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EFEMP1 (EGF containing fibulin-like extracellular matrix protein 1)

Identity

Other namesDHRD
DRAD
FBLN3
FBNL
FIBL-3
MLVT
MTLV
S1-5
HGNC (Hugo) EFEMP1
LocusID (NCBI) 2202
Location 2p16.1
Location_base_pair Starts at 56093097 and ends at 56151298 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

 
  Figure 1. A. Three transcripts were reported in Genebank for variant 1 (NM_004105), variant 2 (NM_001039348), and variant 3 (NM_001039349). NM_004105 has been permanently suppressed because currently there is insufficient support for the transcript. Variant 3 originates from alternative splicing of exon 2 in variant 2. B. Primers used to detect methylation of EFEMP1 promoter in cancer. C. EFEMP1 proximal promoter and sequence upstream of translation start site. Three SP1-binding sites and an estrogen response element (ERE) binding site are underscored, CG residues are marked in green, exons in uppercase, and MSP/BGS primer locations in boldface with sequences shown in B.
Transcription The EFEMP1 coding region extends over a genomic interval of 56485 bp and comprises 10 exons. EFEMP1 proximal promoter lacks TATA or CAAT regulatory boxes and is rich with CG residues. EFEMP1 expression is repressed by promoter methylation in several cancer types and cancer cell lines. Primers used to detect EFEMP1 promoter methylation are show in figures 1B and 1C.

Protein

Note The two transcription variants encode the same EFEMP1 protein of 493-amino acids with a molecular mass of ~ 55 kDa. Consecutive exons from 4 to 9 encode tandem arrays of epidermal growth-factor (EGF)-like domains. There is no EFEMP1 ortholog in non-mammalian species, indicating its recent evolution in higher vertebrates with intragenic exon duplications. There are 92-94% similarity at protein level among EFEMP1 of human, rat and mouse.
 
  Figure 2. Domain structures of EFEMP1 and modular gene structure for EGF-like domains based on variant 2. DSL, Delta-Serrate-Lag (DSL) motif is a motif unique to Delta/Serrate/LAG-2 proteins in addition to repeated copies of EGF motif (Lissemore and Starmer, 1999).
Description EFEMP1 belongs to seven-member family of secreted glycoproteins characterized by a N-terminal signal peptide, a tandem repeat of EGF-like domains and a unique C-terminal fibulin-type module.
Expression EFEMP1 is broadly expressed throughout the body during development and in adult tissues. It is highly expressed by epithelial and endothelial cells.
Localisation Extracellular matrix.
Function EFEMP1 is one member of fibulins that serve to modulate cellular behavior and functions by connecting and integrating multiple partner molecules in extracellular compartment. EFEMP1 is likely to contribute the integrity of basement membrane zones and anchor other extracellular matrix structures such as elastic fibers to basement membranes. Studies based on Efemp1 knock-out mouse implicate EFEMP1 function in withholding tissue integrity by stimulating the expression of Timp1 and Timp3 and inhibiting the expression and activities of matrix metalloproteinase Mmp2, and Mmp9 (Rahn et al., 2009). EFEMP1 interacts with TIMP3 (Klenotic et al., 2004) and hepatitis B virus X antigen (Sun et al., 1998). EFEMP1 suppresses endothelial cell spouting and antagonizes angiogenesis in vivo (Albig et al., 2006). EFEMP1 interacts with EGFR (Camaj et al., 2009). However, opposing effects from EFEMP1 on EGFR-AKT signaling activity were reported in different cancer cells, to promote (Camaj et al., 2009) or suppress (Hu et al., 2011; Hwang et al., 2010; Kim et al., 2012) cancer cell migration/invasion and/or in vivo tumor growth. A Delta-Serrate-Lag motif in EGF-like module with insertion has been revealed to be responsible for EFEMP1-mediated activation of Notch signaling in glioma cells (Hu et al., 2012).
Homology EFEMP1 shares homology with the other members of fibulin family on (EGF)-like domains and fibulin-type module.

