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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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HeLa Cells
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Humans
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Mice
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Models, Molecular
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NIMA-Interacting Peptidylprolyl Isomerase
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptidylprolyl Isomerase / chemistry*
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Peptidylprolyl Isomerase / genetics
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Peptidylprolyl Isomerase / metabolism*
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Peptidylprolyl Isomerase / pharmacology
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Protein Engineering / methods*
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Protein Transport
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Recombinant Fusion Proteins / pharmacology
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S Phase / drug effects
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tat Gene Products, Human Immunodeficiency Virus / chemistry
Substances
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NIMA-Interacting Peptidylprolyl Isomerase
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Peptide Fragments
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Recombinant Fusion Proteins
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tat Gene Products, Human Immunodeficiency Virus
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PIN1 protein, human
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Peptidylprolyl Isomerase
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Pin1 protein, mouse