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David G Camp - One of the best experts on this subject based on the ideXlab platform.

  • characterization of the mouse Brain proteome using global proteomic analysis complemented with cysteinyl Peptide enrichment
    Journal of Proteome Research, 2006
    Co-Authors: Haixing Wang, Weijun Qian, Mark H Chin, Vladislav A Petyuk, Richard C Barry, Marina A Gritsenko, Heather M Mottaz, Ronald J Moore, David G Camp, Arshad H Khan
    Abstract:

    Given the growing interest in applying genomic and proteomic approaches for studying the mammalian Brain using mouse models, we hereby present a global proteomic approach for analyzing Brain tissue and for the first time a comprehensive characterization of the whole mouse Brain proteome. Preparation of the whole Brain sample incorporated a highly efficient cysteinyl-Peptide enrichment (CPE) technique to complement a global enzymatic digestion method. Both the global and the cysteinyl-enriched Peptide samples were analyzed by SCX fractionation coupled with reversed phase LC-MS/MS analysis. A total of 48,328 different Peptides were confidently identified (>98% confidence level), covering 7792 non-redundant proteins (∼34% of the predicted mouse proteome). 1564 and 1859 proteins were identified exclusively from the cysteinyl-Peptide and the global Peptide samples, respectively, corresponding to 25% and 31% improvements in proteome coverage compared to analysis of only the global Peptide or cysteinyl-Peptide samples. The identified proteins provide a broad representation of the mouse proteome with little bias evident due to protein pI, molecular weight, and/or cellular localization. Approximately 26% of the identified proteins with gene ontology (GO) annotations were membrane proteins, with 1447 proteins predicted to have transmembrane domains, and many of the membrane proteins were found to be involved in transport and cell signaling. The MS/MS spectrum count information for the identified proteins was used to provide a measure of relative protein abundances. The mouse Brain Peptide/protein database generated from this study represents the most comprehensive proteome coverage for the mammalian Brain to date, and the basis for future quantitative Brain proteomic studies using mouse models. The proteomic approach presented here may have broad applications for rapid proteomic analyses of various mouse models of human Brain diseases.

  • characterization of the mouse Brain proteome using global proteomic analysis complemented with cysteinyl Peptide enrichment
    Journal of Proteome Research, 2006
    Co-Authors: Haixing Wang, Weijun Qian, Mark H Chin, Vladislav A Petyuk, Richard C Barry, Tao Liu, Marina A Gritsenko, Heather M Mottaz, Ronald J Moore, David G Camp
    Abstract:

    We report a global proteomic approach for analyzing Brain tissue and for the first time a comprehensive characterization of the whole mouse Brain proteome. Preparation of the whole Brain sample incorporated a highly efficient cysteinyl-Peptide enrichment (CPE) technique to complement a global enzymatic digestion method. Both the global and the cysteinyl-enriched Peptide samples were analyzed by SCX fractionation coupled with reversed phase LC-MS/MS analysis. A total of 48,328 different Peptides were confidently identified (>98% confidence level), covering 7792 nonredundant proteins ( approximately 34% of the predicted mouse proteome). A total of 1564 and 1859 proteins were identified exclusively from the cysteinyl-Peptide and the global Peptide samples, respectively, corresponding to 25% and 31% improvements in proteome coverage compared to analysis of only the global Peptide or cysteinyl-Peptide samples. The identified proteins provide a broad representation of the mouse proteome with little bias evident due to protein pI, molecular weight, and/or cellular localization. Approximately 26% of the identified proteins with gene ontology (GO) annotations were membrane proteins, with 1447 proteins predicted to have transmembrane domains, and many of the membrane proteins were found to be involved in transport and cell signaling. The MS/MS spectrum count information for the identified proteins was used to provide a measure of relative protein abundances. The mouse Brain Peptide/protein database generated from this study represents the most comprehensive proteome coverage for the mammalian Brain to date, and the basis for future quantitative Brain proteomic studies using mouse models. The proteomic approach presented here may have broad applications for rapid proteomic analyses of various mouse models of human Brain diseases.

Haixing Wang - One of the best experts on this subject based on the ideXlab platform.

