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{{protein
{{infobox protein
|Name=neuromedin B
|Name=neuromedin B
|caption=
|caption=
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|LocusSupplementaryData=-qter
|LocusSupplementaryData=-qter
}}
}}
{{SI}}
'''Neuromedin B''' (NMB) is a [[bombesin]]-related [[peptide]] in mammals.<ref name="pmid10840151">{{cite journal | author = Ohki-Hamazaki H | title = Neuromedin B | journal = Prog. Neurobiol. | volume = 62 | issue = 3 | pages = 297–312 |date=October 2000 | pmid = 10840151 | doi = 10.1016/S0301-0082(00)00004-6 | url =  }}</ref><ref name="pmid18055507">{{cite journal |vauthors=Jensen RT, Battey JF, Spindel ER, Benya RV | title = International Union of Pharmacology. LXVIII. Mammalian bombesin receptors: nomenclature, distribution, pharmacology, signaling, and functions in normal and disease states | journal = Pharmacol. Rev. | volume = 60 | issue = 1 | pages = 1–42 |date=March 2008 | pmid = 18055507 | doi = 10.1124/pr.107.07108 | url = | pmc = 2517428  }}</ref> It was originally purified from pig spinal cord, and later shown to be present in human [[central nervous system]] and [[gastrointestinal tract]].<ref name="pmid2458345">{{cite journal |vauthors=Krane IM, Naylor SL, Helin-Davis D, Chin WW, Spindel ER | title = Molecular cloning of cDNAs encoding the human bombesin-like peptide neuromedin B. Chromosomal localization and comparison to cDNAs encoding its amphibian homolog ranatensin | journal = J. Biol. Chem. | volume = 263 | issue = 26 | pages = 13317–23 | date=15 September 1988| pmid = 2458345 | url = http://www.jbc.org/cgi/content/abstract/263/26/13317 | issn = }}</ref>


== Sequence ==
The sequence of the C-terminal decapeptide is highly conserved across mammalian species: GNLWATGHFM-(NH2); this decapeptide is sometimes noted as neuromedin B, but it is more accurately described as neuromedin B 23-32. The sequence of neuromedin B (in rat) is : TPFSWDLPEPRSRASKIRVHPRGNLWATGHFM-(NH2).<ref name="pmid2398368">{{cite journal |vauthors=Wada E, Way J, Lebacq-Verheyden AM, Battey JF | title = Neuromedin B and gastrin-releasing peptide mRNAs are differentially distributed in the rat nervous system | journal = J. Neurosci. | volume = 10 | issue = 9 | pages = 2917–30 | date=1 September 1990| pmid = 2398368 | url = http://www.jneurosci.org/cgi/content/abstract/10/9/2917 | issn = }}</ref>


'''Neuromedin B''' (NMB) is a [[bombesin]]-related [[peptide]] in mammals. It was originally purified from pig spinal cord, and later shown to be present in human [[central nervous system]] and [[gastrointestinal tract]].
== Function ==
[[Image:Gpcr2.JPG|thumb|'''Figure 1''': NMB, 7-TMR receptor and G-protein]]
[[Image:Gpcr+cycle.JPG|thumb|'''Figure 2''' : Signal Cascade after NMB binding]]
Neuromedin regulates the following functions:


== Functions of Neuromedin B ==
* [[exocrine gland|exocrine]] and [[endocrine system|endocrine]] secretions
* cell growth
* body temperature
* blood pressure and glucose level


Neuromedin has the following functions:
== Neuromedin signaling pathway ==


* (1) Regulation of exocrine and endocrine secretions
NMB acts by binding to its high affinity cell surface receptor, [[neuromedin B receptor]] (NMBR). This receptor is a [[G protein-coupled receptor]] with seven transmembrane spanning regions, hence the receptor is also denoted as a 7-transmembrane receptor (7-TMR). Upon binding several intracellular signaling pathways are triggered (see '''Figure 2''').
* (2) Regulation of cell growth
* (3) Regulation of body temperature
* (4) Regulation of blood pressure and glucose level


[[Image:Gpcr2.JPG|thumb|left|Figure 1: NMB, 7-TMR receptor and G-protein]]
When NMB binds to its 7-TMR, the [[heterotrimeric G protein]] that is attached to the receptor is activated. The G-protein is called heterotrimeric because it consists of 3 polypeptides: α subunit, β subunit, and γ subunit. In the activated NMBR/G-protein complex, there occurs an exchange of [[Guanosine triphosphate|GTP]] for [[Guanosine diphosphate|GDP]] bound to G-α subunit.  The G-α subunit, in turn, dissociated form the G-βγ subunits. The free G-α inactivates [[adenylate cyclase]] (AC), which, in turn, catalyzes the conversion of ATP to cAMP, the latter of which functioning as a [[second messenger]]. cAMP activates of the enzyme [[Protein Kinase A]] (PKA). PKA enters the nucleus and activates the [[CREB|cAMP response element-binding]] protein. The activated CREB binds along with [[CREB binding protein]], co-activator to the CRE region of the DNA in the nucleus. CREB and CBP are held together by [[leucine zipper]]s. CRE is the control that activates number of growth factors, and thus cell proliferation and some anti-apoptotic genes.  In the brain, CREB plays a role in long-term memory and learning.
[[Image:Gpcr%2Bcycle.JPG|thumb|left|Figure 2 : Signal Cascade after NMB binding]]
{{Clear}}


