Thrombospondin-2

THBS2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1YO8, 2RHP
Identifiers
Aliases	THBS2 , TSP2, thrombospondin 2
External IDs	OMIM: 188061 MGI: 98738 HomoloGene: 2438 GeneCards: THBS2
Gene location (Human)
Chr.	Chromosome 6 (human)
End	169,254,044 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	14,694,235 bp
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• calcium ion binding ; • GO:0001948 protein binding ; • heparin binding ; • extracellular matrix structural constituent ;
Cellular component	• extracellular matrix ; • platelet alpha granule ; • basement membrane ; • extracellular region ; • extracellular ; • collagen-containing extracellular matrix ;
Biological process	• positive regulation of synapse assembly ; • negative regulation of angiogenesis ; • cell adhesion ; • extracellular matrix organization ;
	Sources:Amigo / QuickGO
Orthologs
	7058
	21826
	ENSG00000186340
	ENSMUSG00000023885
	P35442
	Q03350
	NM_003247
	NM_011581
	NP_003238 ; NP_001368868 ; NP_001368869 ; NP_001368870 ; NP_001368871 Contents Interactions ; References ; Further reading ;
	NP_035711
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated January 03, 2021

Thrombospondin-2 is a protein that in humans is encoded by the THBS2 gene.^[5]^[6]

The protein encoded by this gene belongs to the thrombospondin family. It is a disulfide-linked homotrimeric glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. The role of the protein in cancer is controversial, contrasting studies show positive and negative roles for cancer development. Studies of the mouse counterpart suggest that this protein may modulate the cell surface properties of mesenchymal cells and be involved in cell adhesion and migration.^[6]

Interactions

THBS2 has been shown to interact with MMP2.^[7]

Related Research Articles

A disintegrin and metalloproteinase with thrombospondin motifs 5 also known as ADAMTS5 is an enzyme that in humans is encoded by the ADAMTS5 gene.

Thrombospondins (TSPs) are a family of secreted glycoproteins with antiangiogenic functions. Due to their dynamic role within the extracellular matrix they are considered matricellular proteins. The first member of the family, thrombospondin 1 (THBS1), was discovered in 1971 by Nancy L. Baenziger.

Decorin is a protein that in humans is encoded by the DCN gene.

Osteonectin (ON) also known as secreted protein acidic and rich in cysteine (SPARC) or basement-membrane protein 40 (BM-40) is a protein that in humans is encoded by the SPARC gene.

Thrombospondin 1, abbreviated as THBS1, is a protein that in humans is encoded by the THBS1 gene.

72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene. The MMP2 gene is located on chromosome 16 at position 12.2.

A disintegrin and metalloproteinase with thrombospondin motifs 4 is an enzyme that in humans is encoded by the ADAMTS4 gene.

Testicular receptor 4 also known as NR2C2 is a protein that in humans is encoded by the NR2C2 gene.

Lumican, also known as LUM, is an extracellular matrix protein that, in humans, is encoded by the LUM gene on chromosome 12.

Matrix metalloproteinase-19 (MMP-19) also known as matrix metalloproteinase RASI is an enzyme that in humans is encoded by the MMP19 gene.

Dual specificity mitogen-activated protein kinase kinase 5 is an enzyme that in humans is encoded by the MAP2K5 gene.

ADAM19 , is a human gene.

Thrombospondin-3 (TSP3) is a protein that in humans is encoded by the THBS3 gene.

Thrombospondin-4 is a protein that in humans is encoded by the THBS4 gene.

SPARC-like protein 1, also known as hevin, is a secreted protein with high structural similarity to SPARC. It interacts with the extracellular matrix to create intermediate states of cell adhesion. Due to its dynamic extracellular roles, being implicated in cancer metastasis and inflammation, it is considered a matricellular protein. In humans hevin is encoded by the SPARCL1 gene.

A disintegrin and metalloproteinase with thrombospondin motifs 8 is an enzyme that in humans is encoded by the ADAMTS8 gene.

Disintegrin and metalloproteinase domain-containing protein 23 is a non-catalytic protein that in humans is encoded by the ADAM23 gene. It is a member of the ADAM family of extracellular matrix metalloproteinases.

A disintegrin and metalloproteinase with thrombospondin motifs 3 is an enzyme that in humans is encoded by the ADAMTS3 gene. The protein encoded by this gene is the major procollagen II N-propeptidase.