Mutations

Germinal A single mutation of EFEMP1 gene at R345W was identified in patients with Malattia Leventinese (ML) and Doyne honeycombe retinal dystrophy (DHRD) (Stone et al., 1999). Severe atropy of the retina was observed in patients with this mutation, including absence of photoreceptor and RPE cells, and large fibrous scars in the macular region. This mutation was reported to cause protein misfolding, so that it is secreted inefficiently and retained within cells (Marmorstein et al., 2002). Comparison of pathological features of Efemp1 knockout and R345W knock-in mice suggests R345W mutation in causing macular degeneration is not due to loss of EFEMP1, so it is likely that the mutation has an added detrimental effect that alters Bruch's membrane to a greater extent than other structures (Fu et al., 2007; McLaughlin et al., 2007).

Implicated in

Entity Brain cancer
Note EFEMP1 was found to be highly expressed in malignant gliomas and in glioma cells with activation of Notch signaling (Hu et al., 2012; Hu et al., 2009). However, EFEMP1 expression is positively associated with survival of patients with the highest grade of glioma - glioblastoma multiforme (GBM) and consistently, EFEMP1 was shown to suppress highly proliferative GBM cell growth in vivo by attenuation of EGFR-AKT signaling activities and VEGFA-induced angiogenesis (Hu et al., 2011). Along with activation of Notch pathway, EFEMP1 was shown to enhance migration/invasion and growth in vivo by glioma cells high in Notch signaling and stem-like feature (Hu et al., 2012). The contradictory roles of EFEMP1 to the growth of different glioma cells suggest EFEMP1 context-dependent function, thus could be an interesting gene to study glioma initiation, progression and tumor heterogeneity.
  
Entity Breast cancer
Note Hypermethylation of EFEMP1 promoter was found to be the major cause of EFEMP1 expression down-regulation in 50-60% sporadic breast cancer (SBC). Tumor suppressive function of EFEMP1 is implicated in SBC by a favorable prognosis effect of EFEMP1 expression to survival, particularly node-positive patients who received adjuvant anthracycline-based chemotherapy, but not in those treated by either cyclophosphamide-methotrexate-5-fluorouracil (CMF) or tamoxifen (Sadr-Nabavi et al., 2009).
  
Entity Cervical cancer
Note EFEMP1 protein expression was found to be significantly higher in cervical carcinoma with lymph node metastasis and correlates with poor patient survival (En-lin et al., 2010). Tumor-promoting effect of EFEMP1 in cervical cancer is supported by its function in promoting growth in vivo and in vitro invasion by cervical cancer cell line Hela (Song et al., 2011).
  
Entity Colorectal cancer
Note Hypermethylation of EFEMP1 promoter was reported in 38,8% colorectal cancer (CRC), which is correlated with downregulation of EFEMP1 expression and cancer progression to advanced pathological stage with lymph node metastasis. Tumor suppressive function of EFEMP1 is implicated in CRC by a favorable prognosis effect of EFEMP1 expression to overall survival and disease-free survival (Tong et al., 2011).
  
Entity Liver cancer
Note Hypermethylation of EFEMP1 promoter was reported in 50% hepatocellular carcinoma (HCC), which is correlated with downregulation of EFEMP1 expression. Tumor suppressive function of EFEMP1 is implicated in liver cancer by unfavorable prognosis from promoter methylation of EFEMP1 (Nomoto et al., 2010).
  
Entity Lung cancer
Note Hypermethylation of EFEMP1 promoter was independently reported by two laboratories in 36% and 43% of non-small cell lung carcinoma (NSCLC), while it was rarely found in the matched normal samples (Wang et al., 2010; Yue et al., 2007; Zhang et al., 2011). It is correlated with downregulation of EFEMP1 expression and cancer progression to advanced pathological stage and lymph node metastasis. Tumor suppressive function of EFEMP1 in lung cancer cell is demonstrated by its suppression effect on anchorage independent growth and in vitro invasion via suppression the expression of matrix metalloproteinase, including MMP2, MMP7, and MMP9 (Kim et al., 2012).
  
Entity Nasopharyngeal carcinoma
Note Hypermethylation of EFEMP1 promoter has been revealed in nasopharyngeal carcinoma (NPC) tumours compared with normal tissues. Downregulation of EFEMP1 expression was found in NPC at advanced lymph node-metastasis stages and a poor 5-year survival rate. Tumor suppressive function of EFEMP1 in NPC is revealed by suppressing migration and invasion of NPC-derived cells and correspondingly decreasing the AKT phosphorylation (Hwang et al., 2010).
  
