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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Probable serine carboxypeptidase CPVL''' is an [[enzyme]] that in humans is encoded by the ''CPVL'' [[gene]].<ref name="pmid11401439">{{cite journal | vauthors = Mahoney JA, Ntolosi B, DaSilva RP, Gordon S, McKnight AJ | title = Cloning and characterization of CPVL, a novel serine carboxypeptidase, from human macrophages | journal = Genomics | volume = 72 | issue = 3 | pages = 243–51 | date = March 2001 | pmid = 11401439 | pmc =  | doi = 10.1006/geno.2000.6484 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CPVL carboxypeptidase, vitellogenic-like| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54504| accessdate = }}</ref> The "CPVL" gene is expressed mainly in [[monocytes]] and [[macrophages]],<ref name="pmid11401439"/> 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.<ref name="pmid16436111">{{cite journal | vauthors = Harris J, Schwinn N, Mahoney JA, Lin HH, Shaw M, Howard CJ, da Silva RP, Gordon S | title = A vitellogenic-like carboxypeptidase expressed by human macrophages is localized in endoplasmic reticulum and membrane ruffles | journal = International Journal of Experimental Pathology | volume = 87 | issue = 1 | pages = 29–39 | date = February 2006 | pmid = 16436111 | doi = 10.1111/j.0959-9673.2006.00450.x | pmc=2517344}}</ref> Besides those macrophages-rich tissues, the heart and kidney also express high levels of CPVL [[mRNA]].The enzyme is similar to the [[carboxypeptidase]]s [[cathepsin A|CATHA]] and [[SCPEP1]], but no direct confirmation of the enzymatic activity was obtained so far.<ref name="pmid19467448">{{cite journal | vauthors = Pshezhetsky AV, Hinek A | title = Serine carboxypeptidases in regulation of vasoconstriction and elastogenesis | journal = Trends in Cardiovascular Medicine | volume = 19 | issue = 1 | pages = 11–7 | date = January 2009 | pmid = 19467448 | doi = 10.1016/j.tcm.2009.03.002 }}</ref>  The exact function of this protein, however, has not been determined.
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Structure ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Carboxypeptidase, vitellogenic-like
| HGNCid = 14399
| Symbol = CPVL
| AltSymbols =; HVLP; MGC10029
| OMIM = 609780
| ECnumber = 
| Homologene = 80235
| MGIid = 1918537
| GeneAtlas_image1 = PBB_GE_CPVL_208146_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004185 |text = serine carboxypeptidase activity}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 54504
    | Hs_Ensembl = ENSG00000106066
    | Hs_RefseqProtein = NP_061902
    | Hs_RefseqmRNA = NM_019029
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 29001374
    | Hs_GenLoc_end = 29152606
    | Hs_Uniprot = Q9H3G5
    | Mm_EntrezGene = 71287
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = XM_906883
    | Mm_RefseqProtein = XP_911976
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Carboxypeptidase, vitellogenic-like''', also known as '''CPVL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CPVL carboxypeptidase, vitellogenic-like| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54504| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
=== Gene ===
{{PBB_Summary
"CPVL" gene is located at [[chromosome 7]]p15.1, consisting of 14 [[exons]].At least two alternatively spliced transcripts which encode the same protein have been observed.<ref name="entrez" />
| section_title =  
| summary_text = The protein encoded by this gene is a carboxypeptidase and bears strong sequence similarity to serine carboxypeptidases. Carboxypeptidases are a large class of proteases that act to cleave a single amino acid from the carboxy termini of proteins or peptides. The exact function of this protein, however, has not been determined. At least two alternatively spliced transcripts which encode the same protein have been observed.<ref name="entrez">{{cite web | title = Entrez Gene: CPVL carboxypeptidase, vitellogenic-like| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54504| accessdate = }}</ref>
}}


==References==
=== Protein ===
{{reflist|2}}
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.<ref name="pmid16436111"/>
==Further reading==
 
