Preparation of protein transduction domain-fused peptidyl prolyl cis/trans isomerase pin1

Tsubasa Ohashi; Sumito Teshima; Masafumi Hidaka; Takafumi Uchida

doi:10.1271/bbb.100372

Preparation of protein transduction domain-fused peptidyl prolyl cis/trans isomerase pin1

Tsubasa Ohashi, Sumito Teshima, Masafumi Hidaka, Takafumi Uchida

AGR - Agricultural Chemistry

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

1 Citation (Scopus)

Abstract

The phenotypes of mice lacking peptidyl prolyl cis/trans isomerase Pin1 (Pin1^-/-) indicated that deficient Pin1 might be related to a variety of diseases. We created TAT-Pin1, a fusion protein of human immunodeficiency virus 1 trans-activator of transcription factor with Pin1. Treatment of HeLa cells with TAT-Pin1 increased the ratio of the S phase. Moreover, TAT-Pin1 restored the proliferating function of Pin1^-/- mouse embryonic fibroblasts which cannot restart proliferation after G0 arrest. These results indicate that TAT-Pin1 is useful in studying the functions of Pin1 and can be developed as a macromolecular drug for diseases related to Pin1 loss.

Original language	English
Pages (from-to)	2067-2070
Number of pages	4
Journal	Bioscience, Biotechnology and Biochemistry
Volume	74
Issue number	10
DOIs	https://doi.org/10.1271/bbb.100372
Publication status	Published - 2010

Keywords

Cell cycle
Peptidyl prolyl cis/trans isomerase Pin1
Protein transduction domain human immunodeficiency virus-1 trans-actuvatir if transcription factor (TAT)

ASJC Scopus subject areas

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1271/bbb.100372

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title = "Preparation of protein transduction domain-fused peptidyl prolyl cis/trans isomerase pin1",

abstract = "The phenotypes of mice lacking peptidyl prolyl cis/trans isomerase Pin1 (Pin1-/-) indicated that deficient Pin1 might be related to a variety of diseases. We created TAT-Pin1, a fusion protein of human immunodeficiency virus 1 trans-activator of transcription factor with Pin1. Treatment of HeLa cells with TAT-Pin1 increased the ratio of the S phase. Moreover, TAT-Pin1 restored the proliferating function of Pin1-/- mouse embryonic fibroblasts which cannot restart proliferation after G0 arrest. These results indicate that TAT-Pin1 is useful in studying the functions of Pin1 and can be developed as a macromolecular drug for diseases related to Pin1 loss.",

keywords = "Cell cycle, Peptidyl prolyl cis/trans isomerase Pin1, Protein transduction domain human immunodeficiency virus-1 trans-actuvatir if transcription factor (TAT)",

author = "Tsubasa Ohashi and Sumito Teshima and Masafumi Hidaka and Takafumi Uchida",

note = "Funding Information: The work has been supported by a Grant-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan, Seeds Discovery Grant of JST and {\textquoteleft}{\textquoteleft}Mishima Kaiun{\textquoteright}{\textquoteright} foundation.",

year = "2010",

doi = "10.1271/bbb.100372",

language = "English",

volume = "74",

pages = "2067--2070",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "10",

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TY - JOUR

T1 - Preparation of protein transduction domain-fused peptidyl prolyl cis/trans isomerase pin1

AU - Ohashi, Tsubasa

AU - Teshima, Sumito

AU - Hidaka, Masafumi

AU - Uchida, Takafumi

N1 - Funding Information: The work has been supported by a Grant-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan, Seeds Discovery Grant of JST and ‘‘Mishima Kaiun’’ foundation.

PY - 2010

Y1 - 2010

N2 - The phenotypes of mice lacking peptidyl prolyl cis/trans isomerase Pin1 (Pin1-/-) indicated that deficient Pin1 might be related to a variety of diseases. We created TAT-Pin1, a fusion protein of human immunodeficiency virus 1 trans-activator of transcription factor with Pin1. Treatment of HeLa cells with TAT-Pin1 increased the ratio of the S phase. Moreover, TAT-Pin1 restored the proliferating function of Pin1-/- mouse embryonic fibroblasts which cannot restart proliferation after G0 arrest. These results indicate that TAT-Pin1 is useful in studying the functions of Pin1 and can be developed as a macromolecular drug for diseases related to Pin1 loss.

AB - The phenotypes of mice lacking peptidyl prolyl cis/trans isomerase Pin1 (Pin1-/-) indicated that deficient Pin1 might be related to a variety of diseases. We created TAT-Pin1, a fusion protein of human immunodeficiency virus 1 trans-activator of transcription factor with Pin1. Treatment of HeLa cells with TAT-Pin1 increased the ratio of the S phase. Moreover, TAT-Pin1 restored the proliferating function of Pin1-/- mouse embryonic fibroblasts which cannot restart proliferation after G0 arrest. These results indicate that TAT-Pin1 is useful in studying the functions of Pin1 and can be developed as a macromolecular drug for diseases related to Pin1 loss.

KW - Cell cycle

KW - Peptidyl prolyl cis/trans isomerase Pin1

KW - Protein transduction domain human immunodeficiency virus-1 trans-actuvatir if transcription factor (TAT)

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U2 - 10.1271/bbb.100372

DO - 10.1271/bbb.100372

M3 - Article

C2 - 20944414

AN - SCOPUS:78049413628

SN - 0916-8451

VL - 74

SP - 2067

EP - 2070

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 10

ER -

Preparation of protein transduction domain-fused peptidyl prolyl cis/trans isomerase pin1

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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