== Neuromedin Signaling Pathway ==
==References==
{{Reflist|2}}


NMB exerts it's effects by binding to a cell surface receptor. A high affinity receptor called the [[neuromedin B receptor]] (NMBR) has been identified. This receptor is a [[G protein-coupled receptor]] with seven transmembrane spanning regions, hence the receptor is also denoted as 7-TMR or 7 Transmembrane Receptor. Upon binding several intracellular signaling cascades are induced, which are mentioned below (see Figure 2 for signal cascade).
==External links==
 
* {{MeshName|Neuromedin+B}}
When NMB binds to 7-TMR, the heterotrimeric G-protein that is attached to the receptor gets
activated. The G-protein is called heterotrimeric because it consists of 3 polypeptides: α subunit, β subunit and γ subunit. Out of which '''G-β''' and '''G-γ subunits''' function as a monomer. And '''G-α''' has a [[GDP]] bound to it. When the NMB binds to 7-TMR, there occurs GTP exchange for GDP bound to G-α subunit and thus it gets activated, dissociates from the G-βγ. The activated G-α in turn activates [[adenylate cyclase]](AC) which in turn catalyzes the conversion of ATP to cAMP [[second messenger]]. cAMP helps in the activation of the enzyme [[Protein Kinase A]] (PKA). PKA enters the nucleus and activates the [[CREB|cAMP response element-binding]] protein. The activated CREB binds along with [[P300/CBP|CREB binding protein]], co-activator to the CRE region of the DNA in the nucleus. CREB and CBP are held together by [[leucine zipper]]s. CRE is the control that activates number of growth factors, and thus cell proliferation and some anti-apoptotic genes.In the brain, CREB plays a role in long-term memory and learning.


{{Neuropeptides}}


{{Neuropeptides}}
[[Category:Neuropeptides]]
[[Category:Neuropeptides]]
[[it:Neuromedina B]]
{{WH}}
{{WikiDoc Sources}}

Latest revision as of 12:37, 9 January 2019

neuromedin B
Identifiers
SymbolNMB
Entrez4828
HUGO7842
OMIM162340
RefSeqNM_021077
UniProtP08949
Other data
LocusChr. 15 q11-qter

Neuromedin B (NMB) is a bombesin-related peptide in mammals.[1][2] It was originally purified from pig spinal cord, and later shown to be present in human central nervous system and gastrointestinal tract.[3]

Sequence

The sequence of the C-terminal decapeptide is highly conserved across mammalian species: GNLWATGHFM-(NH2); this decapeptide is sometimes noted as neuromedin B, but it is more accurately described as neuromedin B 23-32. The sequence of neuromedin B (in rat) is : TPFSWDLPEPRSRASKIRVHPRGNLWATGHFM-(NH2).[4]

Function

Figure 1: NMB, 7-TMR receptor and G-protein
Figure 2 : Signal Cascade after NMB binding

Neuromedin regulates the following functions:

  • exocrine and endocrine secretions
  • cell growth
  • body temperature
  • blood pressure and glucose level

Neuromedin signaling pathway

NMB acts by binding to its high affinity cell surface receptor, neuromedin B receptor (NMBR). This receptor is a G protein-coupled receptor with seven transmembrane spanning regions, hence the receptor is also denoted as a 7-transmembrane receptor (7-TMR). Upon binding several intracellular signaling pathways are triggered (see Figure 2).

When NMB binds to its 7-TMR, the heterotrimeric G protein that is attached to the receptor is activated. The G-protein is called heterotrimeric because it consists of 3 polypeptides: α subunit, β subunit, and γ subunit. In the activated NMBR/G-protein complex, there occurs an exchange of GTP for GDP bound to G-α subunit. The G-α subunit, in turn, dissociated form the G-βγ subunits. The free G-α inactivates adenylate cyclase (AC), which, in turn, catalyzes the conversion of ATP to cAMP, the latter of which functioning as a second messenger. cAMP activates of the enzyme Protein Kinase A (PKA). PKA enters the nucleus and activates the cAMP response element-binding protein. The activated CREB binds along with CREB binding protein, co-activator to the CRE region of the DNA in the nucleus. CREB and CBP are held together by leucine zippers. CRE is the control that activates number of growth factors, and thus cell proliferation and some anti-apoptotic genes. In the brain, CREB plays a role in long-term memory and learning.

References

  1. Ohki-Hamazaki H (October 2000). "Neuromedin B". Prog. Neurobiol. 62 (3): 297–312. doi:10.1016/S0301-0082(00)00004-6. PMID 10840151.
  2. Jensen RT, Battey JF, Spindel ER, Benya RV (March 2008). "International Union of Pharmacology. LXVIII. Mammalian bombesin receptors: nomenclature, distribution, pharmacology, signaling, and functions in normal and disease states". Pharmacol. Rev. 60 (1): 1–42. doi:10.1124/pr.107.07108. PMC 2517428. PMID 18055507.
  3. Krane IM, Naylor SL, Helin-Davis D, Chin WW, Spindel ER (15 September 1988). "Molecular cloning of cDNAs encoding the human bombesin-like peptide neuromedin B. Chromosomal localization and comparison to cDNAs encoding its amphibian homolog ranatensin". J. Biol. Chem. 263 (26): 13317–23. PMID 2458345.
  4. Wada E, Way J, Lebacq-Verheyden AM, Battey JF (1 September 1990). "Neuromedin B and gastrin-releasing peptide mRNAs are differentially distributed in the rat nervous system". J. Neurosci. 10 (9): 2917–30. PMID 2398368.

External links