Developmental Signals - Bone Morphogenetic Protein

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Introduction

Belongs to the transforming growth factor-beta (TGFB) superfamily, humans have 15 members in this protein signaling family. The proteins are synthesized as prepropeptides, then cleaved, and processed into dimeric proteins.


TGFB family members: TGFB1, TGFB, TGFB3, bone morphogenetic proteins Bmp-2A, Bmp-2B, Bmp-3, and Bmp-6. mullerian inhibitory substance.

Mouse Bmp4 expression face 01.jpg

Mouse Bmp4 expression face.[1]


BMP Mouse Links: Face and limb E9.5-13.5 | Face E9.5-13.5 | Body E11.0 | Body E11.5 | BMP | Mouse Development

Growth Differentiation Factor-6 (Gdf6) is a member of the Bone Morphogenetic Protein (BMP) family of secreted signaling molecules.

Factor Links: AMH | hCG | BMP | sonic hedgehog | bHLH | HOX | FGF | FOX | Hippo | LIM | Nanog | NGF | Nodal | Notch | PAX | retinoic acid | SIX | Slit2/Robo1 | SOX | TBX | TGF-beta | VEGF | WNT | Category:Molecular

Some Recent Findings

  • BMP and FGF signaling interact to pattern mesoderm by controlling basic helix-loop-helix transcription factor activity[2] "The mesodermal germ layer is patterned into mediolateral subtypes by signaling factors including BMP and FGF. How these pathways are integrated to induce specific mediolateral cell fates is not well understood. We used mesoderm derived from post-gastrulation neuromesodermal progenitors (NMPs), which undergo a binary mediolateral patterning decision, as a simplified model to understand how FGF acts together with BMP to impart mediolateral fate. Using zebrafish and mouse NMPs, we identify an evolutionarily conserved mechanism of BMP and FGF mediated mediolateral mesodermal patterning that occurs through modulation of basic helix-loop-helix (bHLH) transcription factor activity. BMP imparts lateral fate through induction of Id helix loop helix (HLH) proteins, which antagonize bHLH transcription factors, induced by FGF signaling, that specify medial fate. We extend our analysis of zebrafish development to show that bHLH activity is responsible for the mediolateral patterning of the entire mesodermal germ layer."
  • Bone morphogenetic protein 4 promotes craniofacial neural crest induction from human pluripotent stem cells[3] "Neural crest (NC) cells are a group of cells located in the neural folds at the boundary between the neural and epidermal ectoderm. Cranial NC cells migrate to the branchial arches and give rise to the majority of the craniofacial region, whereas trunk and tail NC cells contribute to the heart, enteric ganglia of the gut, melanocytes, sympathetic ganglia, and adrenal chromaffin cells. ...These BMP4-treated NC cells were capable of differentiation into osteocytes and chondrocytes. The results of the present study indicate that BMP4 regulates cranial positioning during NC development." Neural Crest Development
  • Review - Embryo Development. Bmp Gradients[4] "Bone morphogenetic proteins (BMPs) act in dose-dependent fashion to regulate cell fate choices in a myriad of developmental contexts. In early vertebrate and invertebrate embryos, BMPs and their antagonists establish epidermal versus central nervous system domains. In this highly conserved system, BMP antagonists mediate the neural-inductive activities proposed by Hans Spemann and Hilde Mangold nearly a century ago. BMPs distributed in gradients subsequently function as morphogens to subdivide the three germ layers into distinct territories and act to organize body axes, regulate growth, maintain stem cell niches, or signal inductively across germ layers. In this Review, we summarize the variety of mechanisms that contribute to generating reliable developmental responses to BMP gradients and other morphogen systems."
  • Construction of a vertebrate embryo from two opposing morphogen gradients[5] "Here, we show that opposing gradients of bone morphogenetic protein (BMP) and Nodal, two transforming growth factor family members that act as morphogens, are sufficient to induce molecular and cellular mechanisms required to organize, in vivo or in vitro, uncommitted cells of the zebrafish blastula animal pole into a well-developed embryo." Zebrafish Development
  • Developmental stalling and organ-autonomous regulation of morphogenesis[6] "Timing of organ development during embryogenesis is coordinated such that at birth, organ and fetal size and maturity are appropriately proportioned. The extent to which local developmental timers are integrated with each other and with the signaling interactions that regulate morphogenesis to achieve this end is not understood. Using the absolute requirement for a signaling pathway activity (bone morphogenetic protein, BMP) during a critical stage of tooth development, we show that suboptimal levels of BMP signaling do not lead to abnormal morphogenesis, as suggested by mutants affecting BMP signaling, but to a 24-h stalling of the intrinsic developmental clock of the tooth. During this time, BMP levels accumulate to reach critical levels whereupon tooth development restarts, accelerates to catch up with development of the rest of the embryo and completes normal morphogenesis. This suggests that individual organs can autonomously control their developmental timing to adjust their stage of development to that of other organs. We also find that although BMP signaling is critical for the bud-to-cap transition in all teeth, levels of BMP signaling are regulated differently in multicusped teeth. We identify an interaction between two homeodomain transcription factors, Barx1 and Msx1, which is responsible for setting critical levels of BMP activity in multicusped teeth and provides evidence that correlates the levels of Barx1 transcriptional activity with cuspal complexity. This study highlights the importance of absolute levels of signaling activity for development and illustrates remarkable self-regulation in organogenesis that ensures coordination of developmental processes such that timing is subordinate to developmental structure."
More recent papers  
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Search term: Bone Morphogenetic Protein

