ knockout. Those DEPs are involved in transmission and modulation of noxious information; cellular homeostasis and metabolism; antioxidant proteins, heat shock proteins and chaperones; membrane receptor trafficking; and cytoskeleton. Three DEPs (SNAP-25, TERA and AR) were validated with Western blot analysis, and confirmed the DEP data. Further study showed that AR-selective inhibitor epalrestat totally turned over the upregulated expression of AR in CCI-NP rats. Those DEP data are extensively associated with the function of PKCγ that regulates NP, and would contribute to the clarification of the mechanisms of PKCγ in NP.

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Identification of differentially expressed proteins in the spinal cord of neuropathic pain models with PKCgamma silence by proteomic analysis.

Identification of differentially expressed proteins in the spinal cord of neuropathic pain models with PKCgamma silence by proteomic analysis.

Brain Res. 2012 Jan 2;
Zou W, Zhan X, Li M, Song Z, Liu C, Peng F, Guo Q

In order to elucidate the mechanisms that PKCγ regulates neuropathic pain (NP), and detect proteins that are associated with the function of PKCγ in NP, we exploited a chronic constriction injury (CCI)-induced neuropathic pain rat (CCI-NP rat) model in which PKCγ knockdown in the spinal cord was successfully carried out with stable RNA interference (RNAi). The spinal cords (L4-L5) were surgically obtained from CCI-NP rats with and without PKCγ knockdown, for comparative proteomic analysis. The total proteins from the spinal cords (L4-L5) were extracted and were separated with two-dimensional gel electrophoresis (2DGE). 2D gel images were analyzed with PDQuest software. Nineteen differential gel-spots were identified with spot-volume increased and 17 spots with spot-volume decreased. Among them, eighteen differentially expressed proteins (DEPs) were identified with matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF MS) between CCI-NP rats with and without PKCγ knockout. Those DEPs are involved in transmission and modulation of noxious information; cellular homeostasis and metabolism; antioxidant proteins, heat shock proteins and chaperones; membrane receptor trafficking; and cytoskeleton. Three DEPs (SNAP-25, TERA and AR) were validated with Western blot analysis, and confirmed the DEP data. Further study showed that AR-selective inhibitor epalrestat totally turned over the upregulated expression of AR in CCI-NP rats. Those DEP data are extensively associated with the function of PKCγ that regulates NP, and would contribute to the clarification of the mechanisms of PKCγ in NP.

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Identification of differentially expressed proteins in the spinal cord of neuropathic pain models with PKCgamma silence by proteomic analysis.

Expression and Localization of Neural Cell Adhesion Molecule and PolySialic Acid during Chick Corneal Development.

Invest Ophthalmol Vis Sci. 2012 Jan 26;
Mao X, Schwend T, Conrad GW

Purpose:To assay for expression and localization of Neural Cell Adhesion Molecule (NCAM) and Polysialic acid (polySia) in the chick cornea during embryonic and postnatal development.Methods:Real time Q-PCR and Western blot were used to determine NCAM expression and polysiaylation in embryonic, hatchling and adult chick corneas. Immunofluorescence staining for NCAM and polySia was conducted on cryosections of embryonic and adult corneas, whole embryonic corneas and trigeminal neurons.Results:NCAM and ST8SiaII mRNA transcripts peaked by E9, remained steady between E10 and E14 and slowly decreased thereafter during embryonic development. Both gene transcripts showed more than 190-fold decline in the adult chick cornea compared to E9. In contrast, ST8SiaIV expression gradually decreased 26.5-fold from E6 to E19, increased thereafter, and rose to the early embryonic level in the adult cornea. Western blot analysis revealed NCAM was polysialylated and its expression developmentally changed. Other polysiaylated proteins aside from NCAM were also detected by Western blot analysis. Five NCAM isoforms including NCAM-120, NCAM-180 and three soluble NCAM isoforms with low molecular weights (87-96kDa) were present in chick corneas, with NCAM-120 being the predominate isoform. NCAM was localized to the epithelium, stroma and stromal extracellular matrix (ECM) of the embryonic cornea. In stroma, NCAM expression shifted from anterior to posterior stroma during embryonic development and eventually became undetectable in 20 wk adult cornea. Additionally, both NCAM and polySia were detected on embryonic corneal and pericorneal nerves.Conclusions:NCAM and polySia are expressed and developmentally regulated in chick corneas. Both membrane-associated and soluble NCAM isoforms are expressed chick corneas. The distributions of NCAM and polySia in cornea and on corneal nerves suggest their potential functions in corneal innervation.

