Full text data of POSTN
POSTN
(OSF2)
[Confidence: low (only semi-automatic identification from reviews)]
Periostin; PN (Osteoblast-specific factor 2; OSF-2; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Periostin; PN (Osteoblast-specific factor 2; OSF-2; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15063
ID POSTN_HUMAN Reviewed; 836 AA.
AC Q15063; Q15064; Q29XZ0; Q3KPJ5; Q5VSY5; Q8IZF9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-MAR-2006, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Periostin;
DE Short=PN;
DE AltName: Full=Osteoblast-specific factor 2;
DE Short=OSF-2;
DE Flags: Precursor;
GN Name=POSTN; Synonyms=OSF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Osteosarcoma, and Placenta;
RX PubMed=8363580;
RA Takeshita S., Kikuno R., Tezuka K., Amann E.;
RT "Osteoblast-specific factor 2: cloning of a putative bone adhesion
RT protein with homology with the insect protein fasciclin I.";
RL Biochem. J. 294:271-278(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12235007;
RA Gillan L., Matei D., Fishman D.A., Gerbin C.S., Karlan B.Y.,
RA Chang D.D.;
RT "Periostin secreted by epithelial ovarian carcinoma is a ligand for
RT alpha(V)beta(3) and alpha(V)beta(5) integrins and promotes cell
RT motility.";
RL Cancer Res. 62:5358-5364(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Periodontal ligament;
RA Yamada S., Maeda K., Matsubara K., Murakami S.;
RT "Identification and characterization of a novel periodontal ligament-
RT specific periostin isoform.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11550156;
RX DOI=10.1002/1097-0142(20010815)92:4<843::AID-CNCR1391>3.0.CO;2-P;
RA Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y.,
RA Fujii Y., Chen L.B.;
RT "Serum level of the periostin, a homologue of an insect cell adhesion
RT molecule, as a prognostic marker in nonsmall cell lung carcinomas.";
RL Cancer 92:843-848(2001).
RN [8]
RP ERRATUM.
RA Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y.,
RA Fujii Y., Chen L.B.;
RL Cancer 95:2580-2580(2002).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=15082792; DOI=10.1128/MCB.24.9.3992-4003.2004;
RA Shao R., Bao S., Bai X., Blanchette C., Anderson R.M., Dang T.,
RA Gishizky M.L., Marks J.R., Wang X.-F.;
RT "Acquired expression of periostin by human breast cancers promotes
RT tumor angiogenesis through up-regulation of vascular endothelial
RT growth factor receptor 2 expression.";
RL Mol. Cell. Biol. 24:3992-4003(2004).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599, AND MASS
RP SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP FUNCTION, AND GAMMA-CARBOXYGLUTAMATION.
RX PubMed=18450759; DOI=10.1074/jbc.M708029200;
RA Coutu D.L., Wu J.H., Monette A., Rivard G.-E., Blostein M.D.,
RA Galipeau J.;
RT "Periostin, a member of a novel family of vitamin K-dependent
RT proteins, is expressed by mesenchymal stromal cells.";
RL J. Biol. Chem. 283:17991-18001(2008).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: Enhances incorporation of BMP1 in the fibronectin matrix
CC of connective tissues, and subsequent proteolytic activation of
CC lysyl oxidase LOX (By similarity). Induces cell attachment and
CC spreading and plays a role in cell adhesion. May play a role in
CC extracellular matrix mineralization.
CC -!- SUBUNIT: Interacts with BMP1 and fibronectin (By similarity).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus (By similarity). Secreted,
CC extracellular space, extracellular matrix. Note=Colocalizes with
CC BMP1 in the Golgi (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=OSF-2OS;
CC IsoId=Q15063-1; Sequence=Displayed;
CC Name=2; Synonyms=OSF-2p1;
CC IsoId=Q15063-2; Sequence=VSP_050005;
CC Name=3;
CC IsoId=Q15063-3; Sequence=VSP_050669, VSP_050670;
CC Name=4;
CC IsoId=Q15063-4; Sequence=VSP_050005, VSP_050670;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in aorta,
CC stomach, lower gastrointestinal tract, placenta, uterus and
CC breast. Up-regulated in epithelial ovarian tumors. Not expressed
CC in normal ovaries. Also highly expressed at the tumor periphery of
CC lung carcinoma tissue but not within the tumor. Overexpressed in
CC breast cancers.
CC -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K
CC dependent carboxylation. These residues are essential for the
CC binding of calcium.
CC -!- SIMILARITY: Contains 1 EMI domain.
CC -!- SIMILARITY: Contains 4 FAS1 domains.
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DR EMBL; D13665; BAA02836.1; -; mRNA.
DR EMBL; D13666; BAA02837.1; -; mRNA.
DR EMBL; AY140646; AAN17733.1; -; mRNA.
DR EMBL; AY918092; AAY15840.1; -; mRNA.
DR EMBL; AL138679; CAH70107.1; -; Genomic_DNA.
DR EMBL; AL646087; CAH70107.1; JOINED; Genomic_DNA.
DR EMBL; AL646087; CAH73568.1; -; Genomic_DNA.
DR EMBL; AL138679; CAH73568.1; JOINED; Genomic_DNA.
DR EMBL; AL138679; CAH70104.1; -; Genomic_DNA.
DR EMBL; AL646087; CAH70104.1; JOINED; Genomic_DNA.
DR EMBL; AL646087; CAH73569.1; -; Genomic_DNA.
DR EMBL; AL138679; CAH73569.1; JOINED; Genomic_DNA.
DR EMBL; CH471075; EAX08590.1; -; Genomic_DNA.
DR EMBL; BC106709; AAI06710.1; -; mRNA.
DR EMBL; BC106710; AAI06711.1; -; mRNA.
DR PIR; S36110; S36110.
DR PIR; S36111; S36111.
DR RefSeq; NP_001129406.1; NM_001135934.1.
DR RefSeq; NP_001129407.1; NM_001135935.1.
DR RefSeq; NP_001129408.1; NM_001135936.1.