<pubmed limit=5>Bone Morphogenetic Protein</pubmed>

Human BMP Family

Table - Human Bmp Family
Approved
Symbol
Approved Name Previous
Symbols
Synonyms Chromosome
BMP1 bone morphogenetic protein 1 PCOLC 8p21.3
BMP2 bone morphogenetic protein 2 BMP2A 20p12.3
BMP3 bone morphogenetic protein 3 4q21.21
BMP4 bone morphogenetic protein 4 BMP2B 14q22.2
BMP5 bone morphogenetic protein 5 6p12.1
BMP6 bone morphogenetic protein 6 VGR VGR1 6p24.3
BMP7 bone morphogenetic protein 7 OP-1 20q13.31
BMP8A bone morphogenetic protein 8a 1p34.3
BMP8B bone morphogenetic protein 8b BMP8 OP-2 1p34.2
BMP10 bone morphogenetic protein 10 2p13.3
BMP15 bone morphogenetic protein 15 GDF9B Xp11.22
    Links: Developmental Signals - Bone Morphogenetic Protein | OMIM BMP2 | HGNC | Bmp Family | Sox Family | Tbx Family


Human BMP Family  
Table - Human Bmp Family
Approved
Symbol
Approved Name Previous
Symbols
Synonyms Chromosome
BMP1 bone morphogenetic protein 1 PCOLC 8p21.3
BMP2 bone morphogenetic protein 2 BMP2A 20p12.3
BMP3 bone morphogenetic protein 3 4q21.21
BMP4 bone morphogenetic protein 4 BMP2B 14q22.2
BMP5 bone morphogenetic protein 5 6p12.1
BMP6 bone morphogenetic protein 6 VGR VGR1 6p24.3
BMP7 bone morphogenetic protein 7 OP-1 20q13.31
BMP8A bone morphogenetic protein 8a 1p34.3
BMP8B bone morphogenetic protein 8b BMP8 OP-2 1p34.2
BMP10 bone morphogenetic protein 10 2p13.3
BMP15 bone morphogenetic protein 15 GDF9B Xp11.22
    Links: Developmental Signals - Bone Morphogenetic Protein | OMIM BMP2 | HGNC | Bmp Family | Sox Family | Tbx Family

Structure

BMP Superfamily Canonical Signalling
BMP superfamily canonical signalling.jpg
Over 30 bone morphogenetic protein (BMP) superfamily ligands have been discovered in humans. Most are secreted as mature disulfide-linked dimers, with the exception of TGF-β1, TGF-β2 and TGF-β3, which can be secreted in a latent form and require proteolytic activation. BMPs signal through a multimeric cell surface complex consisting of two type I receptors and two type II receptors.


Type I and type II BMP receptors are single pass transmembrane proteins with an intracellular serine/threonine kinase domain. After ligand binding, type II receptors phosphorylate (P) the type I receptors.

Activated type I receptors recruit and phosphorylate pathway-specific R-SMADs (SMAD1, SMAD5 and SMAD8 (blue pathway), and SMAD2 and SMAD3 (orange pathway)), which can form trimers with SMAD4 and translocate to the nucleus. SMADs have intrinsic DNA-binding activity and are able to regulate gene expression by recruitment of chromatin-remodelling machinery and integration with tissue-specific transcription factors. SMAD8 is also known as SMAD9.

