Growth differentiation factor

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Growth differentiation factors (GDFs) are a subfamily of proteins belonging to the transforming growth factor beta superfamily that have functions predominantly in development. [1]

Types

Several members of this subfamily have been described, and named GDF1 through GDF15.

Related Research Articles

Bone morphogenetic proteins (BMPs) are a group of growth factors also known as cytokines and as metabologens. Originally discovered by their ability to induce the formation of bone and cartilage, BMPs are now considered to constitute a group of pivotal morphogenetic signals, orchestrating tissue architecture throughout the body. The important functioning of BMP signals in physiology is emphasized by the multitude of roles for dysregulated BMP signalling in pathological processes. Cancerous disease often involves misregulation of the BMP signalling system. Absence of BMP signalling is, for instance, an important factor in the progression of colon cancer, and conversely, overactivation of BMP signalling following reflux-induced esophagitis provokes Barrett's esophagus and is thus instrumental in the development of esophageal adenocarcinoma.

<span class="mw-page-title-main">Growth differentiation factor-9</span> Protein-coding gene in the species Homo sapiens

Growth/differentiation factor 9 is a protein that in humans is encoded by the GDF9 gene.

<span class="mw-page-title-main">Bone morphogenetic protein 4</span> Human protein and coding gene

Bone morphogenetic protein 4 is a protein that in humans is encoded by BMP4 gene. BMP4 is found on chromosome 14q22-q23.

<span class="mw-page-title-main">Bone morphogenetic protein 10</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 10 (BMP10) is a protein that in humans is encoded by the BMP10 gene.

<span class="mw-page-title-main">Bone morphogenetic protein 6</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 6 is a protein that in humans is encoded by the BMP6 gene.

<span class="mw-page-title-main">Bone morphogenetic protein 5</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein 5 is a protein that in humans is encoded by the BMP5 gene.

R-SMADs are receptor-regulated SMADs. SMADs are transcription factors that transduce extracellular TGF-β superfamily ligand signaling from cell membrane bound TGF-β receptors into the nucleus where they activate transcription TGF-β target genes. R-SMADS are directly phosphorylated on their c-terminus by type 1 TGF-β receptors through their intracellular kinase domain, leading to R-SMAD activation.

The transforming growth factor beta (TGFB) signaling pathway is involved in many cellular processes in both the adult organism and the developing embryo including cell growth, cell differentiation, cell migration, apoptosis, cellular homeostasis and other cellular functions. The TGFB signaling pathways are conserved. In spite of the wide range of cellular processes that the TGFβ signaling pathway regulates, the process is relatively simple. TGFβ superfamily ligands bind to a type II receptor, which recruits and phosphorylates a type I receptor. The type I receptor then phosphorylates receptor-regulated SMADs (R-SMADs) which can now bind the coSMAD SMAD4. R-SMAD/coSMAD complexes accumulate in the nucleus where they act as transcription factors and participate in the regulation of target gene expression.

<span class="mw-page-title-main">BMPR2</span> Protein-coding gene in the species Homo sapiens

Bone morphogenetic protein receptor type II or BMPR2 is a serine/threonine receptor kinase encoded by the BMPR2 gene. It binds bone morphogenetic proteins, members of the TGF beta superfamily of ligands, which are involved in paracrine signaling. BMPs are involved in a host of cellular functions including osteogenesis, cell growth and cell differentiation. Signaling in the BMP pathway begins with the binding of a BMP to the type II receptor. This causes the recruitment of a BMP type I receptor, which the type II receptor phosphorylates. The type I receptor phosphorylates an R-SMAD, a transcriptional regulator.

<span class="mw-page-title-main">BMPR1A</span> Bone morphogenetic protein receptor

The bone morphogenetic protein receptor, type IA also known as BMPR1A is a protein which in humans is encoded by the BMPR1A gene. BMPR1A has also been designated as CD292.

<span class="mw-page-title-main">Transforming growth factor beta superfamily</span> Protein family

The transforming growth factor beta (TGF-β) superfamily is a large group of structurally related cell regulatory proteins that was named after its first member, TGF-β1, originally described in 1983. They interact with TGF-beta receptors.

<span class="mw-page-title-main">GDF2</span> Protein-coding gene in the species Homo sapiens

Growth differentiation factor 2 (GDF2) also known as bone morphogenetic protein (BMP)-9 is a protein that in humans is encoded by the GDF2 gene. GDF2 belongs to the transforming growth factor beta superfamily.