DR RefSeq; NP_006466.2; NM_006475.2.
DR UniGene; Hs.136348; -.
DR UniGene; Hs.721018; -.
DR ProteinModelPortal; Q15063; -.
DR SMR; Q15063; 236-367, 503-628.
DR IntAct; Q15063; 2.
DR MINT; MINT-4533078; -.
DR STRING; 9606.ENSP00000369071; -.
DR PhosphoSite; Q15063; -.
DR DMDM; 93138709; -.
DR PaxDb; Q15063; -.
DR PRIDE; Q15063; -.
DR Ensembl; ENST00000379742; ENSP00000369066; ENSG00000133110.
DR Ensembl; ENST00000379747; ENSP00000369071; ENSG00000133110.
DR Ensembl; ENST00000541179; ENSP00000437959; ENSG00000133110.
DR GeneID; 10631; -.
DR KEGG; hsa:10631; -.
DR UCSC; uc001uwo.4; human.
DR CTD; 10631; -.
DR GeneCards; GC13M038136; -.
DR HGNC; HGNC:16953; POSTN.
DR HPA; HPA012306; -.
DR MIM; 608777; gene.
DR neXtProt; NX_Q15063; -.
DR PharmGKB; PA134900304; -.
DR eggNOG; COG2335; -.
DR HOGENOM; HOG000220865; -.
DR HOVERGEN; HBG000715; -.
DR InParanoid; Q15063; -.
DR OMA; HGEPIIK; -.
DR PhylomeDB; Q15063; -.
DR ChiTaRS; POSTN; human.
DR GeneWiki; Periostin; -.
DR GeneWiki; POSTN; -.
DR GenomeRNAi; 10631; -.
DR NextBio; 40399; -.
DR PRO; PR:Q15063; -.
DR ArrayExpress; Q15063; -.
DR Bgee; Q15063; -.
DR CleanEx; HS_POSTN; -.
DR Genevestigator; Q15063; -.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005578; C:proteinaceous extracellular matrix; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR GO; GO:0009888; P:tissue development; IEA:Ensembl.
DR Gene3D; 2.30.180.10; -; 4.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR016666; TGFb-ind_bIGH3/osteoblast_fac2.
DR Pfam; PF02469; Fasciclin; 4.
DR PIRSF; PIRSF016553; BIGH3_OSF2; 1.
DR SMART; SM00554; FAS1; 4.
DR SUPFAM; SSF82153; SSF82153; 4.
DR PROSITE; PS51041; EMI; 1.
DR PROSITE; PS50213; FAS1; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Complete proteome;
KW Disulfide bond; Extracellular matrix; Gamma-carboxyglutamic acid;
KW Glycoprotein; Golgi apparatus; Heparin-binding; Polymorphism;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 21 Potential.
FT CHAIN 22 836 Periostin.
FT /FTId=PRO_0000008789.
FT DOMAIN 40 94 EMI.
FT DOMAIN 97 230 FAS1 1.
FT DOMAIN 234 365 FAS1 2.
FT DOMAIN 368 492 FAS1 3.
FT DOMAIN 496 628 FAS1 4.
FT MOD_RES 124 124 4-carboxyglutamate (Potential).
FT MOD_RES 125 125 4-carboxyglutamate (Potential).
FT MOD_RES 127 127 4-carboxyglutamate (Potential).
FT MOD_RES 140 140 4-carboxyglutamate (Potential).
FT MOD_RES 154 154 4-carboxyglutamate (Potential).
FT MOD_RES 160 160 4-carboxyglutamate (Potential).
FT MOD_RES 242 242 4-carboxyglutamate (Potential).
FT MOD_RES 244 244 4-carboxyglutamate (Potential).
FT MOD_RES 261 261 4-carboxyglutamate (Potential).
FT MOD_RES 277 277 4-carboxyglutamate (Potential).
FT MOD_RES 280 280 4-carboxyglutamate (Potential).
FT MOD_RES 288 288 4-carboxyglutamate (Potential).
FT MOD_RES 298 298 4-carboxyglutamate (Potential).
FT MOD_RES 313 313 4-carboxyglutamate (Potential).
FT MOD_RES 322 322 4-carboxyglutamate (Potential).
FT MOD_RES 325 325 4-carboxyglutamate (Potential).
FT MOD_RES 496 496 4-carboxyglutamate (Potential).
FT MOD_RES 501 501 4-carboxyglutamate (Potential).
FT MOD_RES 517 517 4-carboxyglutamate (Potential).
FT MOD_RES 523 523 4-carboxyglutamate (Potential).
FT MOD_RES 547 547 4-carboxyglutamate (Potential).
FT MOD_RES 548 548 4-carboxyglutamate (Potential).
FT MOD_RES 550 550 4-carboxyglutamate (Potential).
FT MOD_RES 578 578 4-carboxyglutamate (Potential).
FT CARBOHYD 599 599 N-linked (GlcNAc...).
FT DISULFID 44 80 By similarity.
FT DISULFID 60 69 By similarity.
FT DISULFID 79 92 By similarity.
FT VAR_SEQ 670 727 TTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPE
FT FRLIKEGETITEVIHGE -> K (in isoform 2 and
FT isoform 4).
FT /FTId=VSP_050005.
FT VAR_SEQ 670 697 TTKIITKVVEPKIKVIEGSLQPIIKTEG -> R (in
FT isoform 3).
FT /FTId=VSP_050669.
FT VAR_SEQ 783 810 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_050670.
FT VARIANT 339 339 T -> I (in dbSNP:rs9594223).
FT /FTId=VAR_049115.
FT VARIANT 814 814 V -> M (in dbSNP:rs9547952).
FT /FTId=VAR_049116.
FT CONFLICT 290 290 I -> F (in Ref. 1; BAA02836/BAA02837 and
FT 3; AAY15840).
FT CONFLICT 421 421 D -> V (in Ref. 1; BAA02836/BAA02837 and
FT 3; AAY15840).
