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Gene Symbol |
PEPD |
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Aliases |
PROLIDASE |
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Entrez Gene ID |
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Gene Name |
Peptidase D |
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Chromosomal Location |
19q13.11 |
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HGNC ID |
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Summary |
This gene encodes a member of the peptidase family. The protein forms a homodimer that hydrolyzes dipeptides or tripeptides with C-terminal proline or hydroxyproline residues. The enzyme serves an important role in the recycling of proline, and may be rate limiting for the production of collagen. Mutations in this gene result in prolidase deficiency, which is characterized by the excretion of large amount of di- and tri-peptides containing proline. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Oct 2009]
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RefSeq DNA |
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RefSeq mRNA |
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e!Ensembl
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| Protein Information |
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Protein Name |
Xaa-Pro dipeptidase, X-Pro dipeptidase, aminoacyl-L-proline hydrolase, imidodipeptidase, proline dipeptidase, testicular tissue protein Li 138 |
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Function |
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Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen |
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UniProt |
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PDB |
2IW2, 2OKN, 5M4G, 5M4J, 5M4L, 5M4Q, 5MBY, 5MBZ, 5MC0, 5MC1, 5MC2, 5MC3, 5MC4, 5MC5, 6H2P, 6H2Q |
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Interactions |
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| STRING |
MINT |
IntAct |
| ENSP00000446252 |
P04179 |
P04179 |
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View interactions
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Associated Diseases
| Disease group | Disease Name | References |
| Congenital, Hereditary, and Neonatal Diseases and Abnormalities |
| Prolidase deficiency |
19308961, 8198124, 26110198, 2365824, 17142620, 8900231, 16470701, 12384772, 6637477, 24033266, 23516557, 1972707 |
| Endocrine System Diseases |
| Diabetes Mellitus |
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| PCOS |
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| Psychiatric/Brain disorders |
| Schizophrenia |
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| Intellectual Disability |
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| Panic Disorder |
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References |
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| Gupta Sajal, Ghulmiyyah Jana, Sharma Rakesh, Halabi Jacques, Agarwal Ashok |
| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA.| Center for Reproductive Medicine, Cleveland Clinic Foundation, 10681 Carnegie Avenue, Desk X11, Cleveland, OH 44195, USA. |
| Biomed Res Int. 2014;2014:916212. doi: 10.1155/2014/916212. Epub 2014 May 12. |
Abstract
Endometriosis, PCOS, and unexplained infertility are currently the most common diseases rendering large numbers of women infertile worldwide. Oxidative stress, due to its deleterious effects on proteins and nucleic acids, is postulated to be the one of the important mechanistic pathways in differential expression of proteins and in these diseases. The emerging field of proteomics has allowed identification of proteins involved in cell cycle, as antioxidants, extracellular matrix (ECM), cytoskeleton, and their linkage to oxidative stress in female infertility related diseases. The aim of this paper is to assess the association of oxidative stress and protein expression in the reproductive microenvironments such as endometrial fluid, peritoneal fluid, and follicular fluid, as well as reproductive tissues and serum. The review also highlights the literature that proposes the use of the fertility related proteins as potential biomarkers for noninvasive and early diagnosis of the aforementioned diseases rather than utilizing the more invasive methods used currently. The review will highlight the power of proteomic profiles identified in infertility related disease conditions and their linkage with underlying oxidative stress. The power of proteomics will be reviewed with regard to eliciting molecular mechanisms for early detection and management of these infertility related conditions. |
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