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Expression and Localization of Neural Cell Adhesion Molecule and PolySialic Acid during Chick Corneal Development.

Quantitative Proteome Analysis of HCC Cell Lines with Different …

So it suits for not only whole-cell protein analysis, but also membrane protein identification and quantification.In order to make further exploration into the mechanism of Plasma membrane proteins are associated with multiple steps of metastasis process, such as breakaway from primary site, adhesion to extracellular matrix, infiltration into blood and lymphatic vessels, cell migriation, and lodgment to target organs. Because of the accessibility, plasma membrane

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Quantitative Proteome Analysis of HCC Cell Lines with Different …

Quantitative Proteome Analysis of HCC Cell Lines with Different …

So it suits for not only whole-cell protein analysis, but also membrane protein identification and quantification.In order to make further exploration into the mechanism of Plasma membrane proteins are associated with multiple steps of metastasis process, such as breakaway from primary site, adhesion to extracellular matrix, infiltration into blood and lymphatic vessels, cell migriation, and lodgment to target organs. Because of the accessibility, plasma membrane

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Quantitative Proteome Analysis of HCC Cell Lines with Different …

First report on the occurrence of Rickettsia slovaca and Rickettsia raoultii in Dermacentor silvarum in China.

Parasit Vectors . 2012 Jan 19; 5(1): 19 Tian ZC, Liu GY, Shen H, Xie JR, Luo J, Tian MY ABSTRACT: BACKGROUND: Rickettsioses are among both the longest known and most recently recognized infectious diseases. Although new spotted fever group rickettsiae have been isolated in many parts of the world including China, Little is known about the epidemiology of Rickettsia pathogens in ticks from Xinjiang Autonomous Region of China.

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First report on the occurrence of Rickettsia slovaca and Rickettsia raoultii in Dermacentor silvarum in China.

Phosphorylated p120-catenin expression has predictive value for oral cancer progression.

J Clin Pathol. 2012 Jan 18;
Ma LW, Zhou ZT, He QB, Jiang WW

AimsRecent studies have shown that phosphorylation of p120-catenin (p120) promotes progression and invasion of oral squamous cell carcinoma (OSCC) cells. The objective of the current study was to evaluate the usefulness of phosphorylated p120-catenin (pp120) as a biomarker for predicting clinical behaviour in the carcinogenesis of potentially malignant oral lesions.MethodsIn a retrospective follow-up study, the expression pattern of pp120 protein was determined using immunohistochemistry in samples from 68 patients with potentially malignant oral lesions, including patients with untransformed lesions (n=38) and patients with malignant transformed lesions (n=30). Analysis of corresponding post-malignant lesions (OSCCs) was also performed.ResultsThere was high expression of pp120 in 35 of 68 (51.5%) of general potentially malignant oral lesions and 23 of 30 (76.7%) of OSCCs compared with expression in normal oral mucosa. Kaplan-Meier analysis revealed that patients with potentially malignant oral lesions expressing high levels of membranous pp120 had a significantly higher incidence of OSCC than those expressing low expressing pp120 (p=0.002; log-rank test). Cox regression analysis revealed that this pp120 expression pattern was significantly associated with a 3.43-fold increase in the risk of malignant progression (p=0.007). In addition, there was a significant correlation between high levels of membranous expression of pp120 in pre-malignant lesions and cytoplasmic expression in post-malignant lesions (p=0.028).ConclusionsThe data indicated that a high level of membranous expression of pp120 in potentially malignant oral lesions is an early event during oral carcinogenesis, and that the mislocalisation of expression of pp120 from the cell membrane to the cytoplasm is associated with oral cancer progression. pp120 may serve as a useful marker for the identification of a high risk of potentially malignant oral lesions progressing to OSCC.

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Phosphorylated p120-catenin expression has predictive value for oral cancer progression.

Differential Proteomics Analysis of Cytoplasmic and Membrane …

expressions of cytoplasmic and membrane proteins.Methods:1. H8 cells and Caski cells were incubated in RPMI 1640, the cytoplasmic and membrane proteins of them that are in their logarhytmic growth phase at approximately 80% confluence(3×106) were extracted by ProteoExtract Subcel. Differential Proteomics Analysis of Cytoplasmic and Membrane Proteomics between Immortalized Cervical Cells and Cervical Cancer Cell. posted by: Cancer Research

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Differential Proteomics Analysis of Cytoplasmic and Membrane …

Membrane proteomic analysis comparing squamous cell lung cancer tissue and tumour-adjacent normal tissue.