The pathway can be antagonized by many mechanisms including neutralization of ligands by secreted traps such as noggin or follistatin, secretion of latent ligands bound to their propeptides, or via titration of receptors by nonsignalling ligands such as BMP3, activin β/inhibin α dimers or LEFTY monomers.

  • ACVR - activin receptor
  • ALK - activin receptor-like kinase
  • AMH - anti-Müllerian hormone
  • AMHR2 - AMH receptor 2
  • BMPR - BMP receptor
  • GDF - growth/differentiation factor
  • TGF - transforming growth factor
  • TGFBR - TGF-β receptor


Figure from recent BMP review.[7]

Gene

Function

Mouse Bmp4 expression limb and face 01.jpg

Mouse Bmp4 expression limb and face.[1]

Mouse face Bmp4 icon.jpg
 ‎‎Mouse Face Bmp4
Page | Play

Neural Development

During gastrulation the BMP pathway is antagonised and involved with neural induction. Neural induction signaling through the BMP-regulated Smad1/5 proteins appears to be controlled by fibroblast growth factor (FGF)-regulated Ca2+ entry activating calcineurin (CaN) that in turn dephosphorylates Smad1/5 proteins.[8]


Links: Neural Development

Oocyte Development

Ovarian follicle molecular interactions Bovine ovarian follicle BMP15 and GDF9
Molecular paracrine interactions involving BMP15 signaling[9] Localization of BMP15 in calf and cow follicles[10]
Links: Oocyte Development

Limb Development

Bmp2, Bmp4 and Bmp7 are co-required in the mouse AER for normal digit patterning but not limb outgrowth[11]

"Outgrowth and patterning of the vertebrate limb requires a functional apical ectodermal ridge (AER). The AER is a thickening of ectodermal tissue located at the distal end of the limb bud. Loss of this structure, either through genetic or physical manipulations results in truncation of the limb. A number of genes, including Bmps, are expressed in the AER. Previously, it was shown that removal of the BMP receptor Bmpr1a specifically from the AER resulted in complete loss of hindlimbs suggesting that Bmp signaling in the AER is required for limb outgrowth. In this report, we genetically removed the three known AER-expressed Bmp ligands, Bmp2, Bmp4 and Bmp7 from the AER of the limb bud using floxed conditional alleles and the Msx2-cre allele. Surprisingly, only defects in digit patterning and not limb outgrowth were observed. In triple mutants, the anterior and posterior AER was present but loss of the central region of the AER was observed. These data suggest that Bmp ligands expressed in the AER are not required for limb outgrowth but instead play an essential role in maintaining the AER and patterning vertebrate digits."

Limb AER BMP expression01.jpg


Links: Limb Development

Blood Vessel Development

BMP/SMAD signaling pathway regulates angiogenic sprouting and is involved in embryo vascular development.


Signaling Pathway

Identified BMP modulators:[12] Noggin, Chordin, Chordin-like 1, Chordin-like 2, Twisted gastrulation, Dan, BMPER, Sost, Sostdc1, Follistatin, Follistatin-like 1, Follistatin-like 5 and Tolloid.

Receptor

Intracellular Signaling

SNW-domain containing protein 1

(SNW1, SKI-INTERACTING PROTEIN; SKIIP)

A protein that interacts with nuclear receptors and enhances ligand-activated transcription, also called a nuclear receptor co-activator.


Regulator of Spatial BMP Activity, Neural Plate Border Formation, and Neural Crest Specification in Vertebrate Embryos[13]

"Bone morphogenetic protein (BMP) gradients provide positional information to direct cell fate specification, such as patterning of the vertebrate ectoderm into neural, neural crest, and epidermal tissues, with precise borders segregating these domains. However, little is known about how BMP activity is regulated spatially and temporally during vertebrate development to contribute to embryonic patterning, and more specifically to neural crest formation. Through a large-scale in vivo functional screen in Xenopus for neural crest fate, we identified an essential regulator of BMP activity, SNW1. SNW1 is a nuclear protein known to regulate gene expression. Using antisense morpholinos to deplete SNW1 protein in both Xenopus and zebrafish embryos, we demonstrate that dorsally expressed SNW1 is required for neural crest specification, and this is independent of mesoderm formation and gastrulation morphogenetic movements. By exploiting a combination of immunostaining for phosphorylated Smad1 in Xenopus embryos and a BMP-dependent reporter transgenic zebrafish line, we show that SNW1 regulates a specific domain of BMP activity in the dorsal ectoderm at the neural plate border at post-gastrula stages. We use double in situ hybridizations and immunofluorescence to show how this domain of BMP activity is spatially positioned relative to the neural crest domain and that of SNW1 expression. Further in vivo and in vitro assays using cell culture and tissue explants allow us to conclude that SNW1 acts upstream of the BMP receptors. Finally, we show that the requirement of SNW1 for neural crest specification is through its ability to regulate BMP activity, as we demonstrate that targeted overexpression of BMP to the neural plate border is sufficient to restore neural crest formation in Xenopus SNW1 morphants. We conclude that through its ability to regulate a specific domain of BMP activity in the vertebrate embryo, SNW1 is a critical regulator of neural plate border formation and thus neural crest specification."