<span class="mw-page-title-main">GDF3</span> Protein-coding gene in humans

Growth differentiation factor-3 (GDF3), also known as Vg-related gene 2 (Vgr-2) is protein that in humans is encoded by the GDF3 gene. GDF3 belongs to the transforming growth factor beta (TGF-β) superfamily. It has high similarity to other TGF-β superfamily members including Vg1 and GDF1.

<span class="mw-page-title-main">GDF5</span> Protein-coding gene in the species Homo sapiens

Growth/differentiation factor 5 is a protein that in humans is encoded by the GDF5 gene.

<span class="mw-page-title-main">GDF6</span> Protein-coding gene in the species Homo sapiens

Growth differentiation factor 6 (GDF6) is a protein that in humans is encoded by the GDF6 gene.

<span class="mw-page-title-main">GDF7</span> Protein-coding gene in the species Homo sapiens

Growth differentiation factor 7 (GDF7) is a protein that in humans is encoded by the GDF7 gene.

<span class="mw-page-title-main">GDF10</span> Protein-coding gene in the species Homo sapiens

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.

<span class="mw-page-title-main">GDF11</span> Protein-coding gene in humans

Growth differentiation factor 11 (GDF11) also known as bone morphogenetic protein 11 (BMP-11) is a protein that in humans is encoded by the growth differentiation factor 11 gene. GDF11 is a member of the Transforming growth factor beta family.

Gremlin is an inhibitor in the TGF beta signaling pathway. It primarily inhibits bone morphogenesis and is implicated in disorders of increased bone formation and several cancers.

<span class="mw-page-title-main">Transforming growth factor, beta 3</span> Protein-coding gene in the species Homo sapiens

Transforming growth factor beta-3 is a protein that in humans is encoded by the TGFB3 gene.

