The Experts below are selected from a list of 1654422 Experts worldwide ranked by ideXlab platform
Kazuhisa Nakayama - One of the best experts on this subject based on the ideXlab platform.
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arg x lys arg arg motif as a signal for Precursor cleavage catalyzed by furin within the constitutive secretory pathway
Journal of Biological Chemistry, 1991Co-Authors: Masahiro Hosaka, Masami Nagahama, Kazuo Murakami, Tsuyoshi Watanabe, Kiyotaka Hatsuzawa, J Ikemizu, Kazuhisa NakayamaAbstract:Abstract Many peptide hormones are produced from larger Precursors by endoproteolysis at pairs of basic amino acids (e.g. Lys-Arg and Arg-Arg) within the regulated secretory pathway in endocrine cells. However, many other secretory and membrane proteins appear to be produced from Precursors through cleavage at multiple, rather than paired, basic residues within the constitutive secretory pathway in non-endocrine cells. By surveying various Precursors processed constitutively, we noticed that most of them have the consensus sequence, Arg-X-Lys/Arg-Arg (RXK/RR), at the cleavage site. When expressed in endocrine and non-endocrine cells, a Precursor with the RXKR sequence was cleaved in both types of cells, whereas that with the Lys-Arg pair was cleaved only in the endocrine cells. When the RXKR Precursor was coexpressed with furin and PC3, both of which are mammalian homologues of the yeast Precursor-processing endoprotease Kex2, in non-endocrine cells, enhancement of the Precursor cleavage by furin but not by PC3 was observed. By contrast, when the Lys-Arg Precursor was coexpressed with the two mammalian proteases in endocrine cells with no endogenous processing activity at dibasic sites, it was cleaved only by PC3. These results indicate that the basic pair and the RXK/RR sequence are the signals for Precursor cleavages catalyzed by PC3 within the regulated secretory pathway and by furin within the constitutive pathway, respectively.
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Arg-X-Lys/Arg-Arg motif as a signal for Precursor cleavage catalyzed by furin within the constitutive secretory pathway.
The Journal of biological chemistry, 1991Co-Authors: Masahiro Hosaka, Masami Nagahama, Kazuo Murakami, Tsuyoshi Watanabe, Kiyotaka Hatsuzawa, J Ikemizu, Won-sin Kim, Kazuhisa NakayamaAbstract:Many peptide hormones are produced from larger Precursors by endoproteolysis at pairs of basic amino acids (e.g. Lys-Arg and Arg-Arg) within the regulated secretory pathway in endocrine cells. However, many other secretory and membrane proteins appear to be produced from Precursors through cleavage at multiple, rather than paired, basic residues within the constitutive secretory pathway in non-endocrine cells. By surveying various Precursors processed constitutively, we noticed that most of them have the consensus sequence, Arg-X-Lys/Arg-Arg (RXK/RR), at the cleavage site. When expressed in endocrine and non-endocrine cells, a Precursor with the RXKR sequence was cleaved in both types of cells, whereas that with the Lys-Arg pair was cleaved only in the endocrine cells. When the RXKR Precursor was coexpressed with furin and PC3, both of which are mammalian homologues of the yeast Precursor-processing endoprotease Kex2, in non-endocrine cells, enhancement of the Precursor cleavage by furin but not by PC3 was observed. By contrast, when the Lys-Arg Precursor was coexpressed with the two mammalian proteases in endocrine cells with no endogenous processing activity at dibasic sites, it was cleaved only by PC3. These results indicate that the basic pair and the RXK/RR sequence are the signals for Precursor cleavages catalyzed by PC3 within the regulated secretory pathway and by furin within the constitutive pathway, respectively.
Masahiro Hosaka - One of the best experts on this subject based on the ideXlab platform.