  • characterization of the mouse Brain proteome using global proteomic analysis complemented with cysteinyl Peptide enrichment
    Journal of Proteome Research, 2006
    Co-Authors: Haixing Wang, Weijun Qian, Mark H Chin, Vladislav A Petyuk, Richard C Barry, Marina A Gritsenko, Heather M Mottaz, Ronald J Moore, David G Camp, Arshad H Khan
    Abstract:

    Given the growing interest in applying genomic and proteomic approaches for studying the mammalian Brain using mouse models, we hereby present a global proteomic approach for analyzing Brain tissue and for the first time a comprehensive characterization of the whole mouse Brain proteome. Preparation of the whole Brain sample incorporated a highly efficient cysteinyl-Peptide enrichment (CPE) technique to complement a global enzymatic digestion method. Both the global and the cysteinyl-enriched Peptide samples were analyzed by SCX fractionation coupled with reversed phase LC-MS/MS analysis. A total of 48,328 different Peptides were confidently identified (>98% confidence level), covering 7792 non-redundant proteins (∼34% of the predicted mouse proteome). 1564 and 1859 proteins were identified exclusively from the cysteinyl-Peptide and the global Peptide samples, respectively, corresponding to 25% and 31% improvements in proteome coverage compared to analysis of only the global Peptide or cysteinyl-Peptide samples. The identified proteins provide a broad representation of the mouse proteome with little bias evident due to protein pI, molecular weight, and/or cellular localization. Approximately 26% of the identified proteins with gene ontology (GO) annotations were membrane proteins, with 1447 proteins predicted to have transmembrane domains, and many of the membrane proteins were found to be involved in transport and cell signaling. The MS/MS spectrum count information for the identified proteins was used to provide a measure of relative protein abundances. The mouse Brain Peptide/protein database generated from this study represents the most comprehensive proteome coverage for the mammalian Brain to date, and the basis for future quantitative Brain proteomic studies using mouse models. The proteomic approach presented here may have broad applications for rapid proteomic analyses of various mouse models of human Brain diseases.

  • characterization of the mouse Brain proteome using global proteomic analysis complemented with cysteinyl Peptide enrichment
    Journal of Proteome Research, 2006
    Co-Authors: Haixing Wang, Weijun Qian, Mark H Chin, Vladislav A Petyuk, Richard C Barry, Tao Liu, Marina A Gritsenko, Heather M Mottaz, Ronald J Moore, David G Camp
    Abstract:

    We report a global proteomic approach for analyzing Brain tissue and for the first time a comprehensive characterization of the whole mouse Brain proteome. Preparation of the whole Brain sample incorporated a highly efficient cysteinyl-Peptide enrichment (CPE) technique to complement a global enzymatic digestion method. Both the global and the cysteinyl-enriched Peptide samples were analyzed by SCX fractionation coupled with reversed phase LC-MS/MS analysis. A total of 48,328 different Peptides were confidently identified (>98% confidence level), covering 7792 nonredundant proteins ( approximately 34% of the predicted mouse proteome). A total of 1564 and 1859 proteins were identified exclusively from the cysteinyl-Peptide and the global Peptide samples, respectively, corresponding to 25% and 31% improvements in proteome coverage compared to analysis of only the global Peptide or cysteinyl-Peptide samples. The identified proteins provide a broad representation of the mouse proteome with little bias evident due to protein pI, molecular weight, and/or cellular localization. Approximately 26% of the identified proteins with gene ontology (GO) annotations were membrane proteins, with 1447 proteins predicted to have transmembrane domains, and many of the membrane proteins were found to be involved in transport and cell signaling. The MS/MS spectrum count information for the identified proteins was used to provide a measure of relative protein abundances. The mouse Brain Peptide/protein database generated from this study represents the most comprehensive proteome coverage for the mammalian Brain to date, and the basis for future quantitative Brain proteomic studies using mouse models. The proteomic approach presented here may have broad applications for rapid proteomic analyses of various mouse models of human Brain diseases.

A Suzuki - One of the best experts on this subject based on the ideXlab platform.

