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Production of recombinant salmon insulin-like growth factor binding protein-1 subtypes

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Title: Production of recombinant salmon insulin-like growth factor binding protein-1 subtypes
Authors: Tanaka, Hanae Browse this author
Oishi, Gakuto Browse this author
Nakano, Yusuke Browse this author
Mizuta, Hiroko Browse this author
Nagano, Yuta Browse this author
Hiramatsu, Naoshi Browse this author →KAKEN DB
Ando, Hironori Browse this author
Shimizu, Munetaka Browse this author →KAKEN DB
Keywords: insulin-like growth factor binding protein-1
recombinant protein
pituitary cell culture
growth hormone release
Issue Date: 1-Feb-2018
Journal Title: General and Comparative Endocrinology
Volume: 257
Start Page: 184
End Page: 191
Publisher DOI: 10.1016/j.ygcen.2017.06.015
PMID: 28666856
Abstract: Insulin-like growth factor (IGF)-I is a growth promoting hormone that exerts its actions through endocrine, paracrine and autocrine modes. Local IGF-I is essential for normal growth, whereas circulating IGF-I plays a crucial role in regulating the production and secretion of growth hormone (GH) by the pituitary gland. These actions of IGF-I are modulated by six insulin-like growth factor binding proteins (IGFBPs). In teleosts, two subtypes of each IGFBP are present due to an extra round of whole-genome duplication. IGFBP-1 is generally inhibitory to IGF-I action under catabolic conditions such as fasting and stress. In salmon, IGFBP-1a and -1b are two of three major circulating IGFBPs and assumed to affect growth through modulating IGF-I action. However, exact functions of salmon IGFBP-1 subtypes on growth regulation are not known due to the lack of purified or recombinant protein. We expressed recombinant salmon (rs) IGFBP-1a and -1b with a fusion protein (thioredoxin, Trx) and a His-tag using the pET-32a(+) vector expression system in Escherichia coli. Trx.His.rsIGFBP-1s were isolated by Ni-affinity chromatography, enzymatically cleaved by enterokinase to remove the fusion partners and further purified by reversed-phase HPLC. We next examined effects of rsIGFBP-1a and -1b in combination with human IGF-I on GH release from cultured masu salmon (Oncorhynchus masou) pituitary cells. Unexpectedly, IGF-I increased GH release and an addition of rsIGFBP-1a, but not rsIGFBP-1b, restored GH levels. The results suggest that IGFBP-1a can inhibit IGF-I action on the pituitary in masu salmon. Availability of recombinant salmon IGFBP-1s should facilitate further functional analyses and assay development.
Rights: © 2018. This manuscript version is made available under the CC-BY-NC-ND 4.0 license
Type: article (author version)
Appears in Collections:水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 清水 宗敬

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