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arg x lys arg arg motif as a signal for Precursor cleavage catalyzed by furin within the constitutive secretory pathway
Journal of Biological Chemistry, 1991Co-Authors: Masahiro Hosaka, Masami Nagahama, Kazuo Murakami, Tsuyoshi Watanabe, Kiyotaka Hatsuzawa, J Ikemizu, Kazuhisa NakayamaAbstract:Abstract Many peptide hormones are produced from larger Precursors by endoproteolysis at pairs of basic amino acids (e.g. Lys-Arg and Arg-Arg) within the regulated secretory pathway in endocrine cells. However, many other secretory and membrane proteins appear to be produced from Precursors through cleavage at multiple, rather than paired, basic residues within the constitutive secretory pathway in non-endocrine cells. By surveying various Precursors processed constitutively, we noticed that most of them have the consensus sequence, Arg-X-Lys/Arg-Arg (RXK/RR), at the cleavage site. When expressed in endocrine and non-endocrine cells, a Precursor with the RXKR sequence was cleaved in both types of cells, whereas that with the Lys-Arg pair was cleaved only in the endocrine cells. When the RXKR Precursor was coexpressed with furin and PC3, both of which are mammalian homologues of the yeast Precursor-processing endoprotease Kex2, in non-endocrine cells, enhancement of the Precursor cleavage by furin but not by PC3 was observed. By contrast, when the Lys-Arg Precursor was coexpressed with the two mammalian proteases in endocrine cells with no endogenous processing activity at dibasic sites, it was cleaved only by PC3. These results indicate that the basic pair and the RXK/RR sequence are the signals for Precursor cleavages catalyzed by PC3 within the regulated secretory pathway and by furin within the constitutive pathway, respectively.
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Arg-X-Lys/Arg-Arg motif as a signal for Precursor cleavage catalyzed by furin within the constitutive secretory pathway.
The Journal of biological chemistry, 1991Co-Authors: Masahiro Hosaka, Masami Nagahama, Kazuo Murakami, Tsuyoshi Watanabe, Kiyotaka Hatsuzawa, J Ikemizu, Won-sin Kim, Kazuhisa NakayamaAbstract:Many peptide hormones are produced from larger Precursors by endoproteolysis at pairs of basic amino acids (e.g. Lys-Arg and Arg-Arg) within the regulated secretory pathway in endocrine cells. However, many other secretory and membrane proteins appear to be produced from Precursors through cleavage at multiple, rather than paired, basic residues within the constitutive secretory pathway in non-endocrine cells. By surveying various Precursors processed constitutively, we noticed that most of them have the consensus sequence, Arg-X-Lys/Arg-Arg (RXK/RR), at the cleavage site. When expressed in endocrine and non-endocrine cells, a Precursor with the RXKR sequence was cleaved in both types of cells, whereas that with the Lys-Arg pair was cleaved only in the endocrine cells. When the RXKR Precursor was coexpressed with furin and PC3, both of which are mammalian homologues of the yeast Precursor-processing endoprotease Kex2, in non-endocrine cells, enhancement of the Precursor cleavage by furin but not by PC3 was observed. By contrast, when the Lys-Arg Precursor was coexpressed with the two mammalian proteases in endocrine cells with no endogenous processing activity at dibasic sites, it was cleaved only by PC3. These results indicate that the basic pair and the RXK/RR sequence are the signals for Precursor cleavages catalyzed by PC3 within the regulated secretory pathway and by furin within the constitutive pathway, respectively.
J Ikemizu - One of the best experts on this subject based on the ideXlab platform.
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arg x lys arg arg motif as a signal for Precursor cleavage catalyzed by furin within the constitutive secretory pathway
Journal of Biological Chemistry, 1991Co-Authors: Masahiro Hosaka, Masami Nagahama, Kazuo Murakami, Tsuyoshi Watanabe, Kiyotaka Hatsuzawa, J Ikemizu, Kazuhisa NakayamaAbstract:Abstract Many peptide hormones are produced from larger Precursors by endoproteolysis at pairs of basic amino acids (e.g. Lys-Arg and Arg-Arg) within the regulated secretory pathway in endocrine cells. However, many other secretory and membrane proteins appear to be produced from Precursors through cleavage at multiple, rather than paired, basic residues within the constitutive secretory pathway in non-endocrine cells. By surveying various Precursors processed constitutively, we noticed that most of them have the consensus sequence, Arg-X-Lys/Arg-Arg (RXK/RR), at the cleavage site. When expressed in endocrine and non-endocrine cells, a Precursor with the RXKR sequence was cleaved in both types of cells, whereas that with the Lys-Arg pair was cleaved only in the endocrine cells. When the RXKR Precursor was coexpressed with furin and PC3, both of which are mammalian homologues of the yeast Precursor-processing endoprotease Kex2, in non-endocrine cells, enhancement of the Precursor cleavage by furin but not by PC3 was observed. By contrast, when the Lys-Arg Precursor was coexpressed with the two mammalian proteases in endocrine cells with no endogenous processing activity at dibasic sites, it was cleaved only by PC3. These results indicate that the basic pair and the RXK/RR sequence are the signals for Precursor cleavages catalyzed by PC3 within the regulated secretory pathway and by furin within the constitutive pathway, respectively.