SQ SEQUENCE 836 AA; 93314 MW; 55E7B82D094824FD CRC64;
MIPFLPMFSL LLLLIVNPIN ANNHYDKILA HSRIRGRDQG PNVCALQQIL GTKKKYFSTC
KNWYKKSICG QKTTVLYECC PGYMRMEGMK GCPAVLPIDH VYGTLGIVGA TTTQRYSDAS
KLREEIEGKG SFTYFAPSNE AWDNLDSDIR RGLESNVNVE LLNALHSHMI NKRMLTKDLK
NGMIIPSMYN NLGLFINHYP NGVVTVNCAR IIHGNQIATN GVVHVIDRVL TQIGTSIQDF
IEAEDDLSSF RAAAITSDIL EALGRDGHFT LFAPTNEAFE KLPRGVLERI MGDKVASEAL
MKYHILNTLQ CSESIMGGAV FETLEGNTIE IGCDGDSITV NGIKMVNKKD IVTNNGVIHL
IDQVLIPDSA KQVIELAGKQ QTTFTDLVAQ LGLASALRPD GEYTLLAPVN NAFSDDTLSM
DQRLLKLILQ NHILKVKVGL NELYNGQILE TIGGKQLRVF VYRTAVCIEN SCMEKGSKQG
RNGAIHIFRE IIKPAEKSLH EKLKQDKRFS TFLSLLEAAD LKELLTQPGD WTLFVPTNDA
FKGMTSEEKE ILIRDKNALQ NIILYHLTPG VFIGKGFEPG VTNILKTTQG SKIFLKEVND
TLLVNELKSK ESDIMTTNGV IHVVDKLLYP ADTPVGNDQL LEILNKLIKY IQIKFVRGST
FKEIPVTVYT TKIITKVVEP KIKVIEGSLQ PIIKTEGPTL TKVKIEGEPE FRLIKEGETI
TEVIHGEPII KKYTKIIDGV PVEITEKETR EERIITGPEI KYTRISTGGG ETEETLKKLL
QEEVTKVTKF IEGGDGHLFE DEEIKRLLQG DTPVRKLQAN KKVQGSRRRL REGRSQ
//
ID POSTN_HUMAN Reviewed; 836 AA.
AC Q15063; Q15064; Q29XZ0; Q3KPJ5; Q5VSY5; Q8IZF9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-MAR-2006, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Periostin;
DE Short=PN;
DE AltName: Full=Osteoblast-specific factor 2;
DE Short=OSF-2;
DE Flags: Precursor;
GN Name=POSTN; Synonyms=OSF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Osteosarcoma, and Placenta;
RX PubMed=8363580;
RA Takeshita S., Kikuno R., Tezuka K., Amann E.;
RT "Osteoblast-specific factor 2: cloning of a putative bone adhesion
RT protein with homology with the insect protein fasciclin I.";
RL Biochem. J. 294:271-278(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12235007;
RA Gillan L., Matei D., Fishman D.A., Gerbin C.S., Karlan B.Y.,
RA Chang D.D.;
RT "Periostin secreted by epithelial ovarian carcinoma is a ligand for
RT alpha(V)beta(3) and alpha(V)beta(5) integrins and promotes cell
RT motility.";
RL Cancer Res. 62:5358-5364(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Periodontal ligament;
RA Yamada S., Maeda K., Matsubara K., Murakami S.;
RT "Identification and characterization of a novel periodontal ligament-
RT specific periostin isoform.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11550156;
RX DOI=10.1002/1097-0142(20010815)92:4<843::AID-CNCR1391>3.0.CO;2-P;
RA Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y.,
RA Fujii Y., Chen L.B.;
RT "Serum level of the periostin, a homologue of an insect cell adhesion
RT molecule, as a prognostic marker in nonsmall cell lung carcinomas.";
RL Cancer 92:843-848(2001).
RN [8]
RP ERRATUM.
RA Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y.,
RA Fujii Y., Chen L.B.;
RL Cancer 95:2580-2580(2002).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=15082792; DOI=10.1128/MCB.24.9.3992-4003.2004;
RA Shao R., Bao S., Bai X., Blanchette C., Anderson R.M., Dang T.,
RA Gishizky M.L., Marks J.R., Wang X.-F.;
RT "Acquired expression of periostin by human breast cancers promotes
RT tumor angiogenesis through up-regulation of vascular endothelial
RT growth factor receptor 2 expression.";
RL Mol. Cell. Biol. 24:3992-4003(2004).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599, AND MASS
RP SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP FUNCTION, AND GAMMA-CARBOXYGLUTAMATION.
RX PubMed=18450759; DOI=10.1074/jbc.M708029200;
RA Coutu D.L., Wu J.H., Monette A., Rivard G.-E., Blostein M.D.,
RA Galipeau J.;
RT "Periostin, a member of a novel family of vitamin K-dependent
RT proteins, is expressed by mesenchymal stromal cells.";
RL J. Biol. Chem. 283:17991-18001(2008).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: Enhances incorporation of BMP1 in the fibronectin matrix
CC of connective tissues, and subsequent proteolytic activation of
CC lysyl oxidase LOX (By similarity). Induces cell attachment and
CC spreading and plays a role in cell adhesion. May play a role in
CC extracellular matrix mineralization.
CC -!- SUBUNIT: Interacts with BMP1 and fibronectin (By similarity).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus (By similarity). Secreted,
CC extracellular space, extracellular matrix. Note=Colocalizes with
CC BMP1 in the Golgi (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=OSF-2OS;
CC IsoId=Q15063-1; Sequence=Displayed;
CC Name=2; Synonyms=OSF-2p1;
CC IsoId=Q15063-2; Sequence=VSP_050005;
CC Name=3;
CC IsoId=Q15063-3; Sequence=VSP_050669, VSP_050670;
CC Name=4;
CC IsoId=Q15063-4; Sequence=VSP_050005, VSP_050670;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in aorta,
CC stomach, lower gastrointestinal tract, placenta, uterus and
CC breast. Up-regulated in epithelial ovarian tumors. Not expressed
CC in normal ovaries. Also highly expressed at the tumor periphery of
CC lung carcinoma tissue but not within the tumor. Overexpressed in
CC breast cancers.