{{refbegin | 2}}
== Function ==
{{PBB_Further_reading
 
| citations =
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 [[Major histocompatibility complex|MHC]] Ⅰ molecules, or in MHC Ⅱ-dependent APC functions.<ref name="pmid16436111"/> 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.<ref name="pmid11401439"/>
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
 
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
== Clinical significance ==
*{{cite journal | author=Striebich CC, Falta MT, Wang Y, ''et al.'' |title=Selective accumulation of related CD4+ T cell clones in the synovial fluid of patients with rheumatoid arthritis. |journal=J. Immunol. |volume=161 |issue= 8 |pages= 4428-36 |year= 1998 |pmid= 9780222 |doi=  }}
 
*{{cite journal | author=Wang X, Stollar BD |title=Immunoglobulin VH gene expression in human aging. |journal=Clin. Immunol. |volume=93 |issue= 2 |pages= 132-42 |year= 1999 |pmid= 10527689 |doi= 10.1006/clim.1999.4781 }}
The deletion of this gene has been reported associated with Wilms tumor.<ref name="pmid9690521">{{cite journal | vauthors = Grundy RG, Pritchard J, Scambler P, Cowell JK | title = Loss of heterozygosity for the short arm of chromosome 7 in sporadic Wilms tumour | journal = Oncogene | volume = 17 | issue = 3 | pages = 395–400 | date = July 1998 | pmid = 9690521 | doi = 10.1038/sj.onc.1201927 }}</ref> [[Genome-wide association study|GWAS]] show that genetic variations of the CPVL gene are associated with susceptibility to diabetic [[nephropathy]] in European Americans, Japanese and Chinese.<ref name="pmid20460425">{{cite journal | vauthors = 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 | title = 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 | journal = Diabetes | volume = 59 | issue = 8 | pages = 2075–9 | date = August 2010 | pmid = 20460425 | doi = 10.2337/db10-0067 | pmc=2911071}}</ref><ref name="pmid21911749">{{cite journal | vauthors = Hu C, Zhang R, Yu W, Wang J, Wang C, Pang C, Ma X, Bao Y, Xiang K, Jia W | title = CPVL/CHN2 genetic variant is associated with diabetic retinopathy in Chinese type 2 diabetic patients | journal = Diabetes | volume = 60 | issue = 11 | pages = 3085–9 | date = November 2011 | pmid = 21911749 | doi = 10.2337/db11-0028 | pmc=3198055}}</ref><ref name="pmid21127830">{{cite journal | vauthors = Mooyaart AL, Valk EJ, van Es LA, Bruijn JA, de Heer E, Freedman BI, Dekkers OM, Baelde HJ | title = Genetic associations in diabetic nephropathy: a meta-analysis | journal = Diabetologia | volume = 54 | issue = 3 | pages = 544–53 | date = March 2011 | pmid = 21127830 | doi = 10.1007/s00125-010-1996-1 | pmc=3034040}}</ref> 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.<ref name="omid27211554">{{cite journal | vauthors = 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 | title = A Transcriptomic Biomarker to Quantify Systemic Inflammation in Sepsis - A Prospective Multicenter Phase II Diagnostic Study | journal = EBioMedicine | volume = 6 | pages = 114–25 | date = April 2016 | pmid = 27211554 | doi = 10.1016/j.ebiom.2016.03.006 | pmc=4856796}}</ref>
*{{cite journal | author=Ignatovich O, Tomlinson IM, Popov AV, ''et al.'' |title=Dominance of intrinsic genetic factors in shaping the human immunoglobulin Vlambda repertoire. |journal=J. Mol. Biol. |volume=294 |issue= 2 |pages= 457-65 |year= 2000 |pmid= 10610771 |doi= 10.1006/jmbi.1999.3243 }}
 
*{{cite journal | author=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi= }}
== References ==
*{{cite journal | author=Mahoney JA, Ntolosi B, DaSilva RP, ''et al.'' |title=Cloning and characterization of CPVL, a novel serine carboxypeptidase, from human macrophages. |journal=Genomics |volume=72 |issue= 3 |pages= 243-51 |year= 2001 |pmid= 11401439 |doi= 10.1006/geno.2000.6484 }}
{{reflist|33em}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
 
