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Carboxypeptidase E, Identified As a Direct Interactor of Growth Hormone, Is Important for Efficient Secretion of the Hormone

We have identified 88 interactor candidates for human growth hormone (GH) by the yeast two-hybrid assay. Among those, we focused our efforts on carboxypeptidase E (CPE), which has been thought to play a key role in sorting prohormones, such as pro-opiomelanocortin (POMC), to regulated secretory vesi...

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Autores principales: Mizutani, Akiko, Inoko, Hidetoshi, Tanaka, Masafumi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Molecular and Cellular Biology 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5104884/
https://www.ncbi.nlm.nih.gov/pubmed/27788574
http://dx.doi.org/10.14348/molcells.2016.0183
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author Mizutani, Akiko
Inoko, Hidetoshi
Tanaka, Masafumi
author_facet Mizutani, Akiko
Inoko, Hidetoshi
Tanaka, Masafumi
author_sort Mizutani, Akiko
collection PubMed
description We have identified 88 interactor candidates for human growth hormone (GH) by the yeast two-hybrid assay. Among those, we focused our efforts on carboxypeptidase E (CPE), which has been thought to play a key role in sorting prohormones, such as pro-opiomelanocortin (POMC), to regulated secretory vesicles. We found that CPE co-localizes with and interacts with GH in AtT20 pituitary cells. Downregulation of CPE led to decreased levels of GH secretion, consistent with involvement of CPE in GH sorting/secretion. Our binding assay in vitro with bacterially expressed proteins suggested that GH directly interacts with CPE but in a manner different from POMC.
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spelling pubmed-51048842016-12-01 Carboxypeptidase E, Identified As a Direct Interactor of Growth Hormone, Is Important for Efficient Secretion of the Hormone Mizutani, Akiko Inoko, Hidetoshi Tanaka, Masafumi Mol Cells Article We have identified 88 interactor candidates for human growth hormone (GH) by the yeast two-hybrid assay. Among those, we focused our efforts on carboxypeptidase E (CPE), which has been thought to play a key role in sorting prohormones, such as pro-opiomelanocortin (POMC), to regulated secretory vesicles. We found that CPE co-localizes with and interacts with GH in AtT20 pituitary cells. Downregulation of CPE led to decreased levels of GH secretion, consistent with involvement of CPE in GH sorting/secretion. Our binding assay in vitro with bacterially expressed proteins suggested that GH directly interacts with CPE but in a manner different from POMC. Korean Society for Molecular and Cellular Biology 2016-10-31 2016-10-28 /pmc/articles/PMC5104884/ /pubmed/27788574 http://dx.doi.org/10.14348/molcells.2016.0183 Text en © The Korean Society for Molecular and Cellular Biology. All rights reserved. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/.
spellingShingle Article
Mizutani, Akiko
Inoko, Hidetoshi
Tanaka, Masafumi
Carboxypeptidase E, Identified As a Direct Interactor of Growth Hormone, Is Important for Efficient Secretion of the Hormone
title Carboxypeptidase E, Identified As a Direct Interactor of Growth Hormone, Is Important for Efficient Secretion of the Hormone
title_full Carboxypeptidase E, Identified As a Direct Interactor of Growth Hormone, Is Important for Efficient Secretion of the Hormone
title_fullStr Carboxypeptidase E, Identified As a Direct Interactor of Growth Hormone, Is Important for Efficient Secretion of the Hormone
title_full_unstemmed Carboxypeptidase E, Identified As a Direct Interactor of Growth Hormone, Is Important for Efficient Secretion of the Hormone
title_short Carboxypeptidase E, Identified As a Direct Interactor of Growth Hormone, Is Important for Efficient Secretion of the Hormone
title_sort carboxypeptidase e, identified as a direct interactor of growth hormone, is important for efficient secretion of the hormone
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5104884/
https://www.ncbi.nlm.nih.gov/pubmed/27788574
http://dx.doi.org/10.14348/molcells.2016.0183
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