CC -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K
CC dependent carboxylation. These residues are essential for the
CC binding of calcium.
CC -!- SIMILARITY: Contains 1 EMI domain.
CC -!- SIMILARITY: Contains 4 FAS1 domains.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; D13665; BAA02836.1; -; mRNA.
DR EMBL; D13666; BAA02837.1; -; mRNA.
DR EMBL; AY140646; AAN17733.1; -; mRNA.
DR EMBL; AY918092; AAY15840.1; -; mRNA.
DR EMBL; AL138679; CAH70107.1; -; Genomic_DNA.
DR EMBL; AL646087; CAH70107.1; JOINED; Genomic_DNA.
DR EMBL; AL646087; CAH73568.1; -; Genomic_DNA.
DR EMBL; AL138679; CAH73568.1; JOINED; Genomic_DNA.
DR EMBL; AL138679; CAH70104.1; -; Genomic_DNA.
DR EMBL; AL646087; CAH70104.1; JOINED; Genomic_DNA.
DR EMBL; AL646087; CAH73569.1; -; Genomic_DNA.
DR EMBL; AL138679; CAH73569.1; JOINED; Genomic_DNA.
DR EMBL; CH471075; EAX08590.1; -; Genomic_DNA.
DR EMBL; BC106709; AAI06710.1; -; mRNA.
DR EMBL; BC106710; AAI06711.1; -; mRNA.
DR PIR; S36110; S36110.
DR PIR; S36111; S36111.
DR RefSeq; NP_001129406.1; NM_001135934.1.
DR RefSeq; NP_001129407.1; NM_001135935.1.
DR RefSeq; NP_001129408.1; NM_001135936.1.
DR RefSeq; NP_006466.2; NM_006475.2.
DR UniGene; Hs.136348; -.
DR UniGene; Hs.721018; -.
DR ProteinModelPortal; Q15063; -.
DR SMR; Q15063; 236-367, 503-628.
DR IntAct; Q15063; 2.
DR MINT; MINT-4533078; -.
DR STRING; 9606.ENSP00000369071; -.
DR PhosphoSite; Q15063; -.
DR DMDM; 93138709; -.
DR PaxDb; Q15063; -.
DR PRIDE; Q15063; -.
DR Ensembl; ENST00000379742; ENSP00000369066; ENSG00000133110.
DR Ensembl; ENST00000379747; ENSP00000369071; ENSG00000133110.
DR Ensembl; ENST00000541179; ENSP00000437959; ENSG00000133110.
DR GeneID; 10631; -.
DR KEGG; hsa:10631; -.
DR UCSC; uc001uwo.4; human.
DR CTD; 10631; -.
DR GeneCards; GC13M038136; -.
DR HGNC; HGNC:16953; POSTN.
DR HPA; HPA012306; -.
DR MIM; 608777; gene.
DR neXtProt; NX_Q15063; -.
DR PharmGKB; PA134900304; -.
DR eggNOG; COG2335; -.
DR HOGENOM; HOG000220865; -.
DR HOVERGEN; HBG000715; -.
DR InParanoid; Q15063; -.
DR OMA; HGEPIIK; -.
DR PhylomeDB; Q15063; -.
DR ChiTaRS; POSTN; human.
DR GeneWiki; Periostin; -.
DR GeneWiki; POSTN; -.
DR GenomeRNAi; 10631; -.
DR NextBio; 40399; -.
DR PRO; PR:Q15063; -.
DR ArrayExpress; Q15063; -.
DR Bgee; Q15063; -.
DR CleanEx; HS_POSTN; -.
DR Genevestigator; Q15063; -.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005578; C:proteinaceous extracellular matrix; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR GO; GO:0009888; P:tissue development; IEA:Ensembl.
DR Gene3D; 2.30.180.10; -; 4.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR016666; TGFb-ind_bIGH3/osteoblast_fac2.
DR Pfam; PF02469; Fasciclin; 4.
DR PIRSF; PIRSF016553; BIGH3_OSF2; 1.
DR SMART; SM00554; FAS1; 4.
DR SUPFAM; SSF82153; SSF82153; 4.
DR PROSITE; PS51041; EMI; 1.
DR PROSITE; PS50213; FAS1; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Complete proteome;
KW Disulfide bond; Extracellular matrix; Gamma-carboxyglutamic acid;
KW Glycoprotein; Golgi apparatus; Heparin-binding; Polymorphism;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 21 Potential.
FT CHAIN 22 836 Periostin.
FT /FTId=PRO_0000008789.
FT DOMAIN 40 94 EMI.
FT DOMAIN 97 230 FAS1 1.
FT DOMAIN 234 365 FAS1 2.
FT DOMAIN 368 492 FAS1 3.
FT DOMAIN 496 628 FAS1 4.
FT MOD_RES 124 124 4-carboxyglutamate (Potential).
FT MOD_RES 125 125 4-carboxyglutamate (Potential).
FT MOD_RES 127 127 4-carboxyglutamate (Potential).
FT MOD_RES 140 140 4-carboxyglutamate (Potential).
FT MOD_RES 154 154 4-carboxyglutamate (Potential).
FT MOD_RES 160 160 4-carboxyglutamate (Potential).
FT MOD_RES 242 242 4-carboxyglutamate (Potential).
FT MOD_RES 244 244 4-carboxyglutamate (Potential).
FT MOD_RES 261 261 4-carboxyglutamate (Potential).
FT MOD_RES 277 277 4-carboxyglutamate (Potential).
FT MOD_RES 280 280 4-carboxyglutamate (Potential).
FT MOD_RES 288 288 4-carboxyglutamate (Potential).
FT MOD_RES 298 298 4-carboxyglutamate (Potential).
FT MOD_RES 313 313 4-carboxyglutamate (Potential).
FT MOD_RES 322 322 4-carboxyglutamate (Potential).
