The human FK506-binding proteins: characterization of human FKBP19

Rulten, Stuart L.; Kinloch, Ross A.; Tateossian, Hilda; Robinson, Colin; Gettins, Lucy; Kay, John E.

doi:10.1007/s00335-005-0127-7

Cited by 56 publications

(51 citation statements)

References 38 publications

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“…This is similar to the carboxyl-terminal portion of FKBP65 (10). The function of mammalian FKBP22 is not well understood and differs from the well characterized bacterial system in key aspects (39 -41).…”

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confidence: 60%

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A Substrate Preference for the Rough Endoplasmic Reticulum Resident Protein FKBP22 during Collagen Biosynthesis

Ishikawa

Bächinger

2014

Journal of Biological Chemistry

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Background: Procollagen biosynthesis requires a large number of foldases, chaperones, and modifying enzymes. Results: FKBP22 is a foldase and chaperone that interacts with a subset of collagens. Conclusion: Collagen type-specific chaperones and foldases exist in the rER. Significance: The lack of collagen type-specific rER proteins can lead to broader or overlapping phenotypes of connective tissue disorders.

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confidence: 60%

“…This isomerization is catalyzed by peptidylprolyl cis-trans isomerases (PPIases) (6 -9). PPIases are found ubiquitously in all cellular compartments (10,11). Seven PPIases reside in the rER, and three of them, cyclophilin B (CypB) and FK506-binding protein (FKBP) 65 and 22, were shown to be involved in procollagen biosynthesis (4).…”

mentioning

confidence: 99%

A Substrate Preference for the Rough Endoplasmic Reticulum Resident Protein FKBP22 during Collagen Biosynthesis

Ishikawa

Bächinger

2014

Journal of Biological Chemistry

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“…FKBPs are members of the immunophilins, enzymes with a peptidyl-prolyl cis-trans isomerase (PPIase) activity that bind to immunosuppressants such as FK506 (Göthel and Marahiel, 1999). The human FKBP family counts 15 principal members with many different functions (Galat, 2003;Rulten et al, 2006). Four members of this family, FKBP12, FKBP38, FKBP52, and FKBP65, are enriched in the human brain (Steiner et al, 1992;Charters et al, 1994a,b;Coss et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Inhibition of FK506 Binding Proteins Reduces α-Synuclein Aggregation and Parkinson's Disease-Like Pathology

Gérard¹,

Deleersnijder²,

Daniëls³

et al. 2010

J. Neurosci.

109

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“…We also noticed genes encoding for enzymes involved in energy homeostase, such as CKB (creatine kinase) and FKBP11 (peptidyl prolylisomerase), with the latter described as inhibited by rapamycin (45).…”

Section: Discussionmentioning

confidence: 98%

Gene Expression Profile in Response to Doxorubicin–Rapamycin Combined Treatment of HER-2–Overexpressing Human Mammary Epithelial Cell Lines

Trapé

Katayama

Roela

et al. 2012

Molecular Cancer Therapeutics

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HER-2-positive breast cancers frequently sustain elevated AKT/mTOR signaling, which has been associated with resistance to doxorubicin treatment. Here, we investigated whether rapamycin, an mTOR inhibitor, increased the sensitivity to doxorubicin therapy in two HER-2-overexpressing cell lines: C5.2, which was derived from the parental HB4a by transfection with HER-2 and SKBR3, which exhibits HER-2 amplification. The epithelial mammary cell line HB4a was also analyzed. The combined treatment using 20 nmol/L of rapamycin and 30 nmol/L of doxorubicin arrested HB4a and C5.2 cells in S to G 2 -M, whereas SKBR3 cells showed an increase in the G 0 -G 1 phase. Rapamycin increased the sensitivity to doxorubicin in HER-2-overexpressing cells by approximately 2-fold, suggesting that the combination displayed a more effective antiproliferative action. Gene expression profiling showed that these results might reflect alterations in genes involved in canonical pathways related to purine metabolism, oxidative phosphorylation, protein ubiquitination, and mitochondrial dysfunction. A set of 122 genes modulated by the combined treatment and specifically related to HER-2 overexpression was determined by finding genes commonly regulated in both C5.2 and SKBR3 that were not affected in HB4a cells. Network analysis of this particular set showed a smaller subgroup of genes in which coexpression pattern in HB4a cells was disrupted in C5.2 and SKBR3. Altogether, our data showed a subset of genes that might be more robust than individual markers in predicting the response of HER-2-overexpressing breast cancers to doxorubicin and rapamycin combination. Mol Cancer Ther; 11(2); 464-74. Ó2011 AACR.

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The human FK506-binding proteins: characterization of human FKBP19

Cited by 56 publications

References 38 publications

A Substrate Preference for the Rough Endoplasmic Reticulum Resident Protein FKBP22 during Collagen Biosynthesis

A Substrate Preference for the Rough Endoplasmic Reticulum Resident Protein FKBP22 during Collagen Biosynthesis

Inhibition of FK506 Binding Proteins Reduces α-Synuclein Aggregation and Parkinson's Disease-Like Pathology

Gene Expression Profile in Response to Doxorubicin–Rapamycin Combined Treatment of HER-2–Overexpressing Human Mammary Epithelial Cell Lines

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