Additional Images

OMIM

About OMIM "Online Mendelian Inheritance in Man OMIM is a comprehensive, authoritative, and timely compendium of human genes and genetic phenotypes. The full-text, referenced overviews in OMIM contain information on all known mendelian disorders and over 12,000 genes. OMIM focuses on the relationship between phenotype and genotype. It is updated daily, and the entries contain copious links to other genetics resources." OMIM


Links: OMIM300247

Abnormalities

Infertility

Selected Female Infertility Genes
Gene
abbreviation
Name Gene Location Online Mendelian
Inheritance in Man (OMIM)
HUGO Gene Nomenclature
Committee (HGNC)
GeneCards (GCID) Diagnosis
BMP15 Bone morphogenetic protein 15 Xp11.22 300247 1068 GC0XP050910 Primary ovarian insufficiency
  
  Table data source[14] (table 1)    Links: fertilization | oocyte | ovary | | Female Infertility Genes | spermatozoa | testis | Male Infertility Genes | Genetic Abnormalities | ART

 Primary ovarian insufficiency - depletion or dysfunction of ovarian follicles with cessation of menses before age 40 years.

Female Infertility Genes  
Selected Female Infertility Genes
Gene abbreviation Name Gene Location Online Mendelian
Inheritance in Man (OMIM)
HUGO Gene Nomenclature
Committee (HGNC)
GeneCards (GCID) Diagnosis
BMP15 Bone morphogenetic protein 15 Xp11.22 300247 1068 GC0XP050910 Primary ovarian insufficiency
CLPP Caseinolytic mitochondrial matrix peptidase proteolytic subunit 19p13.3 601119 2084 GC19P006369 Primary ovarian insufficiency
EIF2B2 Eukaryotic translation initiation factor 2B subunit beta 14q24.3 606454 3258 GC14P075002 Primary ovarian insufficiency
FIGLA Folliculogenesis-specific BHLH transcription factor 2p13.3 608697 24669 GC02M070741 Primary ovarian insufficiency
FMR1 Fragile X mental retardation 1 Xq27.3 309550 3775 GC0XP147912 Primary ovarian insufficiency
FOXL2 Forkhead box L2 3q22.3 605597 1092 GC03M138944 Primary ovarian insufficiency
FSHR Follicle stimulating hormone receptor 2p16.3 136435 3969 GC02M048866 Primary ovarian insufficiency
GALT Galactose-1-phosphate uridylyltransferase 9p13.3 606999 4135 GC09P034636 Primary ovarian insufficiency
GFD9 Growth differentiation factor 9 5q31.1 601918 4224 GC05M132861 Primary ovarian insufficiency
HARS2 Histidyl-TRNA synthetase 2, mitochondrial 5q31.3 600783 4817 GC05P141975 Primary ovarian insufficiency
HFM1 HFM1, ATP-dependent DNA helicase homolog 1p22.2 615684 20193 GC01M091260 Primary ovarian insufficiency
HSD17B4 Hydroxysteroid 17-beta dehydrogenase 4 5q23.1 601860 5213 GC05P119452 Primary ovarian insufficiency
LARS2 Leucyl-TRNA synthetase 2, mitochondrial 3p21.31 604544 17095 GC03P045405 Primary ovarian insufficiency
LHCGR Luteinizing hormone/choriogonadotropin receptor 2p16.3 152790 6585 GC02M048647 Primary ovarian insufficiency
LHX8 LIM homeobox 8 1p31.1 604425 28838 GC01P075128 Primary ovarian insufficiency
MCM8 Minichromosome maintenance 8 homologous recombination repair factor 20p12.3 608187 16147 GC20P005926 Primary ovarian insufficiency
MCM9 Minichromosome maintenance 9 homologous recombination repair factor 6q22.31 610098 21484 GC06M118813 Primary ovarian insufficiency
NOBOX NOBOX oogenesis homeobox 7q35 610934 22448 GC07M144397 Primary ovarian insufficiency
NOG Noggin 17q22 602991 7866 GC17P056593 Primary ovarian insufficiency
PMM2 Phosphomannomutase 2 16p13.2 601785 9115 GC16P008788 Primary ovarian insufficiency
POLG DNA polymerase gamma, catalytic subunit 15q26.1 174763 9179 GC15M089316 Primary ovarian insufficiency
REC8 REC8 meiotic recombination protein 14q12 608193 16879 GC14P024171 Primary ovarian insufficiency
SMC1B Structural maintenance of chromosomes 1B 22q13.31 608685 11112 GC22M045344 Primary ovarian insufficiency
SOHLH1 Spermatogenesis and oogenesis-specific basic helix–loop–helix 1 9q34.3 610224 27845 GC09M135693 Primary ovarian insufficiency
STAG3 Stromal antigen 3 7q22.1 {{Chr 608489 11356 GC07P100177 Primary ovarian insufficiency
SYCE1 Synaptonemal Complex Central Element Protein 1 10q26.3 611486 28852 GC10M133553 Primary ovarian insufficiency
TLE6 Transducin-like enhancer of split 6 19p13.3 612399 30788 GC19P002976 Embryonic lethalithy
TUBB8 Tubulin beta 8 Class VIII 10p15.3 616768 20773 GC10M000048 Oocyte maturation arrest
TWNK Twinkle MtDNA helicase 10q24.31 606075 1160 GC10P100991 Primary ovarian insufficiency
  Table data source[14] (table 1)    Links: fertilization | oocyte | ovary | | Female Infertility Genes | spermatozoa | testis | Male Infertility Genes | Genetic Abnormalities | ART