  • the Brain secretory Peptides that control moulting and metamorphosis of the silkmoth bombyx mori
    The International Journal of Developmental Biology, 1994
    Co-Authors: H Ishizaki, A Suzuki
    Abstract:

    Progress made toward the elucidation of molecular features of the prothoracicotropic hormone (PTTH) of the silkmoth Bombyx mori is reviewed. PTTH stimulates the prothoracic glands to synthesize and release ecdysone, and is therefore a key hormone for the regulation of insect moulting and metamorphosis. Bombyx PTTH is a 30 kDa homodimeric glycoprotein, whose carbohydrate moiety is not essential for the biological function. The Bombyx genome contains a single copy of the PTTH gene. PTTH is produced by four dorsolateral neurosecretory cells of Brain. Another Bombyx Brain Peptide exerting prothoracicotropic activity to a heterologous moth Samia cynthia ricini but no activity to Bombyx has been identified and termed bombyxin. Bombyxin is a 5 kDa heterodimeric Peptide that shows a high similarity to insulin in the amino acid sequence. The bombyxin gene structure also shows a high similarity with the insulin gene structure. The Bombyx genome contains more than 30 copies of the bombyxin gene. Bombyxin is synthesized by eight dorsomedial neurosecretory cells of Brain.

  • chapter 1 Brain secretory Peptides of the silkmoth bombyx mori prothoracicotropic hormone and bombyxin
    Progress in Brain Research, 1992
    Co-Authors: H Ishizaki, A Suzuki
    Abstract:

    Publisher Summary The prothoracicotropic hormone (PTTH) stimulates a paired thoracic endocrine organ to synthesize and release ecdysone, a steroid indispensable for insect development. Ecdysone plays a central role in the endocrine network controlling insect development; however, its chemical structure has long been undetermined. This chapter describes the progress made toward the determination of the primary structure, gene structure, and cellular localization of the PTTH of the silkmoth Bombyx mori , and another Bombyx Brain Peptide functionally related to PTTH, bombyxin. By using bombyxin antibody, the immunoreactive materials have been detected in the central nervous system of the oligochaete Eisenia foetida , Locusta migratoria , the wax moth Galleria mellonella , and Drosophila. However, studies on physiological and developmental regulations, which are under the control of these Peptides, and the mechanism of evolution of the insulin superfamily Peptides, which are now thought to occur probably throughout the animal kingdom, may open up new avenues for insulin research.

Arshad H Khan - One of the best experts on this subject based on the ideXlab platform.

  • characterization of the mouse Brain proteome using global proteomic analysis complemented with cysteinyl Peptide enrichment
    Journal of Proteome Research, 2006
    Co-Authors: Haixing Wang, Weijun Qian, Mark H Chin, Vladislav A Petyuk, Richard C Barry, Marina A Gritsenko, Heather M Mottaz, Ronald J Moore, David G Camp, Arshad H Khan
    Abstract:

    Given the growing interest in applying genomic and proteomic approaches for studying the mammalian Brain using mouse models, we hereby present a global proteomic approach for analyzing Brain tissue and for the first time a comprehensive characterization of the whole mouse Brain proteome. Preparation of the whole Brain sample incorporated a highly efficient cysteinyl-Peptide enrichment (CPE) technique to complement a global enzymatic digestion method. Both the global and the cysteinyl-enriched Peptide samples were analyzed by SCX fractionation coupled with reversed phase LC-MS/MS analysis. A total of 48,328 different Peptides were confidently identified (>98% confidence level), covering 7792 non-redundant proteins (∼34% of the predicted mouse proteome). 1564 and 1859 proteins were identified exclusively from the cysteinyl-Peptide and the global Peptide samples, respectively, corresponding to 25% and 31% improvements in proteome coverage compared to analysis of only the global Peptide or cysteinyl-Peptide samples. The identified proteins provide a broad representation of the mouse proteome with little bias evident due to protein pI, molecular weight, and/or cellular localization. Approximately 26% of the identified proteins with gene ontology (GO) annotations were membrane proteins, with 1447 proteins predicted to have transmembrane domains, and many of the membrane proteins were found to be involved in transport and cell signaling. The MS/MS spectrum count information for the identified proteins was used to provide a measure of relative protein abundances. The mouse Brain Peptide/protein database generated from this study represents the most comprehensive proteome coverage for the mammalian Brain to date, and the basis for future quantitative Brain proteomic studies using mouse models. The proteomic approach presented here may have broad applications for rapid proteomic analyses of various mouse models of human Brain diseases.

