18-549: PPID may refer to: Peptidylprolyl isomerase D , and enzyme encoded within the PPID gene Pituitary pars intermedia dysfunction in horses. Computer Science [ edit ] Private Personal Identifier in Security Assertion Markup Language Parent process ID. Process identifier of the parent of a process. Topics referred to by
36-452: A C-terminal tetratricopeptide repeat (TPR) domain . The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase ( PPIase ) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Generally, PPIases are found in all eubacteria and eukaryotes, as well as in a few archaea, and thus are highly conserved. The PPIase family
54-423: A β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti-parallel β-strands and capped by two α-helices at the top and bottom. In addition, the β-turns and loops in the strands contribute to the flexibility of the barrel. PPID in particular is composed of 370 residues and shares structural homology with PPIF , FKBP4 , and FKBP5 , including an N-terminal immunophilin-like domain and
72-559: A PPID inhibitor, prevents cytochrome C release and significantly reduces cell death in neurons. As such, PPID proves to be an effective therapeutic target for patients suffering neurodegenerative diseases. In addition, PPIF, as part of the MPTP, is involved in ischemia/reperfusion injury, traumatic brain injury (TBI), muscular dystrophy, and drug toxicity. Though PPIF was identified as a candidate for dilated cardiomyopathy (DCM) for one afflicted family, further study revealed no mutations in
90-467: A cyclophilin, PPI binds cyclosporin A (CsA) and can be found within the cell or secreted by the cell. In eukaryotes, cyclophilins localize ubiquitously to many cell and tissue types, though studies on PPIF focus primarily on heart, liver, and brain tissue. In addition to PPIase and protein chaperone activities, cyclophilins also function in mitochondrial metabolism, apoptosis, immunological response, inflammation, and cell growth and proliferation. PPIF
108-466: 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 ischemia-reperfusion injury . Currently, cyclophilin expression
126-443: A cyclophilin, PPIF binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets calcineurin to inhibit the signaling pathway for T-cell activation. Due to its association with the MPTP, PPIF is also involved in neurodegenerative diseases, including glaucoma , diabetic retinopathy , Parkinson's disease , and Alzheimer's disease . For neurodegenerative diseases, treatment of reperfusion events with CsA,
144-400: A β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti-parallel β-strands and capped by two α-helices at the top and bottom. In addition, the β-turns and loops in the strands contribute to the flexibility of the barrel. PPIF weighs 17.5 kDa and forms part of the MPTP in the inner mitochondrial membrane (IMM). The protein encoded by this gene is a member of
162-456: Is a major component of the mitochondrial permeability transition pore (MPTP) and, thus, highly involved in mitochondrial metabolism and apoptosis , as well as in mitochondrial diseases and related conditions, including cardiac diseases, neurodegenerative diseases, and muscular dystrophy . In addition, PPIF participates in inflammation , as well as in ischemic reperfusion injury , AIDS , and cancer . Like other cyclophilins, PPIF forms
180-519: Is an enzyme that in humans is encoded by the PPIF gene . It has also been referred to as, but should not be confused with, cyclophilin D (CypD), which is encoded by the PPID gene. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds , which allows it to facilitate folding or repair of proteins. PPIF
198-466: Is different from Wikidata All article disambiguation pages All disambiguation pages Peptidylprolyl isomerase D 5481 67738 ENSG00000171497 ENSMUSG00000027804 Q08752 Q9CR16 NM_005038 NM_026352 NM_001356326 NP_005029 NP_080628 NP_001343255 Peptidylprolyl isomerase D (cyclophilin D) , also known as PPID , is an enzyme which in humans
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#1732787087932216-613: Is encoded by the PPID gene on chromosome 4. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds , which allows it to facilitate folding or repair of proteins. In addition, PPID participates in many biological processes, including mitochondrial metabolism , apoptosis , redox , and inflammation , as well as in related diseases and conditions, such as ischemic reperfusion injury , AIDS , and cancer . Like other cyclophilins, PPID forms
234-532: Is especially involved in mitochondrial apoptosis as a major component of the MPTP. Through its PPIase ability, the protein interacts with and induces a conformational change in adenine nucleotide translocase ( ANT ), the other MPTP component. This activation, along with high calcium ion levels, induces the opening the MPTP, resulting in mitochondrial swelling, increasing reactive oxygen species (ROS) levels, membrane depolarization , failing ATP production, caspase cascade activation, and ultimately, apoptosis. As
252-568: Is further divided into three structurally distinct subfamilies: cyclophilin (CyP), FK506-binding protein ( FKBP ), and parvulin (Pvn). As a cyclophilin, PPID binds cyclosporin A (CsA) and can be found within the cell or secreted by the cell. In eukaryotes, cyclophilins localize ubiquitously to many cell and tissue types. In addition to PPIase and protein chaperone activities, cyclophilins also function in mitochondrial metabolism, apoptosis, immunological response, inflammation, and cell growth and proliferation. PPID in particular helps chaperone
270-987: Is highly correlated with cancer pathogenesis, but the specific mechanisms remain to be elucidated. 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. PPID has been shown to interact with: PPIF 2BIT , 2BIU , 2Z6W , 3QYU , 3R49 , 3R4G , 3R54 , 3R56 , 3R57 , 3R59 , 3RCF , 3RCG , 3RCI , 3RCK , 3RCL , 3RD9 , 3RDA , 3RDB , 3RDC , 4J58 , 4J59 , 4J5A , 4J5B , 4J5C , 4J5D , 4J5E , 4O8H , 4O8I , 4XNC , 4ZSC , 4ZSD , 5A0E , 5CCS , 5CCN , 5CCQ , 5CBT , 5CCR 10105 105675 ENSG00000108179 ENSMUSG00000021868 P30405 Q99KR7 NM_005729 NM_134084 NP_005720 NP_598845 Peptidyl-prolyl cis-trans isomerase, mitochondrial (PPIF)
288-468: The assembly of heat shock protein Hsp90 , as well as the nuclear localization of glucocorticoid, estrogen and progesterone receptors. Along with PPIF, PPID regulates mitochondrial apoptosis. In response to elevated reactive oxygen species (ROS) and calcium ion levels, PPID interacts with Bax to promote mitochondrial pore formation, thus releasing pro-apoptotic factors such as cytochrome C and AIF . As
306-497: The peptidyl-prolyl cis-trans isomerase ( PPIase ) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Generally, PPIases are found in all eubacteria and eukaryotes, as well as in a few archaebacteria, and thus are highly conserved. The PPIase family is further divided into three structurally distinct subfamilies: cyclophilin (CyP), FK506-binding protein ( FKBP ), and parvulin (Pvn). As
324-405: The same term [REDACTED] This disambiguation page lists articles associated with the title PPID . If an internal link led you here, you may wish to change the link to point directly to the intended article. Retrieved from " https://en.wikipedia.org/w/index.php?title=PPID&oldid=1190419641 " Category : Disambiguation pages Hidden categories: Short description
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