Pancreatic polypeptide: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{SIB}} +, -{{EH}} +, -{{EJ}} +, -{{Editor Help}} +, -{{Editor Join}} +))
 
imported>Jondr21
mNo edit summary
 
(One intermediate revision by one other user not shown)
Line 1: Line 1:
{{protein
{{distinguish|Pancreatic hormone}}
| Name = pancreatic polypeptide
{{More citations needed|date=June 2015}}
| caption =  
{{infobox protein
| image =  
| Name = Pancreatic polypeptide
| width =  
| caption =
| image = Pancreatic hormone 1TZ5.png
| width =
| HGNCid = 9327
| HGNCid = 9327
| Symbol = PPY
| Symbol = PPY
| AltSymbols =  
| AltSymbols =
| EntrezGene = 5539
| EntrezGene = 5539
| OMIM = 167780
| OMIM = 167780
| RefSeq = NM_002722
| RefSeq = NM_002722
| UniProt = P01298
| UniProt = P01298
| PDB =  
| PDB =
| ECnumber =  
| ECnumber =
| Chromosome = 17
| Chromosome = 17
| Arm = p
| Arm = p
Line 18: Line 20:
| LocusSupplementaryData = -qter
| LocusSupplementaryData = -qter
}}
}}
{{SI}}
[[File:PancreaticPolypeptide.jpg|thumb|IHC for Pancreatic polypeptide in a mouse pancreas, 200×]]
{{GS}}
'''Pancreatic polypeptide''' ('''PP''') is a [[polypeptide]] secreted by [[PP cell]]s in the [[endocrine pancreas]] predominantly in the [[head of the pancreas]]. It consists of 36 [[amino acids]] and has molecular weight about 4200 [[Dalton (unit)|Da]].<ref>{{cite journal |journal=Arch. Surg. |date=Oct 1981 |volume=116 |issue=10 |pages=1256–64 |title=Pancreatic polypeptide |vauthors=Lonovics J, Devitt P, Watson LC, Rayford PL, Thompson JC |pmid=7025798 |doi=10.1001/archsurg.1981.01380220010002}}</ref>


The function of PP is to self-regulate pancreatic secretion activities (endocrine and exocrine). It also has effects on hepatic [[glycogen]] levels and gastrointestinal secretions.


Its secretion in humans is increased after a protein meal, [[fasting]], exercise, and acute [[hypoglycemia]], and is decreased by [[somatostatin]] and intravenous [[glucose]].


'''Pancreatic polypeptide''' is a [[polypeptide]] secreted by [[PP cell]]s in the [[endocrine pancreas]] predominantly in the [[head of the pancreas]]. It consists of 36 [[amino acids]] and has molecular weight about 4200 Da.  
Plasma PP has been shown to be reduced in conditions associated with increased food intake and elevated in [[anorexia nervosa]]. In addition, peripheral administration of PP has been shown to decrease food intake in rodents.<ref name="pmid12915697">{{cite journal|last1=Batterham|first1=RL |last2=Le Roux|first2=CW |last3=Cohen|first3=MA| last4=Park|first4=AJ| last5=Ellis|first5=SM| last6=Patterson|first6=M| last7=Frost|first7=GS| last8=Ghatei|first8=MA| last9=Bloom|first9=SR| title=Pancreatic polypeptide reduces appetite and food intake in humans| journal=The Journal of Clinical Endocrinology and Metabolism|date=Aug 2003|volume=88|issue=8|pages=3989–92 |doi=10.1210/jc.2003-030630|pmid=12915697}}</ref> PP is secreted by PP pancreatic cells of [[Langerhans islets]]. It stimulates the gastric juice secretion, but inhibits the gastric secretion induced by pentagastrine. It is the antagonist of [[cholecystokinin]] and inhibits the pancreatic secretion which is stimulated by cholecystokinin. On fasting, PP seric concentration is 80 pg/ml; after the meal, it rises up from 8 to 10 times more; glucose and fats also induce PP's level increase, but on parenteral introduction of those substances, the level of hormones doesn't change. The administration of [[atropine]], the [[vagotomy]], blocks the PP's after-meal secretion. The excitation of the [[vagus nerve]], the administration of [[gastrin]], [[secretin]] or cholecystokinin induce PP secretion.


