Bombezin

Bombezin
Drugi nazivi Pyr-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val-Gly-His-Leu-Met-NH2
Identifikacija
CAS registarski broj 31362-50-2
PubChem[1][2] 16133891
IUPHAR ligand 616
InChI

InChI=1S/C71H110N24O18S/c1-34(2)24-47(92-62(105)43(14-11-22-79-71(76)77)89-64(107)45(15-18-52(72)96)90-63(106)44-17-20-55(99)85-44)61(104)80-31-56(100)87-51(29-54(74)98)69(112)91-46(16-19-53(73)97)65(108)94-50(27-39-26-38-12-9-10-13-41(38)84-39)66(109)83-37(7)60(103)95-58(36(5)6)70(113)81-32-57(101)86-49(28-40-30-78-33-82-40)68(111)93-48(25-35(3)4)67(110)88-42(59(75)102)21-23-114-8/h9-10,12-13,26,30,33-37,42-51,58,84H,11,14-25,27-29,31-32H2,1-8H3,(H2,72,96)(H2,73,97)(H2,74,98)(H2,75,102)(H,78,82)(H,80,104)(H,81,113)(H,83,109)(H,85,99)(H,86,101)(H,87,100)(H,88,110)(H,89,107)(H,90,106)(H,91,112)(H,92,105)(H,93,111)(H,94,108)(H,95,103)(H4,76,77,79)/t37-,42-,43-,44-,45-,46-,47-,48-,49-,50-,51-,58-/m0/s1 DaY
Kod: DNDCVAGJPBKION-DOPDSADYSA-N DaY

Svojstva
Molekulska formula C71H110N24O18S
Molarna masa 1619.85



Ukoliko nije drugačije napomenuto, podaci se odnose na standardno stanje (25 °C, 100 kPa) materijala

Infobox references

Bombezin je peptid sa 14-aminokiselina[3], koji je originalno izolovan iz kože žabe. On ima dva poznata homologa kod sisara koji se nazivaju neuromedin B i peptid oslobađanja gastrina.

Bombezin stimuliše oslobađanje gastrina i G ćelija. On aktivira tri različita G protein spregnuta receptora, koji su poznati kao BBR1 2 & 3.[4] On takođe aktivira te receptore u mozgu. Zajedno sa holecistokininom, on je drugi najveći izvor negativnog povratnog signala koji zaustavlja traženje hrane.[5]

Bombezin je takođe marker tumora za rak malih ćelija pluća, gastričnog karcinoma, i neuroblastoma.[6]

Povezano

Reference

  1. ↑ Li Q, Cheng T, Wang Y, Bryant SH (2010). „PubChem as a public resource for drug discovery.”. Drug Discov Today 15 (23-24): 1052-7. DOI:10.1016/j.drudis.2010.10.003. PMID 20970519.  edit
  2. ↑ Evan E. Bolton, Yanli Wang, Paul A. Thiessen, Stephen H. Bryant (2008). „Chapter 12 PubChem: Integrated Platform of Small Molecules and Biological Activities”. Annual Reports in Computational Chemistry 4: 217-241. DOI:10.1016/S1574-1400(08)00012-1. 
  3. ↑ Gonzalez N, Moody TW, Igarashi H, Ito T, Jensen RT (February 2008). „Bombesin-related peptides and their receptors: recent advances in their role in physiology and disease states”. Current Opinion in Endocrinology, Diabetes, and Obesity 15 (1): 58–64. DOI:10.1097/MED.0b013e3282f3709b. PMC 2631407. PMID 18185064. 
  4. ↑ Weber HC (February 2009). „Regulation and signaling of human bombezin receptors and their biological effects”. Current Opinion in Endocrinology, Diabetes, and Obesity 16 (1): 66–71. PMID 19115523. 
  5. ↑ Yamada K, Wada E, Wada K (November 2000). „Bombesin-like peptides: studies on food intake and social behaviour with receptor knock-out mice”. Annals of Medicine 32 (8): 519–29. PMID 11127929. 
  6. ↑ Ohlsson B, Fredäng N, Axelson J (December 1999). „The effect of bombesin, cholecystokinin, gastrin, and their antagonists on proliferation of pancreatic cancer cell lines”. Scandinavian Journal of Gastroenterology 34 (12): 1224–9. PMID 10636070. 

Spoljašnje veze

Portal Hemija
  • p
  • r
  • u
Hormoni
vidi hormoni
Opioidni peptidi
Drugi
Drugi neuropeptidi
Kinini
Neuromedini
B • N • S • U
Drugi
B trdu: peptidi (nrpl/grfl/cytl/horl), receptori (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd, signalni putevi (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)