References

  1. ↑ Herpin A, Lelong C, Favrel P (2004). "Transforming growth factor-beta-related proteins: an ancestral and widespread superfamily of cytokines in metazoans". Dev Comp Immunol. 28 (5): 461–85. doi:10.1016/j.dci.2003.09.007. PMID   15062644.
  2. ↑ Rankin C, Bunton T, Lawler A, Lee S (2000). "Regulation of left-right patterning in mice by growth/differentiation factor-1". Nat Genet. 24 (3): 262–5. doi:10.1038/73472. PMID   10700179. S2CID   6787053.
  3. ↑ Lopez-Coviella I, Follettie M, Mellott T, Kovacheva V, Slack B, Diesl V, Berse B, Thies R, Blusztajn J (2005). "Bone morphogenetic protein 9 induces the transcriptome of basal forebrain cholinergic neurons". Proc Natl Acad Sci USA. 102 (19): 6984–9. Bibcode:2005PNAS..102.6984L. doi: 10.1073/pnas.0502097102 . PMC   1088172 . PMID   15870197.
  4. ↑ Truksa J, Peng H, Lee P, Beutler E (2006). "Bone morphogenetic proteins 2, 4, and 9 stimulate murine hepcidin 1 expression independently of Hfe, transferrin receptor 2 (Tfr2), and IL-6". Proc Natl Acad Sci USA. 103 (27): 10289–93. Bibcode:2006PNAS..10310289T. doi: 10.1073/pnas.0603124103 . PMC   1502450 . PMID   16801541.
  5. ↑ Levine A, Brivanlou A (2006). "GDF3 at the crossroads of TGF-beta signaling". Cell Cycle. 5 (10): 1069–73. doi: 10.4161/cc.5.10.2771 . PMID   16721050.
  6. ↑ Levine A, Brivanlou A (2006). "GDF3, a BMP inhibitor, regulates cell fate in stem cells and early embryos". Development. 133 (2): 209–16. doi:10.1242/dev.02192. PMID   16339188.
  7. ↑ Chen C, Ware S, Sato A, Houston-Hawkins D, Habas R, Matzuk M, Shen M, Brown C (2006). "The Vg1-related protein Gdf3 acts in a Nodal signaling pathway in the pre-gastrulation mouse embryo". Development. 133 (2): 319–29. doi:10.1242/dev.02210. PMID   16368929.
  8. ↑ O'Keeffe G, Dockery P, Sullivan A (2004). "Effects of growth/differentiation factor 5 on the survival and morphology of embryonic rat midbrain dopaminergic neurones in vitro". J Neurocytol. 33 (5): 479–88. doi:10.1007/s11068-004-0511-y. PMID   15906156. S2CID   25940876.
  9. ↑ Buxton P, Edwards C, Archer C, Francis-West P (2001). "Growth/differentiation factor-5 (GDF-5) and skeletal development". J Bone Joint Surg Am. 83-A Suppl 1 (Pt 1): S23–30. PMID   11263662.
  10. ↑ Francis-West P, Parish J, Lee K, Archer C (1999). "BMP/GDF-signalling interactions during synovial joint development". Cell Tissue Res. 296 (1): 111–9. doi:10.1007/s004410051272. PMID   10199971. S2CID   21942870.
  11. ↑ Chang C, Hemmati-Brivanlou A (1999). "Xenopus GDF6, a new antagonist of noggin and a partner of BMPs". Development. 126 (15): 3347–57. doi:10.1242/dev.126.15.3347. PMID   10393114.
  12. ↑ Asai-Coakwell M, French C, Berry K, Ye M, Koss R, Somerville M, Mueller R, van Heyningen V, Waskiewicz A, Lehmann O (2007). "GDF6, a novel locus for a spectrum of ocular developmental anomalies". American Journal of Human Genetics. 80 (2): 306–15. doi:10.1086/511280. PMC   1785352 . PMID   17236135.
  13. ↑ Hanel M, Hensey C (2006). "Eye and neural defects associated with loss of GDF6". BMC Dev Biol. 6: 43. doi: 10.1186/1471-213X-6-43 . PMC   1609107 . PMID   17010201.
  14. ↑ McPherron AC, Lawler AM, Lee SJ (May 1997). "Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member". Nature. 387 (6628): 83–90. doi:10.1038/387083a0. PMID   9139826. S2CID   4271945.
  15. ↑ Juengel J, Bodensteiner K, Heath D, Hudson N, Moeller C, Smith P, Galloway S, Davis G, Sawyer H, McNatty K (2004). "Physiology of GDF9 and BMP15 signalling molecules". Anim Reprod Sci . 82–83: 447–60. doi:10.1016/j.anireprosci.2004.04.021. PMID   15271472.
  16. ↑ Hreinsson J, Scott J, Rasmussen C, Swahn M, Hsueh A, Hovatta O (2002). "Growth differentiation factor-9 promotes the growth, development, and survival of human ovarian follicles in organ culture". J Clin Endocrinol Metab. 87 (1): 316–21. doi: 10.1210/jcem.87.1.8185 . PMID   11788667.
  17. ↑ Hino J, Kangawa K, Matsuo H, Nohno T, Nishimatsu S (2004). "Bone morphogenetic protein-3 family members and their biological functions". Front Biosci. 9 (1–3): 1520–9. doi: 10.2741/1355 . PMID   14977563.
  18. ↑ Cunningham N, Jenkins N, Gilbert D, Copeland N, Reddi A, Lee S (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.
  19. ↑ Andersson O, Reissmann E, Ibáñez C (2006). "Growth differentiation factor 11 signals through the transforming growth factor-beta receptor ALK5 to regionalize the anterior-posterior axis". EMBO Reports. 7 (8): 831–7. doi:10.1038/sj.embor.7400752. PMC   1525155 . PMID   16845371.
  20. ↑ Wu H, Ivkovic S, Murray R, Jaramillo S, Lyons K, Johnson J, Calof A (2003). "Autoregulation of neurogenesis by GDF11" (PDF). Neuron. 37 (2): 197–207. doi:10.1016/S0896-6273(02)01172-8. PMID   12546816. S2CID   15399794.
  21. ↑ Kim J, Wu H, Lander A, Lyons K, Matzuk M, Calof A (2005). "GDF11 controls the timing of progenitor cell competence in developing retina". Science. 308 (5730): 1927–30. Bibcode:2005Sci...308.1927K. doi:10.1126/science.1110175. PMID   15976303. S2CID   42002862.
  22. ↑ Zimmers T, Jin X, Hsiao E, McGrath S, Esquela A, Koniaris L (2005). "Growth differentiation factor-15/macrophage inhibitory cytokine-1 induction after kidney and lung injury". Shock. 23 (6): 543–8. PMID   15897808.
  23. ↑ Hsiao E, Koniaris L, Zimmers-Koniaris T, Sebald S, Huynh T, Lee S (2000). "Characterization of growth-differentiation factor 15, a transforming growth factor beta superfamily member induced following liver injury". Mol Cell Biol. 20 (10): 3742–51. doi:10.1128/MCB.20.10.3742-3751.2000. PMC   85678 . PMID   10779363.
  24. ↑ Ago T, Sadoshima J (2006). "GDF15, a cardioprotective TGF-beta superfamily protein". Circ Res. 98 (3): 294–7. doi: 10.1161/01.RES.0000207919.83894.9d . PMID   16484622.
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