FT MOD_RES 325 325 4-carboxyglutamate (Potential).
FT MOD_RES 496 496 4-carboxyglutamate (Potential).
FT MOD_RES 501 501 4-carboxyglutamate (Potential).
FT MOD_RES 517 517 4-carboxyglutamate (Potential).
FT MOD_RES 523 523 4-carboxyglutamate (Potential).
FT MOD_RES 547 547 4-carboxyglutamate (Potential).
FT MOD_RES 548 548 4-carboxyglutamate (Potential).
FT MOD_RES 550 550 4-carboxyglutamate (Potential).
FT MOD_RES 578 578 4-carboxyglutamate (Potential).
FT CARBOHYD 599 599 N-linked (GlcNAc...).
FT DISULFID 44 80 By similarity.
FT DISULFID 60 69 By similarity.
FT DISULFID 79 92 By similarity.
FT VAR_SEQ 670 727 TTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPE
FT FRLIKEGETITEVIHGE -> K (in isoform 2 and
FT isoform 4).
FT /FTId=VSP_050005.
FT VAR_SEQ 670 697 TTKIITKVVEPKIKVIEGSLQPIIKTEG -> R (in
FT isoform 3).
FT /FTId=VSP_050669.
FT VAR_SEQ 783 810 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_050670.
FT VARIANT 339 339 T -> I (in dbSNP:rs9594223).
FT /FTId=VAR_049115.
FT VARIANT 814 814 V -> M (in dbSNP:rs9547952).
FT /FTId=VAR_049116.
FT CONFLICT 290 290 I -> F (in Ref. 1; BAA02836/BAA02837 and
FT 3; AAY15840).
FT CONFLICT 421 421 D -> V (in Ref. 1; BAA02836/BAA02837 and
FT 3; AAY15840).
SQ SEQUENCE 836 AA; 93314 MW; 55E7B82D094824FD CRC64;
MIPFLPMFSL LLLLIVNPIN ANNHYDKILA HSRIRGRDQG PNVCALQQIL GTKKKYFSTC
KNWYKKSICG QKTTVLYECC PGYMRMEGMK GCPAVLPIDH VYGTLGIVGA TTTQRYSDAS
KLREEIEGKG SFTYFAPSNE AWDNLDSDIR RGLESNVNVE LLNALHSHMI NKRMLTKDLK
NGMIIPSMYN NLGLFINHYP NGVVTVNCAR IIHGNQIATN GVVHVIDRVL TQIGTSIQDF
IEAEDDLSSF RAAAITSDIL EALGRDGHFT LFAPTNEAFE KLPRGVLERI MGDKVASEAL
MKYHILNTLQ CSESIMGGAV FETLEGNTIE IGCDGDSITV NGIKMVNKKD IVTNNGVIHL
IDQVLIPDSA KQVIELAGKQ QTTFTDLVAQ LGLASALRPD GEYTLLAPVN NAFSDDTLSM
DQRLLKLILQ NHILKVKVGL NELYNGQILE TIGGKQLRVF VYRTAVCIEN SCMEKGSKQG
RNGAIHIFRE IIKPAEKSLH EKLKQDKRFS TFLSLLEAAD LKELLTQPGD WTLFVPTNDA
FKGMTSEEKE ILIRDKNALQ NIILYHLTPG VFIGKGFEPG VTNILKTTQG SKIFLKEVND
TLLVNELKSK ESDIMTTNGV IHVVDKLLYP ADTPVGNDQL LEILNKLIKY IQIKFVRGST
FKEIPVTVYT TKIITKVVEP KIKVIEGSLQ PIIKTEGPTL TKVKIEGEPE FRLIKEGETI
TEVIHGEPII KKYTKIIDGV PVEITEKETR EERIITGPEI KYTRISTGGG ETEETLKKLL
QEEVTKVTKF IEGGDGHLFE DEEIKRLLQG DTPVRKLQAN KKVQGSRRRL REGRSQ
//
MIM
608777
*RECORD*
*FIELD* NO
608777
*FIELD* TI
*608777 PERIOSTIN; POSTN
;;PN;;
OSTEOBLAST-SPECIFIC FACTOR 2; OSF2
*FIELD* TX
CLONING
read more
Takeshita et al. (1993) cloned mouse Postn, which they designated Osf2.
By screening human placenta and osteosarcoma cDNA libraries with mouse
Postn as probe, they cloned 2 variants of human POSTN. One variant
encodes a deduced 779-amino acid protein with an apparent molecular mass
of 87.0 kD, and the other encodes a deduced 836-amino acid protein with
an apparent molecular mass of 93.3 kD. POSTN contains a typical signal
sequence, followed by a cysteine-rich domain, a 4-fold repeat structure
of about 150 amino acids, and a C-terminal domain. Mouse and human POSTN
share 89.2% amino acid identity overall and 90.1% identity in their
mature forms. Northern blot analysis of a mouse osteoblastic cell line
detected a 3.4-kb Postn transcript. RNA dot blot analysis detected
expression of Postn in primary mouse osteoblasts and in lung, but not in
any other tissues examined.
Gillan et al. (2002) identified a periostin (PN) EST clone encoding a
deduced 782-amino acid protein. RNA dot blot analysis detected PN
expression in a wide range of normal adult tissues, including aorta,
stomach, lower gastrointestinal tract, placenta, uterus, and breast. PN
was expressed at variable levels in all fetal tissues examined. Western
blot analysis detected strong periostin staining in fetal calf serum,
but not in newborn calf serum. Gillan et al. (2002) found that PN was
secreted by cultures derived from epithelial ovarian cancer, but not
from normal ovarian epithelial cells. They identified multiple protein
bands of about 90 kD, as well as a band of about 170 kD, which may
represent a covalently linked multimer. PN was present in 20 of 21
ascites from ovarian cancer patients.
