CPVL

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CPVL
Identifiers
Aliases CPVL, HVLP, carboxypeptidase, vitellogenic like
External IDs MGI: 1918537 HomoloGene: 80235 GeneCards: CPVL
RNA expression pattern
PBB GE CPVL 208146 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_019029
NM_031311

NM_001289713
NM_001289714
NM_027749

RefSeq (protein)

NP_061902
NP_112601
NP_001334981
NP_001334983

Location (UCSC) Chr 7: 29 – 29.2 Mb Chr 6: 53.87 – 53.98 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Probable serine carboxypeptidase CPVL is an enzyme that in humans is encoded by the CPVL gene.[3][4] The "CPVL" gene is expressed mainly in monocytes and macrophages,[3] and it is located in the endoplasmatic reticulum and in the endosomal/lysosomal compartment. The distribution of CPVL suggests that the enzyme may be involved in antigen processing and the secretory pathway.[5] Besides those macrophages-rich tissues, the heart and kidney also express high levels of CPVL mRNA.The enzyme is similar to the carboxypeptidases CATHA and SCPEP1, but no direct confirmation of the enzymatic activity was obtained so far.[6] The exact function of this protein, however, has not been determined.

Structure[edit]

Gene[edit]

"CPVL" gene is located at chromosome 7p15.1, consisting of 14 exons.At least two alternatively spliced transcripts which encode the same protein have been observed.[4]

Protein[edit]

The designation of CPVL is a true serine carboxypeptidase. Although the primary sequence displays the expected serine carboxypeptidase active site, the enzymatic activity remains to be demonstrated. The primary sequence of CPVL contains a putative signal sequence, four potential N-linked glycosylation sites and four myristoylation sites, but no transmembrane domain, suggesting that it may be luminal in an organelle and/or involved in the secretory pathway.[5]

Function[edit]

Although the primary sequence of CPVL bears every hallmarks of a serine carboxypeptidase, the enzymatic function of CPVL has not been confirmed. On the basis of its localization, CPVL is postulated to play a role in the biosynthesis of secretory molecules or in the processing and transport of peptides for loading onto MHC Ⅰ molecules, or in MHC Ⅱ-dependent APC functions.[5] The high-level expression of CPVL mRNA in heart and kidney implies that CPVL may also have extraimmune functions, such as regulation of cardiovascular homeostasis.[3]

Clinical significance[edit]

The deletion of this gene has been reported associated with Wilms tumor.[7] GWAS show that genetic variations of the CPVL gene are associated with susceptibility to diabetic nephropathy in European Americans, Japanese and Chinese.[8][9][10] CPVL is also reported to be one of the four down-regulated proteins which is related to severity of inflammation, and it may be a potential biomarker for identification of infection and prediction of outcome.[11]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b c Mahoney JA, Ntolosi B, DaSilva RP, Gordon S, McKnight AJ (March 2001). "Cloning and characterization of CPVL, a novel serine carboxypeptidase, from human macrophages". Genomics. 72 (3): 243–51. doi:10.1006/geno.2000.6484. PMID 11401439. 
  4. ^ a b "Entrez Gene: CPVL carboxypeptidase, vitellogenic-like". 
  5. ^ a b c Harris J, Schwinn N, Mahoney JA, Lin HH, Shaw M, Howard CJ, da Silva RP, Gordon S (February 2006). "A vitellogenic-like carboxypeptidase expressed by human macrophages is localized in endoplasmic reticulum and membrane ruffles". International Journal of Experimental Pathology. 87 (1): 29–39. doi:10.1111/j.0959-9673.2006.00450.x. PMC 2517344Freely accessible. PMID 16436111. 
  6. ^ Pshezhetsky AV, Hinek A (January 2009). "Serine carboxypeptidases in regulation of vasoconstriction and elastogenesis". Trends in Cardiovascular Medicine. 19 (1): 11–7. doi:10.1016/j.tcm.2009.03.002. PMID 19467448. 
  7. ^ Grundy RG, Pritchard J, Scambler P, Cowell JK (July 1998). "Loss of heterozygosity for the short arm of chromosome 7 in sporadic Wilms tumour". Oncogene. 17 (3): 395–400. doi:10.1038/sj.onc.1201927. PMID 9690521. 
  8. ^ Maeda S, Araki S, Babazono T, Toyoda M, Umezono T, Kawai K, Imanishi M, Uzu T, Watada H, Suzuki D, Kashiwagi A, Iwamoto Y, Kaku K, Kawamori R, Nakamura Y (August 2010). "Replication study for the association between four Loci identified by a genome-wide association study on European American subjects with type 1 diabetes and susceptibility to diabetic nephropathy in Japanese subjects with type 2 diabetes". Diabetes. 59 (8): 2075–9. doi:10.2337/db10-0067. PMC 2911071Freely accessible. PMID 20460425. 
  9. ^ Hu C, Zhang R, Yu W, Wang J, Wang C, Pang C, Ma X, Bao Y, Xiang K, Jia W (November 2011). "CPVL/CHN2 genetic variant is associated with diabetic retinopathy in Chinese type 2 diabetic patients". Diabetes. 60 (11): 3085–9. doi:10.2337/db11-0028. PMC 3198055Freely accessible. PMID 21911749. 
  10. ^ Mooyaart AL, Valk EJ, van Es LA, Bruijn JA, de Heer E, Freedman BI, Dekkers OM, Baelde HJ (March 2011). "Genetic associations in diabetic nephropathy: a meta-analysis". Diabetologia. 54 (3): 544–53. doi:10.1007/s00125-010-1996-1. PMC 3034040Freely accessible. PMID 21127830. 
  11. ^ Bauer M, Giamarellos-Bourboulis EJ, Kortgen A, Möller E, Felsmann K, Cavaillon JM, Guntinas-Lichius O, Rutschmann O, Ruryk A, Kohl M, Wlotzka B, Rußwurm S, Marshall JC, Reinhart K (April 2016). "A Transcriptomic Biomarker to Quantify Systemic Inflammation in Sepsis - A Prospective Multicenter Phase II Diagnostic Study". EBioMedicine. 6: 114–25. doi:10.1016/j.ebiom.2016.03.006. PMC 4856796Freely accessible. PMID 27211554. 

External links[edit]

Further reading[edit]