Entity Pancreatic cancer
Note EFEMP1 was reported to bind EGFR and activate MAPK and AKT pathways in pancreatic carcinoma cells and promote in vivo tumor growth with a stimulation of VEGFA production by tumors (Camaj et al., 2009; Seeliger et al., 2009).
  
Entity Prostate cancer
Note Hypermethylation of EFEMP1 promoter was reported in 95,3% of prostate cancer (PCa) but 13,4% of benign prostate hyperplasia (BPH), and EFEMP1 expression was significantly higher in tissue samples from patients with BPH than in those with PCa (Kim et al., 2011).
  
Entity Werner syndrome
Note S1-5 mRNA is overexpressed in Werner syndrome and senescent human diploid fibroblasts (Lecka-Czernik et al., 1995).
  
Entity Adult height
Note The EFEMP1 locus is one of 20 loci identified in a genome-wide association analysis that influence adult height (Okada et al., 2010).
  

External links

Nomenclature
HGNC (Hugo)EFEMP1   3218
Cards
AtlasEFEMP1ID49818ch2p16
Entrez_Gene (NCBI)EFEMP1  2202  EGF containing fibulin-like extracellular matrix protein 1
GeneCards (Weizmann)EFEMP1
Ensembl (Hinxton)ENSG00000115380 [Gene_View]  chr2:56093097-56151298 [Contig_View]  EFEMP1 [Vega]
ICGC DataPortalENSG00000115380
AceView (NCBI)EFEMP1
Genatlas (Paris)EFEMP1
WikiGenes2202
SOURCE (Princeton)NM_001039348 NM_001039349 NM_004105
Genomic and cartography
GoldenPath (UCSC)EFEMP1  -  2p16.1   chr2:56093097-56151298 -  2p16   [Description]    (hg19-Feb_2009)
EnsemblEFEMP1 - 2p16 [CytoView]
Mapping of homologs : NCBIEFEMP1 [Mapview]
OMIM126600   601548   
Gene and transcription
Genbank (Entrez)AA704122 AB209212 AI472137 AK092854 AK290599
RefSeq transcript (Entrez)NM_001039348 NM_001039349 NM_004105
RefSeq genomic (Entrez)AC_000134 NC_000002 NC_018913 NG_009098 NT_022184 NW_001838769 NW_004929300
Consensus coding sequences : CCDS (NCBI)EFEMP1
Cluster EST : UnigeneHs.732348 [ NCBI ]
CGAP (NCI)Hs.732348
Alternative Splicing : Fast-db (Paris)GSHG0017633
Alternative Splicing GalleryENSG00000115380
Gene ExpressionEFEMP1 [ NCBI-GEO ]     EFEMP1 [ SEEK ]   EFEMP1 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ12805 (Uniprot)
NextProtQ12805  [Medical]
With graphics : InterProQ12805
Splice isoforms : SwissVarQ12805 (Swissvar)
Domaine pattern : Prosite (Expaxy)ASX_HYDROXYL (PS00010)    EGF_2 (PS01186)    EGF_3 (PS50026)    EGF_CA (PS01187)   
Domains : Interpro (EBI)cEGF    EG-like_dom    EGF-like_Ca-bd_dom    EGF-like_CS    EGF-type_Asp/Asn_hydroxyl_site    EGF_Ca-bd_CS    Growth_fac_rcpt_N_dom   
Related proteins : CluSTrQ12805
Domain families : Pfam (Sanger)cEGF (PF12662)    EGF_CA (PF07645)   
Domain families : Pfam (NCBI)pfam12662    pfam07645   
Domain families : Smart (EMBL)EGF_CA (SM00179)  
DMDM Disease mutations2202
Blocks (Seattle)Q12805
Human Protein AtlasENSG00000115380
Peptide AtlasQ12805
HPRD03331
IPIIPI00029658   IPI00220813   IPI00220814   IPI00220815   IPI00922935   IPI00908496   IPI00893769   IPI00893517   IPI00894009   IPI00894125   IPI00894239   IPI00894374   IPI00894496   
Protein Interaction databases
DIP (DOE-UCLA)Q12805
IntAct (EBI)Q12805
FunCoupENSG00000115380
BioGRIDEFEMP1
IntegromeDBEFEMP1
STRING (EMBL)EFEMP1
Ontologies - Pathways
QuickGOQ12805
Ontology : AmiGOepidermal growth factor-activated receptor activity  epidermal growth factor receptor binding  calcium ion binding  protein binding  extracellular region  proteinaceous extracellular matrix  extracellular space  regulation of transcription, DNA-templated  epidermal growth factor receptor signaling pathway  visual perception  growth factor activity  peptidyl-tyrosine phosphorylation  extracellular matrix organization  extracellular matrix  negative regulation of chondrocyte differentiation  extracellular vesicular exosome  
Ontology : EGO-EBIepidermal growth factor-activated receptor activity  epidermal growth factor receptor binding  calcium ion binding  protein binding  extracellular region  proteinaceous extracellular matrix  extracellular space  regulation of transcription, DNA-templated  epidermal growth factor receptor signaling pathway  visual perception  growth factor activity  peptidyl-tyrosine phosphorylation  extracellular matrix organization  extracellular matrix  negative regulation of chondrocyte differentiation  extracellular vesicular exosome  
REACTOMEQ12805 [protein]
REACTOME PathwaysREACT_118779 Extracellular matrix organization [pathway]
Protein Interaction DatabaseEFEMP1
Wikipedia pathwaysEFEMP1
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)EFEMP1
SNP (GeneSNP Utah)EFEMP1
SNP : HGBaseEFEMP1
Genetic variants : HAPMAPEFEMP1
1000_GenomesEFEMP1 
ICGC programENSG00000115380 
CONAN: Copy Number AnalysisEFEMP1 
Somatic Mutations in Cancer : COSMICEFEMP1 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
LOVD (Leiden Open Variation Database)Eye diseases - LOVD
DECIPHER (Syndromes)2:56093097-56151298
Mutations and Diseases : HGMDEFEMP1
OMIM126600    601548   
MedgenEFEMP1
GENETestsEFEMP1
Disease Genetic AssociationEFEMP1
Huge Navigator EFEMP1 [HugePedia]  EFEMP1 [HugeCancerGEM]
Genomic VariantsEFEMP1  EFEMP1 [DGVbeta]
Exome VariantEFEMP1
dbVarEFEMP1
ClinVarEFEMP1
snp3D : Map Gene to Disease2202
General knowledge
Homologs : HomoloGeneEFEMP1
Homology/Alignments : Family Browser (UCSC)EFEMP1
Phylogenetic Trees/Animal Genes : TreeFamEFEMP1
Chemical/Protein Interactions : CTD2202
Chemical/Pharm GKB GenePA27652
Clinical trialEFEMP1
Cancer Resource (Charite)ENSG00000115380
Other databases
Probes
Litterature
PubMed80 Pubmed reference(s) in Entrez
CoreMineEFEMP1
GoPubMedEFEMP1
iHOPEFEMP1