*{{cite journal  | author=Scherer SW, Cheung J, MacDonald JR, ''et al.'' |title=Human chromosome 7: DNA sequence and biology. |journal=Science |volume=300 |issue= 5620 |pages= 767-72 |year= 2003 |pmid= 12690205 |doi= 10.1126/science.1083423 }}
==External links==
*{{cite journal  | author=Hillier LW, Fulton RS, Fulton LA, ''et al.'' |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157-64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
* {{UCSC gene info|CPVL}}
*{{cite journal  | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
 
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
== Further reading ==
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
{{refbegin|33em}}
*{{cite journal  | author=Otsuki T, Ota T, Nishikawa T, ''et al.'' |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117-26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117 }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
}}
* {{cite journal | vauthors = Striebich CC, Falta MT, Wang Y, Bill J, Kotzin BL | title = Selective accumulation of related CD4+ T cell clones in the synovial fluid of patients with rheumatoid arthritis | journal = Journal of Immunology | volume = 161 | issue = 8 | pages = 4428–36 | date = October 1998 | pmid = 9780222 | doi =  }}
* {{cite journal | vauthors = Wang X, Stollar BD | title = Immunoglobulin VH gene expression in human aging | journal = Clinical Immunology | volume = 93 | issue = 2 | pages = 132–42 | date = November 1999 | pmid = 10527689 | doi = 10.1006/clim.1999.4781 }}
* {{cite journal | vauthors = Ignatovich O, Tomlinson IM, Popov AV, Brüggemann M, Winter G | title = Dominance of intrinsic genetic factors in shaping the human immunoglobulin Vlambda repertoire | journal = Journal of Molecular Biology | volume = 294 | issue = 2 | pages = 457–65 | date = November 1999 | pmid = 10610771 | doi = 10.1006/jmbi.1999.3243 }}
* {{cite journal | vauthors = Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z | title = Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells | journal = Genome Research | volume = 10 | issue = 10 | pages = 1546–60 | date = October 2000 | pmid = 11042152 | pmc = 310934 | doi = 10.1101/gr.140200 }}
* {{cite journal | vauthors = Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A | title = The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment | journal = Genome Research | volume = 13 | issue = 10 | pages = 2265–70 | date = October 2003 | pmid = 12975309 | pmc = 403697 | doi = 10.1101/gr.1293003 }}
* {{cite journal | vauthors = Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T | title = Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries | journal = DNA Research | volume = 12 | issue = 2 | pages = 117–26 | year = 2007 | pmid = 16303743 | doi = 10.1093/dnares/12.2.117 }}
* {{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
{{refend}}
{{refend}}


{{protein-stub}}
 
{{WikiDoc Sources}}
{{gene-7-stub}}

Latest revision as of 02:30, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Probable serine carboxypeptidase CPVL is an enzyme that in humans is encoded by the CPVL gene.[1][2] The "CPVL" gene is expressed mainly in monocytes and macrophages,[1] 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.[3] 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.[4] The exact function of this protein, however, has not been determined.

Structure

Gene

"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.[2]

Protein

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.[3]

Function

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.[3] 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.[1]

Clinical significance

The deletion of this gene has been reported associated with Wilms tumor.[5] GWAS show that genetic variations of the CPVL gene are associated with susceptibility to diabetic nephropathy in European Americans, Japanese and Chinese.[6][7][8] 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.[9]

References

  1. 1.0 1.1 1.2 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.
  2. 2.0 2.1 "Entrez Gene: CPVL carboxypeptidase, vitellogenic-like".
  3. 3.0 3.1 3.2 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 2517344. PMID 16436111.
  4. 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.
  5. 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.
  6. 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 2911071. PMID 20460425.
  7. 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 3198055. PMID 21911749.
  8. 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 3034040. PMID 21127830.
  9. 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 4856796. PMID 27211554.

External links

Further reading