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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Detalles Bibliográficos
Autores principales: Mizutani, Akiko, Inoko, Hidetoshi, Tanaka, Masafumi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Molecular and Cellular Biology 2016
Materias:
Article
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
Descripción
Sumario: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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