 Primary ovarian insufficiency - depletion or dysfunction of ovarian follicles with cessation of menses before age 40 years.
 Oocyte maturation arrest - arrest of human oocytes may occur at different stages of meiosis.

References

  1. 1.0 1.1 Jumlongras D, Lachke SA, O'Connell DJ, Aboukhalil A, Li X, Choe SE, Ho JW, Turbe-Doan A, Robertson EA, Olsen BR, Bulyk ML, Amendt BA & Maas RL. (2012). An evolutionarily conserved enhancer regulates Bmp4 expression in developing incisor and limb bud. PLoS ONE , 7, e38568. PMID: 22701669 DOI.
  2. Row RH, Pegg A, Kinney B, Farr GH, Maves L, Lowell S, Wilson V & Martin BL. (2018). BMP and FGF signaling interact to pattern mesoderm by controlling basic helix-loop-helix transcription factor activity. Elife , 7, . PMID: 29877796 DOI.
  3. Mimura S, Suga M, Okada K, Kinehara M, Nikawa H & Furue MK. (2016). Bone morphogenetic protein 4 promotes craniofacial neural crest induction from human pluripotent stem cells. Int. J. Dev. Biol. , 60, 21-8. PMID: 26934293 DOI.
  4. Bier E & De Robertis EM. (2015). EMBRYO DEVELOPMENT. BMP gradients: A paradigm for morphogen-mediated developmental patterning. Science , 348, aaa5838. PMID: 26113727 DOI.
  5. Xu PF, Houssin N, Ferri-Lagneau KF, Thisse B & Thisse C. (2014). Construction of a vertebrate embryo from two opposing morphogen gradients. Science , 344, 87-9. PMID: 24700857 DOI.
  6. Miletich I, Yu WY, Zhang R, Yang K, Caixeta de Andrade S, Pereira SF, Ohazama A, Mock OB, Buchner G, Sealby J, Webster Z, Zhao M, Bei M & Sharpe PT. (2011). Developmental stalling and organ-autonomous regulation of morphogenesis. Proc. Natl. Acad. Sci. U.S.A. , 108, 19270-5. PMID: 22084104 DOI.
  7. Salazar VS, Gamer LW & Rosen V. (2016). BMP signalling in skeletal development, disease and repair. Nat Rev Endocrinol , 12, 203-21. PMID: 26893264 DOI.
  8. Cho A, Tang Y, Davila J, Deng S, Chen L, Miller E, Wernig M & Graef IA. (2014). Calcineurin signaling regulates neural induction through antagonizing the BMP pathway. Neuron , 82, 109-124. PMID: 24698271 DOI.
  9. Chronowska E. (2014). High-throughput analysis of ovarian granulosa cell transcriptome. Biomed Res Int , 2014, 213570. PMID: 24711992 DOI.
  10. Hosoe M, Kaneyama K, Ushizawa K, Hayashi KG & Takahashi T. (2011). Quantitative analysis of bone morphogenetic protein 15 (BMP15) and growth differentiation factor 9 (GDF9) gene expression in calf and adult bovine ovaries. Reprod. Biol. Endocrinol. , 9, 33. PMID: 21401961 DOI.
  11. Choi KS, Lee C, Maatouk DM & Harfe BD. (2012). Bmp2, Bmp4 and Bmp7 are co-required in the mouse AER for normal digit patterning but not limb outgrowth. PLoS ONE , 7, e37826. PMID: 22662233 DOI.
  12. Lorda-Diez CI, Montero JA, Rodriguez-Leon J, Garcia-Porrero JA & Hurle JM. (2013). Expression and functional study of extracellular BMP antagonists during the morphogenesis of the digits and their associated connective tissues. PLoS ONE , 8, e60423. PMID: 23573253 DOI.
  13. Wu MY, Ramel MC, Howell M & Hill CS. (2011). SNW1 is a critical regulator of spatial BMP activity, neural plate border formation, and neural crest specification in vertebrate embryos. PLoS Biol. , 9, e1000593. PMID: 21358802 DOI.
  14. 14.0 14.1 Harper JC, Aittomäki K, Borry P, Cornel MC, de Wert G, Dondorp W, Geraedts J, Gianaroli L, Ketterson K, Liebaers I, Lundin K, Mertes H, Morris M, Pennings G, Sermon K, Spits C, Soini S, van Montfoort APA, Veiga A, Vermeesch JR, Viville S & Macek M. (2018). Recent developments in genetics and medically assisted reproduction: from research to clinical applications. Eur. J. Hum. Genet. , 26, 12-33. PMID: 29199274 DOI.