Bibliography

An overexpressed gene transcript in senescent and quiescent human fibroblasts encoding a novel protein in the epidermal growth factor-like repeat family stimulates DNA synthesis.
Lecka-Czernik B, Lumpkin CK Jr, Goldstein S.
Mol Cell Biol. 1995 Jan;15(1):120-8.
PMID 7799918
 
Identification of a protein isolated from senescent human cells that binds to hepatitis B virus X antigen.
Sun BS, Zhu X, Clayton MM, Pan J, Feitelson MA.
Hepatology. 1998 Jan;27(1):228-39.
PMID 9425942
 
Phylogenetic analysis of vertebrate and invertebrate Delta/Serrate/LAG-2 (DSL) proteins.
Lissemore JL, Starmer WT.
Mol Phylogenet Evol. 1999 Mar;11(2):308-19.
PMID 10191075
 
A single EFEMP1 mutation associated with both Malattia Leventinese and Doyne honeycomb retinal dystrophy.
Stone EM, Lotery AJ, Munier FL, Heon E, Piguet B, Guymer RH, Vandenburgh K, Cousin P, Nishimura D, Swiderski RE, Silvestri G, Mackey DA, Hageman GS, Bird AC, Sheffield VC, Schorderet DF.
Nat Genet. 1999 Jun;22(2):199-202.
PMID 10369267
 
Aberrant accumulation of EFEMP1 underlies drusen formation in Malattia Leventinese and age-related macular degeneration.
Marmorstein LY, Munier FL, Arsenijevic Y, Schorderet DF, McLaughlin PJ, Chung D, Traboulsi E, Marmorstein AD.
Proc Natl Acad Sci U S A. 2002 Oct 1;99(20):13067-72. Epub 2002 Sep 19.
PMID 12242346
 
Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a binding partner of epithelial growth factor-containing fibulin-like extracellular matrix protein 1 (EFEMP1). Implications for macular degenerations.
Klenotic PA, Munier FL, Marmorstein LY, Anand-Apte B.
J Biol Chem. 2004 Jul 16;279(29):30469-73. Epub 2004 Apr 28.
PMID 15123717
 
Fibulins 3 and 5 antagonize tumor angiogenesis in vivo.
Albig AR, Neil JR, Schiemann WP.
Cancer Res. 2006 Mar 1;66(5):2621-9.
PMID 16510581
 
The R345W mutation in EFEMP1 is pathogenic and causes AMD-like deposits in mice.
Fu L, Garland D, Yang Z, Shukla D, Rajendran A, Pearson E, Stone EM, Zhang K, Pierce EA.
Hum Mol Genet. 2007 Oct 15;16(20):2411-22. Epub 2007 Jul 30.
PMID 17666404
 
Lack of fibulin-3 causes early aging and herniation, but not macular degeneration in mice.
McLaughlin PJ, Bakall B, Choi J, Liu Z, Sasaki T, Davis EC, Marmorstein AD, Marmorstein LY.
Hum Mol Genet. 2007 Dec 15;16(24):3059-70. Epub 2007 Sep 13.
PMID 17872905
 
Frequent inactivation of RAMP2, EFEMP1 and Dutt1 in lung cancer by promoter hypermethylation.
Yue W, Dacic S, Sun Q, Landreneau R, Guo M, Zhou W, Siegfried JM, Yu J, Zhang L.
Clin Cancer Res. 2007 Aug 1;13(15 Pt 1):4336-44.
PMID 17671114
 
EFEMP1 binds the EGF receptor and activates MAPK and Akt pathways in pancreatic carcinoma cells.
Camaj P, Seeliger H, Ischenko I, Krebs S, Blum H, De Toni EN, Faktorova D, Jauch KW, Bruns CJ.
Biol Chem. 2009 Dec;390(12):1293-302.
PMID 19804359
 
Fibulin-3 is uniquely upregulated in malignant gliomas and promotes tumor cell motility and invasion.
Hu B, Thirtamara-Rajamani KK, Sim H, Viapiano MS.
Mol Cancer Res. 2009 Nov;7(11):1756-70. Epub 2009 Nov 3.
PMID 19887559
 
Failure of pelvic organ support in mice deficient in fibulin-3.
Rahn DD, Acevedo JF, Roshanravan S, Keller PW, Davis EC, Marmorstein LY, Word RA.
Am J Pathol. 2009 Jan;174(1):206-15. Epub 2008 Dec 18.
PMID 19095964
 
Decreased expression of angiogenesis antagonist EFEMP1 in sporadic breast cancer is caused by aberrant promoter methylation and points to an impact of EFEMP1 as molecular biomarker.
Sadr-Nabavi A, Ramser J, Volkmann J, Naehrig J, Wiesmann F, Betz B, Hellebrand H, Engert S, Seitz S, Kreutzfeld R, Sasaki T, Arnold N, Schmutzler R, Kiechle M, Niederacher D, Harbeck N, Dahl E, Meindl A.
Int J Cancer. 2009 Apr 1;124(7):1727-35.
PMID 19115204
 
EFEMP1 expression promotes in vivo tumor growth in human pancreatic adenocarcinoma.
Seeliger H, Camaj P, Ischenko I, Kleespies A, De Toni EN, Thieme SE, Blum H, Assmann G, Jauch KW, Bruns CJ.
Mol Cancer Res. 2009 Feb;7(2):189-98. Epub 2009 Feb 10.
PMID 19208748
 
The expression of EFEMP1 in cervical carcinoma and its relationship with prognosis.
En-lin S, Sheng-guo C, Hua-qiao W.
Gynecol Oncol. 2010 Jun;117(3):417-22. Epub 2010 Apr 7.
PMID 20378157
 
Fibulin-3 is associated with tumour progression and a poor prognosis in nasopharyngeal carcinomas and inhibits cell migration and invasion via suppressed AKT activity.
Hwang CF, Chien CY, Huang SC, Yin YF, Huang CC, Fang FM, Tsai HT, Su LJ, Chen CH.
J Pathol. 2010 Dec;222(4):367-79.
PMID 20927779
 