GENE FUNCTION
Gillan et al. (2002) found that purified recombinant PN supported
adhesion of ovarian epithelial cells. Adhesion was inhibited by
antibodies against alpha-V (ITGAV; 193210)/beta-3 (ITGB3; 173470) or
alpha-V/beta-5 (ITGB5; 147561) integrins, but not by antibodies against
beta-1 integrin (ITGB1; 135630). Furthermore, alpha-V/beta-3 integrin,
but not beta-1 integrin, colocalized to the focal adhesion plaques
formed on PN. Cells plated on PN formed fewer stress fibers and were
more motile compared with those plated on fibronectin (135600). Gillan
et al. (2002) concluded that PN functions as a ligand for alpha-V/beta-3
and alpha-V/beta-5 integrins to support adhesion and migration of
ovarian epithelial cells.
Shao et al. (2004) found that periostin was overexpressed by the
majority of human primary breast cancers examined. Transfected tumor
cell lines overexpressing periostin showed accelerated growth and
angiogenesis as xenografts in immunocompromised animals.
Periostin-mediated angiogenesis was derived in part from upregulation of
vascular endothelial growth factor receptor (KDR; 191306) by endothelial
cells through an alpha-V/beta-3 integrin-focal adhesion kinase
(600758)-mediated signaling pathway.
Using gene expression microarrays, Woodruff et al. (2007) found that
CLCA1 (603906), POSTN, and SERPINB2 (PAI2; 173390) were upregulated in
airway epithelial cells of individuals with asthma (see 600807), but not
smokers. Corticosteroid treatment downregulated expression of these 3
genes and upregulated expression of FKBP51 (602623). High baseline
expression of CLCA1, POSTN, and SERPINB2 was associated with a good
clinical response to corticosteroids, whereas high expression of FKBP51
was associated with a poor response. Treatment of airway epithelial
cells with IL13 resulted in increased expression of CLCA1, POSTN, and
SERPINB2, an effect that could be suppressed by corticosteroids.
Kuhn et al. (2007) showed that extracellular periostin induced reentry
of differentiated mammalian cardiomyocytes into the cell cycle.
Periostin stimulated mononucleated cardiomyocytes to go through the full
mitotic cell cycle. Periostin activated alpha-V, beta-1, beta-3, and
beta-5 integrins located in the cardiomyocyte cell membrane. Activation
of phosphatidylinositol-3-OH kinase (see 171833) was required for
periostin-induced reentry of cardiomyocytes into the cell cycle and was
sufficient for cell cycle reentry in the absence of periostin. After
myocardial infarction, periostin-induced cardiomyocyte cell cycle
reentry and mitosis were associated with improved ventricular remodeling
and myocardial function, reduced fibrosis and infarct size, and increase
angiogenesis.
Using immunohistochemical analysis, Snider et al. (2008) showed that
periostin was expressed in pediatric aortic valves in a trilaminar
pattern, with increased expression in fibrosa and spongiosa relative to
ventricularis. Stenotic pediatric bicuspid valves that had lost normal
trilaminar stratification of the extracellular matrix showed greatly
reduced periostin expression. In mice, periostin was expressed
throughout cardiac development in the fibrous cardiac skeleton and
endocardial cushions, but it was absent from cardiomyocytes. Periostin
was detected in all 4 adult mouse valves examined.
Malanchi et al. (2012) demonstrated that a small population of cancer
stem cells is critical for metastatic colonization, i.e., the initial
expansion of cancer cells at the secondary site, and that stromal niche
signals are crucial to this expansion process. The authors found that
periostin, a component of the extracellular matrix, is expressed by
fibroblasts in the normal tissue and in the stroma of the primary tumor.
Infiltrating tumor cells need to induce stromal POSTN expression in the
secondary target organ (in this case the lung) to initiate colonization.
POSTN is required to allow cancer stem cell maintenance, and blocking
its function prevents metastasis. POSTN recruits Wnt ligands and thereby
increases Wnt signaling in cancer stem cells. Malanchi et al. (2012)
suggested that the education of stromal cells by infiltrating tumor
cells is an important step in metastatic colonization and that
preventing de novo niche formation may be a novel strategy for the
treatment of metastatic disease.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the POSTN
gene to chromosome 13 (TMAP STS-H12747).
ANIMAL MODEL
Snider et al. (2008) found that periostin-null mice exhibited variable
cardiac valve disease, with neonatal lethality in 14%. Periostin-null
animals that survived showed truncated leaflets with ectopic
cardiomyocytes and smooth muscle cells, misexpression of the cartilage
proteoglycan aggrecan (ACAN; 155760), disorganized matrix
stratification, and reduced Tgf-beta (TGFB1; 190180) signaling. Those
that died also showed leaflet discontinuities, delamination defects, and
deposition of acellular extracellular matrix. Periostin-deficient
fibroblasts were unable to support normal valve remodeling or establish
a mature cardiac skeleton. Snider et al. (2008) concluded that periostin
is required for TGF-beta-dependent development of noncardiomyocyte
lineages in the heart.
*FIELD* RF
1. Gillan, L.; Matei, D.; Fishman, D. A.; Gerbin, C. S.; Karlan, B.
Y.; Chang, D. D.: Periostin secreted by epithelial ovarian carcinoma
is a ligand for alpha-V-beta-3 and alpha-V-beta-5 integrins and promotes
cell motility. Cancer Res. 62: 5358-5364, 2002.
2. Kuhn, B.; del Monte, F.; Hajjar, R. J.; Chang, Y.-S.; Lebeche,
D.; Arab, S.; Keating, M. T.: Periostin induces proliferation of
differentiated cardiomyocytes and promotes cardiac repair. Nature
Med. 13: 962-969, 2007.
3. Malanchi, I.; Santamaria-Martinez, A.; Susanto, E.; Peng, H.; Lehr,
H.-A.; Delaloye, J.-F.; Huelsken, J.: Interactions between cancer
stem cells and their niche govern metastatic colonization. Nature 481:
85-89, 2012.
4. Shao, R.; Bao, S.; Bai, X.; Blanchette, C.; Anderson, R. M.; Dang,
T.; Gishizky, M. L.; Marks, J. R.; Wang, X.-F.: Acquired expression
of periostin by human breast cancers promotes tumor angiogenesis through
up-regulation of vascular endothelial growth factor receptor 2 expression. Molec.
