GDF10

Growth differentiation factor 10
Identifiers
Symbols	GDF10 ; BMP-3b; BMP3B
External IDs	OMIM: 601361 MGI: 95684 HomoloGene: 3640 GeneCards: GDF10 Gene
Gene ontology Molecular function • cytokine activity • transforming growth factor beta receptor binding • growth factor activity Cellular component • extracellular space Biological process • skeletal system development • osteoblast differentiation • transforming growth factor beta receptor signaling pathway • positive regulation of pathway-restricted SMAD protein phosphorylation • regulation of apoptotic process • regulation of MAPK cascade • fat cell differentiation • negative regulation of osteoblast differentiation • cell development • SMAD protein signal transduction Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2662	14560
Ensembl	ENSG00000266524	ENSMUSG00000021943
UniProt	P55107	P97737
RefSeq (mRNA)	NM_004962	NM_145741
RefSeq (protein)	NP_004953	NP_665684
Location (UCSC)	Chr 10: 47.3 – 47.31 Mb	Chr 14: 33.92 – 33.94 Mb
PubMed search

Growth differentiation factor 10 (GDF10) also known as bone morphogenetic protein 3B (BMP-3B) is a protein that in humans is encoded by the GDF10 gene.^[1]

GDF10 belongs to the transforming growth factor beta superfamily that is closely related to bone morphogenetic protein-3 (BMP3). It plays a role in head formation and may have multiple roles in skeletal morphogenesis.^[2][1] GDF10 is also known as BMP-3b, with GDF10 and BMP3 regarded as a separate subgroup within the TGF-beta superfamily.^[1]

In mice, GDF10 mRNA is abundant in the brain, inner ear, uterus, prostate, neural tissues, blood vessels and adipose tissue with low expression in spleen and liver. It is also present in bone of both adults and neonatal mice.^[1] Human GDF10 mRNA is found in the cochlea and lung of foetuses, and in testis, retina, pineal gland, and other neural tissues of adults.^[3]

References

1. Cunningham NS, Jenkins NA, Gilbert DJ, Copeland NG, Reddi AH, Lee SJ (1995). "Growth/differentiation factor-10: a new member of the transforming growth factor-beta superfamily related to bone morphogenetic protein-3". Growth Factors 12 (2): 99–109. doi:10.3109/08977199509028956. PMID 8679252.
2. Hino J, Kangawa K, Matsuo H, Nohno T, Nishimatsu S (2004). "Bone morphogenetic protein-3 family members and their biological functions". Front Biosci 9: 1520–9. doi:10.2741/1355. PMID 14977563.
3. Katoh Y, Katoh M (2006). "Comparative integromics on BMP/GDF family". Int J Mol Med 17 (5): 951–5. doi:10.3892/ijmm.17.5.951. PMID 16596286.

Further reading

• Davila S, Froeling FE, Tan A; et al. (2010). "New genetic associations detected in a host response study to hepatitis B vaccine.". Genes Immun. 11 (3): 232–8. doi:10.1038/gene.2010.1. PMID 20237496.
• Ducy P, Karsenty G (2000). "The family of bone morphogenetic proteins.". Kidney Int. 57 (6): 2207–14. doi:10.1046/j.1523-1755.2000.00081.x. PMID 10844590.
• Grupe A, Li Y, Rowland C; et al. (2006). "A scan of chromosome 10 identifies a novel locus showing strong association with late-onset Alzheimer disease.". Am. J. Hum. Genet. 78 (1): 78–88. doi:10.1086/498851. PMC 1380225. PMID 16385451.
• Hino J, Takao M, Takeshita N; et al. (1996). "cDNA cloning and genomic structure of human bone morphogenetic protein-3B (BMP-3b).". Biochem. Biophys. Res. Commun. 223 (2): 304–10. doi:10.1006/bbrc.1996.0889. PMID 8670277.
• Zhou M, Lucas DA, Chan KC; et al. (2004). "An investigation into the human serum "interactome".". Electrophoresis 25 (9): 1289–98. doi:10.1002/elps.200405866. PMID 15174051.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Kimura K, Toyooka S, Tsukuda K; et al. (2008). "The aberrant promoter methylation of BMP3b and BMP6 in malignant pleural mesotheliomas.". Oncol. Rep. 20 (5): 1265–8. doi:10.3892/or_00000139. PMID 18949431.
• Lafont JE, Talma S, Hopfgarten C, Murphy CL (2008). "Hypoxia promotes the differentiated human articular chondrocyte phenotype through SOX9-dependent and -independent pathways.". J. Biol. Chem. 283 (8): 4778–86. doi:10.1074/jbc.M707729200. PMID 18077449.