Mark H Chin - One of the best experts on this subject based on the ideXlab platform.

  • characterization of the mouse Brain proteome using global proteomic analysis complemented with cysteinyl Peptide enrichment
    Journal of Proteome Research, 2006
    Co-Authors: Haixing Wang, Weijun Qian, Mark H Chin, Vladislav A Petyuk, Richard C Barry, Marina A Gritsenko, Heather M Mottaz, Ronald J Moore, David G Camp, Arshad H Khan
    Abstract:

    Given the growing interest in applying genomic and proteomic approaches for studying the mammalian Brain using mouse models, we hereby present a global proteomic approach for analyzing Brain tissue and for the first time a comprehensive characterization of the whole mouse Brain proteome. Preparation of the whole Brain sample incorporated a highly efficient cysteinyl-Peptide enrichment (CPE) technique to complement a global enzymatic digestion method. Both the global and the cysteinyl-enriched Peptide samples were analyzed by SCX fractionation coupled with reversed phase LC-MS/MS analysis. A total of 48,328 different Peptides were confidently identified (>98% confidence level), covering 7792 non-redundant proteins (∼34% of the predicted mouse proteome). 1564 and 1859 proteins were identified exclusively from the cysteinyl-Peptide and the global Peptide samples, respectively, corresponding to 25% and 31% improvements in proteome coverage compared to analysis of only the global Peptide or cysteinyl-Peptide samples. The identified proteins provide a broad representation of the mouse proteome with little bias evident due to protein pI, molecular weight, and/or cellular localization. Approximately 26% of the identified proteins with gene ontology (GO) annotations were membrane proteins, with 1447 proteins predicted to have transmembrane domains, and many of the membrane proteins were found to be involved in transport and cell signaling. The MS/MS spectrum count information for the identified proteins was used to provide a measure of relative protein abundances. The mouse Brain Peptide/protein database generated from this study represents the most comprehensive proteome coverage for the mammalian Brain to date, and the basis for future quantitative Brain proteomic studies using mouse models. The proteomic approach presented here may have broad applications for rapid proteomic analyses of various mouse models of human Brain diseases.

  • characterization of the mouse Brain proteome using global proteomic analysis complemented with cysteinyl Peptide enrichment
    Journal of Proteome Research, 2006
    Co-Authors: Haixing Wang, Weijun Qian, Mark H Chin, Vladislav A Petyuk, Richard C Barry, Tao Liu, Marina A Gritsenko, Heather M Mottaz, Ronald J Moore, David G Camp
    Abstract:

    We report a global proteomic approach for analyzing Brain tissue and for the first time a comprehensive characterization of the whole mouse Brain proteome. Preparation of the whole Brain sample incorporated a highly efficient cysteinyl-Peptide enrichment (CPE) technique to complement a global enzymatic digestion method. Both the global and the cysteinyl-enriched Peptide samples were analyzed by SCX fractionation coupled with reversed phase LC-MS/MS analysis. A total of 48,328 different Peptides were confidently identified (>98% confidence level), covering 7792 nonredundant proteins ( approximately 34% of the predicted mouse proteome). A total of 1564 and 1859 proteins were identified exclusively from the cysteinyl-Peptide and the global Peptide samples, respectively, corresponding to 25% and 31% improvements in proteome coverage compared to analysis of only the global Peptide or cysteinyl-Peptide samples. The identified proteins provide a broad representation of the mouse proteome with little bias evident due to protein pI, molecular weight, and/or cellular localization. Approximately 26% of the identified proteins with gene ontology (GO) annotations were membrane proteins, with 1447 proteins predicted to have transmembrane domains, and many of the membrane proteins were found to be involved in transport and cell signaling. The MS/MS spectrum count information for the identified proteins was used to provide a measure of relative protein abundances. The mouse Brain Peptide/protein database generated from this study represents the most comprehensive proteome coverage for the mammalian Brain to date, and the basis for future quantitative Brain proteomic studies using mouse models. The proteomic approach presented here may have broad applications for rapid proteomic analyses of various mouse models of human Brain diseases.