Cell. Biol. 24: 3992-4003, 2004.
5. Snider, P.; Hinton, R. B.; Moreno-Rodriguez, R. A.; Wang, J.; Rogers,
R.; Lindsley, A.; Li, F.; Ingram, D. A.; Menick, D.; Field, L.; Firulli,
A. B.; Molkentin, J. D.; Markwald, R.; Conway, S. J.: Periostin is
required for maturation and extracellular matrix stabilization of
noncardiomyocyte lineages of the heart. Circ. Res. 102: 752-760,
2008.
6. Takeshita, S.; Kikuno, R.; Tezuka, K.; Amann, E.: Osteoblast-specific
factor 2: cloning of a putative bone adhesion protein with homology
with the insect protein fasciclin 1. Biochem. J. 294: 271-278, 1993.
7. Woodruff, P. G.; Boushey, H. A.; Dolganov, G. M.; Barker, C. S.;
Yang, Y. H.; Donnelly, S.; Ellwanger, A.; Sidhu, S. S.; Dao-Pick,
T. P.; Pantoja, C.; Erle, D. J.; Yamamoto, K. R.; Fahy, J. V.: Genome-wide
profiling identifies epithelial cell genes associated with asthma
and with treatment response to corticosteroids. Proc. Nat. Acad.
Sci. 104: 15858-15863, 2007.
*FIELD* CN
Ada Hamosh - updated: 02/07/2012
Patricia A. Hartz - updated: 4/15/2009
Ada Hamosh - updated: 3/28/2008
Paul J. Converse - updated: 3/24/2008
*FIELD* CD
Patricia A. Hartz: 7/6/2004
*FIELD* ED
terry: 02/07/2012
mgross: 4/15/2009
alopez: 3/28/2008
mgross: 3/24/2008
mgross: 7/6/2004
*RECORD*
*FIELD* NO
608777
*FIELD* TI
*608777 PERIOSTIN; POSTN
;;PN;;
OSTEOBLAST-SPECIFIC FACTOR 2; OSF2
*FIELD* TX
CLONING
read more
Takeshita et al. (1993) cloned mouse Postn, which they designated Osf2.
By screening human placenta and osteosarcoma cDNA libraries with mouse
Postn as probe, they cloned 2 variants of human POSTN. One variant
encodes a deduced 779-amino acid protein with an apparent molecular mass
of 87.0 kD, and the other encodes a deduced 836-amino acid protein with
an apparent molecular mass of 93.3 kD. POSTN contains a typical signal
sequence, followed by a cysteine-rich domain, a 4-fold repeat structure
of about 150 amino acids, and a C-terminal domain. Mouse and human POSTN
share 89.2% amino acid identity overall and 90.1% identity in their
mature forms. Northern blot analysis of a mouse osteoblastic cell line
detected a 3.4-kb Postn transcript. RNA dot blot analysis detected
expression of Postn in primary mouse osteoblasts and in lung, but not in
any other tissues examined.
Gillan et al. (2002) identified a periostin (PN) EST clone encoding a
deduced 782-amino acid protein. RNA dot blot analysis detected PN
expression in a wide range of normal adult tissues, including aorta,
stomach, lower gastrointestinal tract, placenta, uterus, and breast. PN
was expressed at variable levels in all fetal tissues examined. Western
blot analysis detected strong periostin staining in fetal calf serum,
but not in newborn calf serum. Gillan et al. (2002) found that PN was
secreted by cultures derived from epithelial ovarian cancer, but not
from normal ovarian epithelial cells. They identified multiple protein
bands of about 90 kD, as well as a band of about 170 kD, which may
represent a covalently linked multimer. PN was present in 20 of 21
ascites from ovarian cancer patients.
GENE FUNCTION
Gillan et al. (2002) found that purified recombinant PN supported
adhesion of ovarian epithelial cells. Adhesion was inhibited by
antibodies against alpha-V (ITGAV; 193210)/beta-3 (ITGB3; 173470) or
alpha-V/beta-5 (ITGB5; 147561) integrins, but not by antibodies against
beta-1 integrin (ITGB1; 135630). Furthermore, alpha-V/beta-3 integrin,
but not beta-1 integrin, colocalized to the focal adhesion plaques
formed on PN. Cells plated on PN formed fewer stress fibers and were
more motile compared with those plated on fibronectin (135600). Gillan
et al. (2002) concluded that PN functions as a ligand for alpha-V/beta-3
and alpha-V/beta-5 integrins to support adhesion and migration of
ovarian epithelial cells.
Shao et al. (2004) found that periostin was overexpressed by the
majority of human primary breast cancers examined. Transfected tumor
cell lines overexpressing periostin showed accelerated growth and
angiogenesis as xenografts in immunocompromised animals.
Periostin-mediated angiogenesis was derived in part from upregulation of
vascular endothelial growth factor receptor (KDR; 191306) by endothelial
cells through an alpha-V/beta-3 integrin-focal adhesion kinase
(600758)-mediated signaling pathway.
Using gene expression microarrays, Woodruff et al. (2007) found that
CLCA1 (603906), POSTN, and SERPINB2 (PAI2; 173390) were upregulated in
airway epithelial cells of individuals with asthma (see 600807), but not
smokers. Corticosteroid treatment downregulated expression of these 3
genes and upregulated expression of FKBP51 (602623). High baseline
expression of CLCA1, POSTN, and SERPINB2 was associated with a good
clinical response to corticosteroids, whereas high expression of FKBP51
was associated with a poor response. Treatment of airway epithelial
cells with IL13 resulted in increased expression of CLCA1, POSTN, and
SERPINB2, an effect that could be suppressed by corticosteroids.
Kuhn et al. (2007) showed that extracellular periostin induced reentry
of differentiated mammalian cardiomyocytes into the cell cycle.