A disintegrin and metalloproteinase with thrombospondin motifs 12 is an enzyme that in humans is encoded by the ADAMTS12 gene.

ADAM metallopeptidase with thrombospondin type 1 motif, 17 is a protein that in humans is encoded by the ADAMTS17 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000186340 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000023885 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Hirose Y, Chiba K, Karasugi T, Nakajima M, Kawaguchi Y, Mikami Y, Furuichi T, Mio F, Miyake A, Miyamoto T, Ozaki K, Takahashi A, Mizuta H, Kubo T, Kimura T, Tanaka T, Toyama Y, Ikegawa S (May 2008). "A functional polymorphism in THBS2 that affects alternative splicing and MMP binding is associated with lumbar-disc herniation". American Journal of Human Genetics. 82 (5): 1122–9. doi:10.1016/j.ajhg.2008.03.013. PMC 2427305 . PMID 18455130.
1 2 "Entrez Gene: THBS2 thrombospondin 2".
↑ Bein K, Simons M (Oct 2000). "Thrombospondin type 1 repeats interact with matrix metalloproteinase 2. Regulation of metalloproteinase activity". The Journal of Biological Chemistry. 275 (41): 32167–73. doi: 10.1074/jbc.M003834200 . PMID 10900205.

Bornstein P, Kyriakides TR, Yang Z, Armstrong LC, Birk DE (Dec 2000). "Thrombospondin 2 modulates collagen fibrillogenesis and angiogenesis". The Journal of Investigative Dermatology. Symposium Proceedings. 5 (1): 61–6. doi:10.1046/j.1087-0024.2000.00005.x. PMID 11147677.
O'Rourke KM, Laherty CD, Dixit VM (Dec 1992). "Thrombospondin 1 and thrombospondin 2 are expressed as both homo- and heterotrimers". The Journal of Biological Chemistry. 267 (35): 24921–4. PMID 1459996.
LaBell TL, Milewicz DJ, Disteche CM, Byers PH (Mar 1992). "Thrombospondin II: partial cDNA sequence, chromosome location, and expression of a second member of the thrombospondin gene family in humans". Genomics. 12 (3): 421–9. doi:10.1016/0888-7543(92)90430-Z. PMID 1559694.
LaBell TL, Byers PH (Jul 1993). "Sequence and characterization of the complete human thrombospondin 2 cDNA: potential regulatory role for the 3' untranslated region". Genomics. 17 (1): 225–9. doi:10.1006/geno.1993.1308. PMID 8406456.
Adolph KW, Liska DJ, Bornstein P (Jul 1997). "Analysis of the promoter and transcription start sites of the human thrombospondin 2 gene (THBS2)". Gene. 193 (1): 5–11. doi:10.1016/S0378-1119(97)00070-X. PMID 9249061.
Kyriakides TR, Zhu YH, Smith LT, Bain SD, Yang Z, Lin MT, Danielson KG, Iozzo RV, LaMarca M, McKinney CE, Ginns EI, Bornstein P (Jan 1998). "Mice that lack thrombospondin 2 display connective tissue abnormalities that are associated with disordered collagen fibrillogenesis, an increased vascular density, and a bleeding diathesis". The Journal of Cell Biology. 140 (2): 419–30. doi:10.1083/jcb.140.2.419. PMC 2132586 . PMID 9442117.
Adolph KW (May 1999). "Relative abundance of thrombospondin 2 and thrombospondin 3 mRNAs in human tissues". Biochemical and Biophysical Research Communications. 258 (3): 792–6. doi:10.1006/bbrc.1999.0710. PMID 10329465.
Carron JA, Bowler WB, Wagstaff SC, Gallagher JA (Sep 1999). "Expression of members of the thrombospondin family by human skeletal tissues and cultured cells". Biochemical and Biophysical Research Communications. 263 (2): 389–91. doi:10.1006/bbrc.1999.1380. PMID 10491303.
Bein K, Simons M (Oct 2000). "Thrombospondin type 1 repeats interact with matrix metalloproteinase 2. Regulation of metalloproteinase activity". The Journal of Biological Chemistry. 275 (41): 32167–73. doi: 10.1074/jbc.M003834200 . PMID 10900205.