Reviews

Schliermann A & Nickel J. (2018). Unraveling the Connection between Fibroblast Growth Factor and Bone Morphogenetic Protein Signaling. Int J Mol Sci , 19, . PMID: 30340367 DOI.

Salazar VS, Gamer LW & Rosen V. (2016). BMP signalling in skeletal development, disease and repair. Nat Rev Endocrinol , 12, 203-21. PMID: 26893264 DOI.

Bier E & De Robertis EM. (2015). EMBRYO DEVELOPMENT. BMP gradients: A paradigm for morphogen-mediated developmental patterning. Science , 348, aaa5838. PMID: 26113727 DOI.

Jain AP, Pundir S & Sharma A. (2013). Bone morphogenetic proteins: The anomalous molecules. J Indian Soc Periodontol , 17, 583-6. PMID: 24174749 DOI.

Ruschke K, Hiepen C, Becker J & Knaus P. (2012). BMPs are mediators in tissue crosstalk of the regenerating musculoskeletal system. Cell Tissue Res. , 347, 521-44. PMID: 22327483 DOI.

Gazzerro E & Canalis E. (2006). Bone morphogenetic proteins and their antagonists. Rev Endocr Metab Disord , 7, 51-65. PMID: 17029022 DOI.

Chen D, Zhao M & Mundy GR. (2004). Bone morphogenetic proteins. Growth Factors , 22, 233-41. PMID: 15621726 DOI.

Articles

Cho A, Tang Y, Davila J, Deng S, Chen L, Miller E, Wernig M & Graef IA. (2014). Calcineurin signaling regulates neural induction through antagonizing the BMP pathway. Neuron , 82, 109-124. PMID: 24698271 DOI.

Luo YJ & Su YH. (2012). Opposing nodal and BMP signals regulate left-right asymmetry in the sea urchin larva. PLoS Biol. , 10, e1001402. PMID: 23055827 DOI.

Kuypers E, Collins JJ, Jellema RK, Wolfs TG, Kemp MW, Nitsos I, Pillow JJ, Polglase GR, Newnham JP, Germeraad WT, Kallapur SG, Jobe AH & Kramer BW. (2012). Ovine fetal thymus response to lipopolysaccharide-induced chorioamnionitis and antenatal corticosteroids. PLoS ONE , 7, e38257. PMID: 22693607 DOI.

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Cite this page: Hill, M.A. (2018, December 18) Embryology Developmental Signals - Bone Morphogenetic Protein. Retrieved from https://embryology.med.unsw.edu.au/embryology/index.php/Developmental_Signals_-_Bone_Morphogenetic_Protein

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