Peptidylprolyl isomerase D
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RefSeq (protein) | |||||||||
Location (UCSC) | Chr 4: 158.71 – 158.72 Mb | Chr 3: 79.5 – 79.51 Mb | |||||||
PubMed search | [3] | [4] |
View/Edit Human | View/Edit Mouse |
Peptidylprolyl isomerase D (cyclophilin D), also known as PPID, is an
Structure
Like other cyclophilins, PPID forms a
Function
The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (
Clinical Significance
As a cyclophilin, PPID binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets calcineurin to inhibit the signaling pathway for T-cell activation.
In cardiac myogenic cells, cyclophilins have been observed to be activated by heat shock and hypoxia-reoxygenation as well as complex with heat shock proteins. Thus, cyclophilins may function in cardioprotection during
Currently, cyclophilin expression is highly correlated with cancer pathogenesis, but the specific mechanisms remain to be elucidated.[7] Studies have shown that PPID protects human keratinocytes from UVA-induced apoptosis, so medication and therapies that inhibit PPID, such as CsA, may inadvertently aid skin cancer development. Conversely, treatments promoting PPID activity may improve patient outcomes when paired with UVA therapies against cancer.[10]
Interactions
PPID has been shown to
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000171497 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027804 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b "Entrez Gene: PPID peptidylprolyl isomerase D (cyclophilin D)".
- ^ PMID 1530810.
- ^ S2CID 11678319.
- ^ PMID 15963461.
- PMID 24990953.
- ^ PMID 23220213.
- S2CID 32395688.
Further reading
- Berardini TZ, Bollman K, Sun H, Poethig RS (Mar 2001). "Regulation of vegetative phase change in Arabidopsis thaliana by cyclophilin 40". Science. 291 (5512): 2405–7. S2CID 31121128.
- Kieffer LJ, Thalhammer T, Handschumacher RE (Mar 1992). "Isolation and characterization of a 40-kDa cyclophilin-related protein". The Journal of Biological Chemistry. 267 (8): 5503–7. PMID 1544925.
- Hoffmann K, Kakalis LT, Anderson KS, Armitage IM, Handschumacher RE (Apr 1995). "Expression of human cyclophilin-40 and the effect of the His141-->Trp mutation on catalysis and cyclosporin A binding". European Journal of Biochemistry. 229 (1): 188–93. PMID 7744028.
- Kieffer LJ, Seng TW, Li W, Osterman DG, Handschumacher RE, Bayney RM (Jun 1993). "Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterization". The Journal of Biological Chemistry. 268 (17): 12303–10. PMID 8509368.
- Yokoi H, Shimizu Y, Anazawa H, Lefebvre CA, Korneluk RG, Ikeda JE (Aug 1996). "The structure and complete nucleotide sequence of the human cyclophilin 40 (PPID) gene". Genomics. 35 (3): 448–55. PMID 8812478.
- Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. PMID 8889548.
- Silverstein AM, Galigniana MD, Chen MS, Owens-Grillo JK, Chinkers M, Pratt WB (Jun 1997). "Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin". The Journal of Biological Chemistry. 272 (26): 16224–30. PMID 9195923.
- Young JC, Obermann WM, Hartl FU (Jul 1998). "Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90". The Journal of Biological Chemistry. 273 (29): 18007–10. PMID 9660753.
- Mark PJ, Ward BK, Kumar P, Lahooti H, Minchin RF, Ratajczak T (Jan 2001). "Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shock". Cell Stress & Chaperones. 6 (1): 59–70. PMID 11525244.)
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: CS1 maint: DOI inactive as of April 2024 (link - Ward BK, Allan RK, Mok D, Temple SE, Taylor P, Dornan J, Mark PJ, Shaw DJ, Kumar P, Walkinshaw MD, Ratajczak T (Oct 2002). "A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90". The Journal of Biological Chemistry. 277 (43): 40799–809. PMID 12145316.
- McStay GP, Clarke SJ, Halestrap AP (Oct 2002). "Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore". The Biochemical Journal. 367 (Pt 2): 541–8. PMID 12149099.
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. S2CID 23783563.
- Schubert A, Grimm S (Jan 2004). "Cyclophilin D, a component of the permeability transition-pore, is an apoptosis repressor". Cancer Research. 64 (1): 85–93. PMID 14729611.
- Machida K, Osada H (Dec 2003). "Molecular interaction between cyclophilin D and adenine nucleotide translocase in cytochrome c release: does it determine whether cytochrome c release is dependent on permeability transition or not?". Annals of the New York Academy of Sciences. 1010 (1): 182–5. S2CID 1034903.
- Carrello A, Allan RK, Morgan SL, Owen BA, Mok D, Ward BK, Minchin RF, Toft DO, Ratajczak T (2005). "Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70". Cell Stress & Chaperones. 9 (2): 167–81. PMID 15497503.)
{{cite journal}}
: CS1 maint: DOI inactive as of April 2024 (link - Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (Mar 2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. S2CID 39457788.
- Machida K, Ohta Y, Osada H (May 2006). "Suppression of apoptosis by cyclophilin D via stabilization of hexokinase II mitochondrial binding in cancer cells". The Journal of Biological Chemistry. 281 (20): 14314–20. PMID 16551620.
- Mok D, Allan RK, Carrello A, Wangoo K, Walkinshaw MD, Ratajczak T (May 2006). "The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains". FEBS Letters. 580 (11): 2761–8. S2CID 26811748.