Hawighorst T, Velasco P, Streit M, Hong YK, Kyriakides TR, Brown LF, Bornstein P, Detmar M (Jun 2001). "Thrombospondin-2 plays a protective role in multistep carcinogenesis: a novel host anti-tumor defense mechanism". The EMBO Journal. 20 (11): 2631–40. doi:10.1093/emboj/20.11.2631. PMC 125494 . PMID 11387198.
Misenheimer TM, Hahr AJ, Harms AC, Annis DS, Mosher DF (Dec 2001). "Disulfide connectivity of recombinant C-terminal region of human thrombospondin 2". The Journal of Biological Chemistry. 276 (49): 45882–7. doi: 10.1074/jbc.M104218200 . PMID 11590138.
Armstrong DJ, Hiscott P, Batterbury M, Kaye S (Jun 2002). "Corneal stromal cells (keratocytes) express thrombospondins 2 and 3 in wound repair phenotype". The International Journal of Biochemistry & Cell Biology. 34 (6): 588–93. doi:10.1016/S1357-2725(01)00157-1. PMID 11943589.
Li Z, Calzada MJ, Sipes JM, Cashel JA, Krutzsch HC, Annis DS, Mosher DF, Roberts DD (Apr 2002). "Interactions of thrombospondins with alpha4beta1 integrin and CD47 differentially modulate T cell behavior". The Journal of Cell Biology. 157 (3): 509–19. doi:10.1083/jcb.200109098. PMC 2173289 . PMID 11980922.
Armstrong LC, Björkblom B, Hankenson KD, Siadak AW, Stiles CE, Bornstein P (Jun 2002). "Thrombospondin 2 inhibits microvascular endothelial cell proliferation by a caspase-independent mechanism". Molecular Biology of the Cell. 13 (6): 1893–905. doi:10.1091/mbc.E01-09-0066. PMC 117612 . PMID 12058057.
Hatakeyama H, Nishizawa M, Nakagawa A, Nakano S, Kigoshi T, Miyamori I, Uchida K (Jul 2002). "Thrombospondin expression in aldosterone-producing adenomas". Hypertension Research. 25 (4): 523–7. doi: 10.1291/hypres.25.523 . PMID 12358136.
Boekholdt SM, Trip MD, Peters RJ, Engelen M, Boer JM, Feskens EJ, Zwinderman AH, Kastelein JJ, Reitsma PH (Dec 2002). "Thrombospondin-2 polymorphism is associated with a reduced risk of premature myocardial infarction". Arteriosclerosis, Thrombosis, and Vascular Biology. 22 (12): e24–7. doi: 10.1161/01.ATV.0000046235.22451.66 . PMID 12482844.
Kyriakides TR, Rojnuckarin P, Reidy MA, Hankenson KD, Papayannopoulou T, Kaushansky K, Bornstein P (May 2003). "Megakaryocytes require thrombospondin-2 for normal platelet formation and function". Blood. 101 (10): 3915–23. doi: 10.1182/blood.V101.10.3915 . PMID 12732502.
Kishi M, Nakamura M, Nishimine M, Ishida E, Shimada K, Kirita T, Konishi N (Jun 2003). "Loss of heterozygosity on chromosome 6q correlates with decreased thrombospondin-2 expression in human salivary gland carcinomas". Cancer Science. 94 (6): 530–5. doi: 10.1111/j.1349-7006.2003.tb01478.x . PMID 12824879. S2CID 19472764.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000186340 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000023885 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid18455130-5] Hirose Y, Chiba K, Karasugi T, Nakajima M, Kawaguchi Y, Mikami Y, Furuichi T, Mio F, Miyake A, Miyamoto T, Ozaki K, Takahashi A, Mizuta H, Kubo T, Kimura T, Tanaka T, Toyama Y, Ikegawa S (May 2008). "A functional polymorphism in THBS2 that affects alternative splicing and MMP binding is associated with lumbar-disc herniation". American Journal of Human Genetics. 82 (5): 1122–9. doi:10.1016/j.ajhg.2008.03.013. PMC 2427305 . PMID 18455130.

[entrez-6] 1 2 "Entrez Gene: THBS2 thrombospondin 2".

[pmid10900205-7] Bein K, Simons M (Oct 2000). "Thrombospondin type 1 repeats interact with matrix metalloproteinase 2. Regulation of metalloproteinase activity". The Journal of Biological Chemistry. 275 (41): 32167–73. doi: 10.1074/jbc.M003834200 . PMID 10900205.

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Thrombospondin-2

Contents

Interactions

Related Research Articles

References

Further reading