Periostin stimulated mononucleated cardiomyocytes to go through the full
mitotic cell cycle. Periostin activated alpha-V, beta-1, beta-3, and
beta-5 integrins located in the cardiomyocyte cell membrane. Activation
of phosphatidylinositol-3-OH kinase (see 171833) was required for
periostin-induced reentry of cardiomyocytes into the cell cycle and was
sufficient for cell cycle reentry in the absence of periostin. After
myocardial infarction, periostin-induced cardiomyocyte cell cycle
reentry and mitosis were associated with improved ventricular remodeling
and myocardial function, reduced fibrosis and infarct size, and increase
angiogenesis.
Using immunohistochemical analysis, Snider et al. (2008) showed that
periostin was expressed in pediatric aortic valves in a trilaminar
pattern, with increased expression in fibrosa and spongiosa relative to
ventricularis. Stenotic pediatric bicuspid valves that had lost normal
trilaminar stratification of the extracellular matrix showed greatly
reduced periostin expression. In mice, periostin was expressed
throughout cardiac development in the fibrous cardiac skeleton and
endocardial cushions, but it was absent from cardiomyocytes. Periostin
was detected in all 4 adult mouse valves examined.
Malanchi et al. (2012) demonstrated that a small population of cancer
stem cells is critical for metastatic colonization, i.e., the initial
expansion of cancer cells at the secondary site, and that stromal niche
signals are crucial to this expansion process. The authors found that
periostin, a component of the extracellular matrix, is expressed by
fibroblasts in the normal tissue and in the stroma of the primary tumor.
Infiltrating tumor cells need to induce stromal POSTN expression in the
secondary target organ (in this case the lung) to initiate colonization.
POSTN is required to allow cancer stem cell maintenance, and blocking
its function prevents metastasis. POSTN recruits Wnt ligands and thereby
increases Wnt signaling in cancer stem cells. Malanchi et al. (2012)
suggested that the education of stromal cells by infiltrating tumor
cells is an important step in metastatic colonization and that
preventing de novo niche formation may be a novel strategy for the
treatment of metastatic disease.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the POSTN
gene to chromosome 13 (TMAP STS-H12747).
ANIMAL MODEL
Snider et al. (2008) found that periostin-null mice exhibited variable
cardiac valve disease, with neonatal lethality in 14%. Periostin-null
animals that survived showed truncated leaflets with ectopic
cardiomyocytes and smooth muscle cells, misexpression of the cartilage
proteoglycan aggrecan (ACAN; 155760), disorganized matrix
stratification, and reduced Tgf-beta (TGFB1; 190180) signaling. Those
that died also showed leaflet discontinuities, delamination defects, and
deposition of acellular extracellular matrix. Periostin-deficient
fibroblasts were unable to support normal valve remodeling or establish
a mature cardiac skeleton. Snider et al. (2008) concluded that periostin
is required for TGF-beta-dependent development of noncardiomyocyte
lineages in the heart.
*FIELD* RF
1. Gillan, L.; Matei, D.; Fishman, D. A.; Gerbin, C. S.; Karlan, B.
Y.; Chang, D. D.: Periostin secreted by epithelial ovarian carcinoma
is a ligand for alpha-V-beta-3 and alpha-V-beta-5 integrins and promotes
cell motility. Cancer Res. 62: 5358-5364, 2002.
2. Kuhn, B.; del Monte, F.; Hajjar, R. J.; Chang, Y.-S.; Lebeche,
D.; Arab, S.; Keating, M. T.: Periostin induces proliferation of
differentiated cardiomyocytes and promotes cardiac repair. Nature
Med. 13: 962-969, 2007.
3. Malanchi, I.; Santamaria-Martinez, A.; Susanto, E.; Peng, H.; Lehr,
H.-A.; Delaloye, J.-F.; Huelsken, J.: Interactions between cancer
stem cells and their niche govern metastatic colonization. Nature 481:
85-89, 2012.
4. Shao, R.; Bao, S.; Bai, X.; Blanchette, C.; Anderson, R. M.; Dang,
T.; Gishizky, M. L.; Marks, J. R.; Wang, X.-F.: Acquired expression
of periostin by human breast cancers promotes tumor angiogenesis through
up-regulation of vascular endothelial growth factor receptor 2 expression. Molec.
Cell. Biol. 24: 3992-4003, 2004.
5. Snider, P.; Hinton, R. B.; Moreno-Rodriguez, R. A.; Wang, J.; Rogers,
R.; Lindsley, A.; Li, F.; Ingram, D. A.; Menick, D.; Field, L.; Firulli,
A. B.; Molkentin, J. D.; Markwald, R.; Conway, S. J.: Periostin is
required for maturation and extracellular matrix stabilization of
noncardiomyocyte lineages of the heart. Circ. Res. 102: 752-760,
2008.
6. Takeshita, S.; Kikuno, R.; Tezuka, K.; Amann, E.: Osteoblast-specific
factor 2: cloning of a putative bone adhesion protein with homology
with the insect protein fasciclin 1. Biochem. J. 294: 271-278, 1993.
7. Woodruff, P. G.; Boushey, H. A.; Dolganov, G. M.; Barker, C. S.;
Yang, Y. H.; Donnelly, S.; Ellwanger, A.; Sidhu, S. S.; Dao-Pick,
T. P.; Pantoja, C.; Erle, D. J.; Yamamoto, K. R.; Fahy, J. V.: Genome-wide
profiling identifies epithelial cell genes associated with asthma
and with treatment response to corticosteroids. Proc. Nat. Acad.
Sci. 104: 15858-15863, 2007.
*FIELD* CN
Ada Hamosh - updated: 02/07/2012
Patricia A. Hartz - updated: 4/15/2009
Ada Hamosh - updated: 3/28/2008
Paul J. Converse - updated: 3/24/2008
*FIELD* CD
Patricia A. Hartz: 7/6/2004
*FIELD* ED
terry: 02/07/2012
mgross: 4/15/2009
alopez: 3/28/2008
mgross: 3/24/2008
mgross: 7/6/2004