Epidermal growth factor-containing fibulin-like extracellular matrix protein 1, EFEMP1, a novel tumor-suppressor gene detected in hepatocellular carcinoma using double combination array analysis.
Nomoto S, Kanda M, Okamura Y, Nishikawa Y, Qiyong L, Fujii T, Sugimoto H, Takeda S, Nakao A.
Ann Surg Oncol. 2010 Mar;17(3):923-32. Epub 2009 Nov 7.
PMID 19898900
 
A genome-wide association study in 19 633 Japanese subjects identified LHX3-QSOX2 and IGF1 as adult height loci.
Okada Y, Kamatani Y, Takahashi A, Matsuda K, Hosono N, Ohmiya H, Daigo Y, Yamamoto K, Kubo M, Nakamura Y, Kamatani N.
Hum Mol Genet. 2010 Jun 1;19(11):2303-12. Epub 2010 Feb 26.
PMID 20189936
 
Aberrant promoter methylation of FBLN-3 gene and clinicopathological significance in non-small cell lung carcinoma.
Wang R, Zhang YW, Chen LB.
Lung Cancer. 2010 Aug;69(2):239-44. Epub 2009 Nov 12.
PMID 19913326
 
EFEMP1 suppresses malignant glioma growth and exerts its action within the tumor extracellular compartment.
Hu Y, Pioli PD, Siegel E, Zhang Q, Nelson J, Chaturbedi A, Mathews MS, Ro DI, Alkafeef S, Hsu N, Hamamura M, Yu L, Hess KR, Tromberg BJ, Linskey ME, Zhou YH.
Mol Cancer. 2011 Sep 28;10:123.
PMID 21955618
 
EFEMP1 as a novel DNA methylation marker for prostate cancer: array-based DNA methylation and expression profiling.
Kim YJ, Yoon HY, Kim SK, Kim YW, Kim EJ, Kim IY, Kim WJ.
Clin Cancer Res. 2011 Jul 1;17(13):4523-30. Epub 2011 May 13.
PMID 21571867
 
EFEMP1 expression promotes angiogenesis and accelerates the growth of cervical cancer in vivo.
Song EL, Hou YP, Yu SP, Chen SG, Huang JT, Luo T, Kong LP, Xu J, Wang HQ.
Gynecol Oncol. 2011 Apr;121(1):174-80. Epub 2010 Dec 15.
PMID 21163514
 
Downregulation of fibulin-3 gene by promoter methylation in colorectal cancer predicts adverse prognosis.
Tong JD, Jiao NL, Wang YX, Zhang YW, Han F.
Neoplasma. 2011;58(5):441-8.
PMID 21744999
 
Methylation of multiple genes as a candidate biomarker in non-small cell lung cancer.
Zhang Y, Wang R, Song H, Huang G, Yi J, Zheng Y, Wang J, Chen L.
Cancer Lett. 2011 Apr 1;303(1):21-8. Epub 2011 Jan 20.
PMID 21255913
 
Fibulin-3 promotes glioma growth and resistance through a novel paracrine regulation of Notch signaling.
Hu B, Nandhu MS, Sim H, Agudelo-Garcia PA, Saldivar JC, Dolan CE, Mora ME, Nuovo GJ, Cole SE, Viapiano MS.
Cancer Res. 2012 Aug 1;72(15):3873-85. doi: 10.1158/0008-5472.CAN-12-1060. Epub 2012 Jun 4.
PMID 22665268
 
Fibulin-3 promoter methylation alters the invasive behavior of non-small cell lung cancer cell lines via MMP-7 and MMP-2 regulation.
Kim EJ, Lee SY, Woo MK, Choi SI, Kim TR, Kim MJ, Kim KC, Cho EW, Kim IG.
Int J Oncol. 2012 Feb;40(2):402-8. doi: 10.3892/ijo.2011.1191. Epub 2011 Sep 7.
PMID 21901248
 
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Contributor(s)

Written09-2012Yi-Hong Zhou
The University of California, Irvine, USA

Citation

This paper should be referenced as such :
Zhou, YH
EFEMP1 (EGF containing fibulin-like extracellular matrix protein 1)
Atlas Genet Cytogenet Oncol Haematol. 2013;17(2):115-120.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/EFEMP1ID49818ch2p16.html

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