Cancer Lett. 2012 Jan 14;
Li B, Chang J, Chu Y, Kang H, Yang J, Jiang J, Ma H

Lung cancer is the leading cause of cancer-related deaths worldwide. Squamous cell carcinoma is one of the predominant histological subtypes of lung cancer. Detecting lung cancer at an early stage is essential for successful therapy and increasing survival. There are still no satisfactory biomarkers for the early detection of lung cancer. In this study, tumour tissue paired with tumour-adjacent normal bronchial epithelial tissue was obtained from patients with squamous cell lung carcinoma without metastasis. The proteins extracted from the cell membrane were separated by two-dimensional polyacrylamide gel electrophoresis (2-DE) and were analysed with the Image Master two-dimensional platinum software. Twenty-five significantly different protein spots were selected and identified with matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOF MS). A total of 19 proteins were successfully identified. Twelve proteins were up-regulated, and seven proteins were down-regulated in the cancerous tissue compared with the tumour-adjacent normal tissue. One up-regulated protein and one down-regulated protein in squamous cell lung carcinoma were verified by Western blot analysis and RT-PCR; the results were consistent with the 2-DE analysis. In conclusion, membrane proteomics identified a number of candidate biomarker proteins that were differentially expressed between squamous cell lung cancer tissue and adjacent normal tissue. These biomarker candidates have the potential to elucidate the underlying pathogenesis of squamous cell lung cancer.

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Membrane proteomic analysis comparing squamous cell lung cancer tissue and tumour-adjacent normal tissue.

Membrane proteomic analysis comparing squamous cell lung cancer tissue and tumour-adjacent normal tissue.

Cancer Lett. 2012 Jan 14;
Li B, Chang J, Chu Y, Kang H, Yang J, Jiang J, Ma H

Lung cancer is the leading cause of cancer-related deaths worldwide. Squamous cell carcinoma is one of the predominant histological subtypes of lung cancer. Detecting lung cancer at an early stage is essential for successful therapy and increasing survival. There are still no satisfactory biomarkers for the early detection of lung cancer. In this study, tumour tissue paired with tumour-adjacent normal bronchial epithelial tissue was obtained from patients with squamous cell lung carcinoma without metastasis. The proteins extracted from the cell membrane were separated by two-dimensional polyacrylamide gel electrophoresis (2-DE) and were analysed with the Image Master two-dimensional platinum software. Twenty-five significantly different protein spots were selected and identified with matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOF MS). A total of 19 proteins were successfully identified. Twelve proteins were up-regulated, and seven proteins were down-regulated in the cancerous tissue compared with the tumour-adjacent normal tissue. One up-regulated protein and one down-regulated protein in squamous cell lung carcinoma were verified by Western blot analysis and RT-PCR; the results were consistent with the 2-DE analysis. In conclusion, membrane proteomics identified a number of candidate biomarker proteins that were differentially expressed between squamous cell lung cancer tissue and adjacent normal tissue. These biomarker candidates have the potential to elucidate the underlying pathogenesis of squamous cell lung cancer.

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Membrane proteomic analysis comparing squamous cell lung cancer tissue and tumour-adjacent normal tissue.

Impairment on sperm quality and fertility of adult rats after antiandrogen exposure during prepuberty.

Reprod Toxicol. 2011 Dec 31;
Perobelli JE, Alves TR, de Toledo FC, Fernandez CD, Anselmo-Franci JA, Klinefelter GR, Kempinas WD

This study evaluated the effects of antiandrogen exposure during the prepubertal period on reproductive development and reproductive competence in adults. Male rats were divided into two groups: flutamide, receiving 25mg/kg/day of flutamide by oral gavage and control, receiving vehicle daily. Dosing continued from PND 21 to 44, and animals were killed on PND 50 or PND 75-80. The epididymis, prostate, vas deferens and seminal vesicle weights were lower in Flutamide group on PND 50, while on PND 80 only seminal vesicle weight was reduced. Fertility assessed by IUI revealed a decrease in the fertility potential in the flutamide-treated adults. Flutamide accelerated sperm transit time through the epididymis, impairing sperm motility and storage. A quantitative analysis of the cauda sperm membrane proteome revealed a few significant changes in protein expression. Thus, exposure to flutamide during the prepubertal period compromises the function of the epididymis along with epididymal sperm quality at adulthood.

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Impairment on sperm quality and fertility of adult rats after antiandrogen exposure during prepuberty.