cDNA cloning and expression of human activin βE subunit

Osamu Hashimoto; Kunihiro Tsuchida; Yuuki Ushiro; Yuko Hosoi; Nobuhiko Hoshi; Hiromu Sugino; Yoshihisa Hasegawa

doi:10.1016/S0303-7207(02)00157-0

cDNA cloning and expression of human activin βE subunit

Osamu Hashimoto, Kunihiro Tsuchida, Yuuki Ushiro, Yuko Hosoi, Nobuhiko Hoshi, Hiromu Sugino, Yoshihisa Hasegawa

Research output: Contribution to journal › Article › peer-review

47 Citations (Scopus)

Abstract

We cloned human activin βE subunit cDNA from a liver cDNA library using the polymerase chain reaction (PCR) technique. The deduced amino acid sequence was 97 and 96% homologous to the mouse and rat activin βE subunits. Human activin βE subunit tagged with Myc and polyhistidine residues at the COOH terminus was expressed in mammalian cells and secreted into the medium as a disulphide-linked homodimer protein. We also found that the human activin βE protein could bind to follistatin, an activin-binding protein. Northern blot analysis showed that this gene was expressed as a major transcript of 2.7 kb predominantly in human liver. These findings suggest that activin E (dimeric protein) may play a role in humans.

Original language	English
Pages (from-to)	117-122
Number of pages	6
Journal	Molecular and Cellular Endocrinology
Volume	194
Issue number	1-2
DOIs	https://doi.org/10.1016/S0303-7207(02)00157-0
Publication status	Published - 30-08-2002
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Endocrinology

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10.1016/S0303-7207(02)00157-0

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title = "cDNA cloning and expression of human activin βE subunit",

abstract = "We cloned human activin βE subunit cDNA from a liver cDNA library using the polymerase chain reaction (PCR) technique. The deduced amino acid sequence was 97 and 96% homologous to the mouse and rat activin βE subunits. Human activin βE subunit tagged with Myc and polyhistidine residues at the COOH terminus was expressed in mammalian cells and secreted into the medium as a disulphide-linked homodimer protein. We also found that the human activin βE protein could bind to follistatin, an activin-binding protein. Northern blot analysis showed that this gene was expressed as a major transcript of 2.7 kb predominantly in human liver. These findings suggest that activin E (dimeric protein) may play a role in humans.",

author = "Osamu Hashimoto and Kunihiro Tsuchida and Yuuki Ushiro and Yuko Hosoi and Nobuhiko Hoshi and Hiromu Sugino and Yoshihisa Hasegawa",

note = "Funding Information: This work was supported by a grant from Kitasato University Research Grant for Young Researchers (to O. Hashimoto), by a Grant for Encouragement of Young Scientists from Kitasato University, School of Veterinary Medicine and Animal Sciences (to O. Hashimoto), and by Grants-in-Aid for Encouragement of Young Scientists (13760212) from the Ministry of Education, Science, Sports and Culture of Japan (to O. Hashimoto). The authors thank Ms. Janet K. Cook for revising the English text.",

year = "2002",

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doi = "10.1016/S0303-7207(02)00157-0",

language = "English",

volume = "194",

pages = "117--122",

journal = "Molecular and Cellular Endocrinology",

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TY - JOUR

T1 - cDNA cloning and expression of human activin βE subunit

AU - Hashimoto, Osamu

AU - Tsuchida, Kunihiro

AU - Ushiro, Yuuki

AU - Hosoi, Yuko

AU - Hoshi, Nobuhiko

AU - Sugino, Hiromu

AU - Hasegawa, Yoshihisa

N1 - Funding Information: This work was supported by a grant from Kitasato University Research Grant for Young Researchers (to O. Hashimoto), by a Grant for Encouragement of Young Scientists from Kitasato University, School of Veterinary Medicine and Animal Sciences (to O. Hashimoto), and by Grants-in-Aid for Encouragement of Young Scientists (13760212) from the Ministry of Education, Science, Sports and Culture of Japan (to O. Hashimoto). The authors thank Ms. Janet K. Cook for revising the English text.

PY - 2002/8/30

Y1 - 2002/8/30

N2 - We cloned human activin βE subunit cDNA from a liver cDNA library using the polymerase chain reaction (PCR) technique. The deduced amino acid sequence was 97 and 96% homologous to the mouse and rat activin βE subunits. Human activin βE subunit tagged with Myc and polyhistidine residues at the COOH terminus was expressed in mammalian cells and secreted into the medium as a disulphide-linked homodimer protein. We also found that the human activin βE protein could bind to follistatin, an activin-binding protein. Northern blot analysis showed that this gene was expressed as a major transcript of 2.7 kb predominantly in human liver. These findings suggest that activin E (dimeric protein) may play a role in humans.

AB - We cloned human activin βE subunit cDNA from a liver cDNA library using the polymerase chain reaction (PCR) technique. The deduced amino acid sequence was 97 and 96% homologous to the mouse and rat activin βE subunits. Human activin βE subunit tagged with Myc and polyhistidine residues at the COOH terminus was expressed in mammalian cells and secreted into the medium as a disulphide-linked homodimer protein. We also found that the human activin βE protein could bind to follistatin, an activin-binding protein. Northern blot analysis showed that this gene was expressed as a major transcript of 2.7 kb predominantly in human liver. These findings suggest that activin E (dimeric protein) may play a role in humans.

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AN - SCOPUS:0037200660

SN - 0303-7207

VL - 194

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EP - 122

JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

IS - 1-2

ER -

cDNA cloning and expression of human activin βE subunit

Abstract

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