Cyclophilin
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD | |||||||||
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Cyclophilins (CYPs) are a family of
peptide bonds from trans form to cis form at proline residues and facilitates protein folding
.
Cyclophilin A is a
secreted
.
Mammalian cyclophilins
Human genes encoding proteins containing the cyclophilin domain include:
Cyclophilin A
TNF alpha and interleukin 2
.
Cyclophilin A is also known to be recruited by the Gag polyprotein during
HIV-1 virus infection, and its incorporation into new virus particles is essential for HIV-1 infectivity.[5]
Cyclophilin D
Cyclophilin D (PPIF, note that literature is confusing, the mitochondrial cyclophilin is encoded by the PPIF gene), which is located in the
mitochondria fall into a functional disorder, so the opening of the pore plays an important role in cell death
. Cyclophilin D is thought to regulate the opening of the pore because cyclosporin A, which binds to CyP-D, inhibits the pore opening.
However, mitochondria obtained from the cysts of Artemia franciscana, do not exhibit the mitochondrial permeability transition pore [8][9]
Clinical significance
Diseases
Overexpression of Cyclophilin A has been linked to poor response to inflammatory diseases, the progression or metastasis of cancer, and aging.[10]
Cyclophilins as drug targets
Cyclophilin inhibitors, such as
cyclosporin, are being developed to treat neurodegenerative diseases.[11] Cyclophilin inhibition may also be a therapy for liver diseases.[12]
This section needs expansion. You can help by adding to it. (December 2015) |
References
External links
- Cyclophilins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)