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Arg-X-Lys/Arg-Arg motif as a signal for Precursor cleavage catalyzed by furin within the constitutive secretory pathway.
The Journal of biological chemistry, 1991Co-Authors: Masahiro Hosaka, Masami Nagahama, Kazuo Murakami, Tsuyoshi Watanabe, Kiyotaka Hatsuzawa, J Ikemizu, Won-sin Kim, Kazuhisa NakayamaAbstract:Many peptide hormones are produced from larger Precursors by endoproteolysis at pairs of basic amino acids (e.g. Lys-Arg and Arg-Arg) within the regulated secretory pathway in endocrine cells. However, many other secretory and membrane proteins appear to be produced from Precursors through cleavage at multiple, rather than paired, basic residues within the constitutive secretory pathway in non-endocrine cells. By surveying various Precursors processed constitutively, we noticed that most of them have the consensus sequence, Arg-X-Lys/Arg-Arg (RXK/RR), at the cleavage site. When expressed in endocrine and non-endocrine cells, a Precursor with the RXKR sequence was cleaved in both types of cells, whereas that with the Lys-Arg pair was cleaved only in the endocrine cells. When the RXKR Precursor was coexpressed with furin and PC3, both of which are mammalian homologues of the yeast Precursor-processing endoprotease Kex2, in non-endocrine cells, enhancement of the Precursor cleavage by furin but not by PC3 was observed. By contrast, when the Lys-Arg Precursor was coexpressed with the two mammalian proteases in endocrine cells with no endogenous processing activity at dibasic sites, it was cleaved only by PC3. These results indicate that the basic pair and the RXK/RR sequence are the signals for Precursor cleavages catalyzed by PC3 within the regulated secretory pathway and by furin within the constitutive pathway, respectively.
Kiyotaka Hatsuzawa - One of the best experts on this subject based on the ideXlab platform.
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arg x lys arg arg motif as a signal for Precursor cleavage catalyzed by furin within the constitutive secretory pathway
Journal of Biological Chemistry, 1991Co-Authors: Masahiro Hosaka, Masami Nagahama, Kazuo Murakami, Tsuyoshi Watanabe, Kiyotaka Hatsuzawa, J Ikemizu, Kazuhisa NakayamaAbstract:Abstract Many peptide hormones are produced from larger Precursors by endoproteolysis at pairs of basic amino acids (e.g. Lys-Arg and Arg-Arg) within the regulated secretory pathway in endocrine cells. However, many other secretory and membrane proteins appear to be produced from Precursors through cleavage at multiple, rather than paired, basic residues within the constitutive secretory pathway in non-endocrine cells. By surveying various Precursors processed constitutively, we noticed that most of them have the consensus sequence, Arg-X-Lys/Arg-Arg (RXK/RR), at the cleavage site. When expressed in endocrine and non-endocrine cells, a Precursor with the RXKR sequence was cleaved in both types of cells, whereas that with the Lys-Arg pair was cleaved only in the endocrine cells. When the RXKR Precursor was coexpressed with furin and PC3, both of which are mammalian homologues of the yeast Precursor-processing endoprotease Kex2, in non-endocrine cells, enhancement of the Precursor cleavage by furin but not by PC3 was observed. By contrast, when the Lys-Arg Precursor was coexpressed with the two mammalian proteases in endocrine cells with no endogenous processing activity at dibasic sites, it was cleaved only by PC3. These results indicate that the basic pair and the RXK/RR sequence are the signals for Precursor cleavages catalyzed by PC3 within the regulated secretory pathway and by furin within the constitutive pathway, respectively.
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Arg-X-Lys/Arg-Arg motif as a signal for Precursor cleavage catalyzed by furin within the constitutive secretory pathway.
The Journal of biological chemistry, 1991Co-Authors: Masahiro Hosaka, Masami Nagahama, Kazuo Murakami, Tsuyoshi Watanabe, Kiyotaka Hatsuzawa, J Ikemizu, Won-sin Kim, Kazuhisa NakayamaAbstract:Many peptide hormones are produced from larger Precursors by endoproteolysis at pairs of basic amino acids (e.g. Lys-Arg and Arg-Arg) within the regulated secretory pathway in endocrine cells. However, many other secretory and membrane proteins appear to be produced from Precursors through cleavage at multiple, rather than paired, basic residues within the constitutive secretory pathway in non-endocrine cells. By surveying various Precursors processed constitutively, we noticed that most of them have the consensus sequence, Arg-X-Lys/Arg-Arg (RXK/RR), at the cleavage site. When expressed in endocrine and non-endocrine cells, a Precursor with the RXKR sequence was cleaved in both types of cells, whereas that with the Lys-Arg pair was cleaved only in the endocrine cells. When the RXKR Precursor was coexpressed with furin and PC3, both of which are mammalian homologues of the yeast Precursor-processing endoprotease Kex2, in non-endocrine cells, enhancement of the Precursor cleavage by furin but not by PC3 was observed. By contrast, when the Lys-Arg Precursor was coexpressed with the two mammalian proteases in endocrine cells with no endogenous processing activity at dibasic sites, it was cleaved only by PC3. These results indicate that the basic pair and the RXK/RR sequence are the signals for Precursor cleavages catalyzed by PC3 within the regulated secretory pathway and by furin within the constitutive pathway, respectively.
Kazuo Murakami - One of the best experts on this subject based on the ideXlab platform.
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arg x lys arg arg motif as a signal for Precursor cleavage catalyzed by furin within the constitutive secretory pathway
Journal of Biological Chemistry, 1991Co-Authors: Masahiro Hosaka, Masami Nagahama, Kazuo Murakami, Tsuyoshi Watanabe, Kiyotaka Hatsuzawa, J Ikemizu, Kazuhisa NakayamaAbstract:Abstract Many peptide hormones are produced from larger Precursors by endoproteolysis at pairs of basic amino acids (e.g. Lys-Arg and Arg-Arg) within the regulated secretory pathway in endocrine cells. However, many other secretory and membrane proteins appear to be produced from Precursors through cleavage at multiple, rather than paired, basic residues within the constitutive secretory pathway in non-endocrine cells. By surveying various Precursors processed constitutively, we noticed that most of them have the consensus sequence, Arg-X-Lys/Arg-Arg (RXK/RR), at the cleavage site. When expressed in endocrine and non-endocrine cells, a Precursor with the RXKR sequence was cleaved in both types of cells, whereas that with the Lys-Arg pair was cleaved only in the endocrine cells. When the RXKR Precursor was coexpressed with furin and PC3, both of which are mammalian homologues of the yeast Precursor-processing endoprotease Kex2, in non-endocrine cells, enhancement of the Precursor cleavage by furin but not by PC3 was observed. By contrast, when the Lys-Arg Precursor was coexpressed with the two mammalian proteases in endocrine cells with no endogenous processing activity at dibasic sites, it was cleaved only by PC3. These results indicate that the basic pair and the RXK/RR sequence are the signals for Precursor cleavages catalyzed by PC3 within the regulated secretory pathway and by furin within the constitutive pathway, respectively.
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Arg-X-Lys/Arg-Arg motif as a signal for Precursor cleavage catalyzed by furin within the constitutive secretory pathway.
The Journal of biological chemistry, 1991Co-Authors: Masahiro Hosaka, Masami Nagahama, Kazuo Murakami, Tsuyoshi Watanabe, Kiyotaka Hatsuzawa, J Ikemizu, Won-sin Kim, Kazuhisa NakayamaAbstract:Many peptide hormones are produced from larger Precursors by endoproteolysis at pairs of basic amino acids (e.g. Lys-Arg and Arg-Arg) within the regulated secretory pathway in endocrine cells. However, many other secretory and membrane proteins appear to be produced from Precursors through cleavage at multiple, rather than paired, basic residues within the constitutive secretory pathway in non-endocrine cells. By surveying various Precursors processed constitutively, we noticed that most of them have the consensus sequence, Arg-X-Lys/Arg-Arg (RXK/RR), at the cleavage site. When expressed in endocrine and non-endocrine cells, a Precursor with the RXKR sequence was cleaved in both types of cells, whereas that with the Lys-Arg pair was cleaved only in the endocrine cells. When the RXKR Precursor was coexpressed with furin and PC3, both of which are mammalian homologues of the yeast Precursor-processing endoprotease Kex2, in non-endocrine cells, enhancement of the Precursor cleavage by furin but not by PC3 was observed. By contrast, when the Lys-Arg Precursor was coexpressed with the two mammalian proteases in endocrine cells with no endogenous processing activity at dibasic sites, it was cleaved only by PC3. These results indicate that the basic pair and the RXK/RR sequence are the signals for Precursor cleavages catalyzed by PC3 within the regulated secretory pathway and by furin within the constitutive pathway, respectively.