The function of PP is unknown, but effects on hepatic [[glycogen]] levels and gastrointestinal secretions have been suggested. For instance, it it thought to be a a [[cholecystokinin]] antagonist, and thus suppress the pancreatic secretion and stimulate gastric secretion.
The augmentation of PP secretion has been observed in hormonal-active pancreatic tumors ([[insulin]], [[glucagon]]), in [[Verner-Morrison syndrome]], and in [[gastrinoma]]s.


Its secretion in humans is increased after a protein meal, fasting, exercise, and acute [[hypoglycemia]] and is decreased by [[somatostatin]] and intravenous [[glucose]].
The '''PPY''' gene encodes an unusually short protein precursor that is cleaved to produce PP, as well as '''pancreatic icosapeptide''' and a 5- to 7- amino-acid oligopeptide.<ref>{{cite journal |last1=Boel |first1=E. |last2=Schwartz |first2=T. W. |last3=Norris |first3=K. E. |last4=Fiil |first4=N. P. |title=A cDNA encoding a small common precursor for human pancreatic polypeptide and pancreatic icosapeptide |date=April 1984 |journal=EMBO Journal |volume=3 |issue=4 |pages=909–912 |pmc=557446 |pmid=6373251}}</ref>


== Differential Diagnosis ==  
== See also ==


===Increased===
* [[Polypeptide-p]]
*Advanced Age
* [[Pancreas]]
*Gastrinoma
*[[List of human cell types derived from the germ layers]]
*Insulinoma
 
*PPoma
== References ==
*VIPoma
{{reflist}}


==External links==
==External links==
* {{GeorgiaPhysiology|6/6ch2/s6ch2_25}}
* {{GeorgiaPhysiology|6/6ch2/s6ch2_25}}
* {{MeshName|Pancreatic+polypeptide}}
* {{MeshName|Pancreatic+polypeptide}}
* BBC [http://news.bbc.co.uk/1/hi/health/6262347.stm Hope over 'obesity-busting gum'] 15 January, 2007
* BBC [http://news.bbc.co.uk/1/hi/health/6262347.stm Hope over 'obesity-busting gum'] 15 January 2007
* http://library.usmf.md/downloads/ebooks/Endocrinology_Anestiadi_en_2003/Lecture_11_p.(167-200).pdf


{{Endocrine pancreas}}
{{Neuropeptides}}
{{Neuropeptides}}
 
{{Gastrointestinal hormones}}
{{Neuropeptidergics}}


[[Category:Pancreatic hormones]]
[[Category:Pancreatic hormones]]
[[Category:Endocrinology]]
{{WikiDoc Help Menu}}
{{WikiDoc Sources}}
[[de:Pankreatisches Polypeptid]]
[[dv:ޕެންކްރިއެޓިކް ޕޮލިޕެޕްޓައިޑް]]
[[pt:Polipeptídeo pancreático]]
[[ru:Панкреатический полипептид]]

Latest revision as of 04:49, 21 December 2018

Not to be confused with Pancreatic hormone.
Pancreatic polypeptide
File:Pancreatic hormone 1TZ5.png
Identifiers
SymbolPPY
Entrez5539
HUGO9327
OMIM167780
RefSeqNM_002722
UniProtP01298
Other data
LocusChr. 17 p11.1-qter
File:PancreaticPolypeptide.jpg
IHC for Pancreatic polypeptide in a mouse pancreas, 200×

Pancreatic polypeptide (PP) is a polypeptide secreted by PP cells in the endocrine pancreas predominantly in the head of the pancreas. It consists of 36 amino acids and has molecular weight about 4200 Da.[1]

The function of PP is to self-regulate pancreatic secretion activities (endocrine and exocrine). It also has effects on hepatic glycogen levels and gastrointestinal secretions.

Its secretion in humans is increased after a protein meal, fasting, exercise, and acute hypoglycemia, and is decreased by somatostatin and intravenous glucose.

Plasma PP has been shown to be reduced in conditions associated with increased food intake and elevated in anorexia nervosa. In addition, peripheral administration of PP has been shown to decrease food intake in rodents.[2] PP is secreted by PP pancreatic cells of Langerhans islets. It stimulates the gastric juice secretion, but inhibits the gastric secretion induced by pentagastrine. It is the antagonist of cholecystokinin and inhibits the pancreatic secretion which is stimulated by cholecystokinin. On fasting, PP seric concentration is 80 pg/ml; after the meal, it rises up from 8 to 10 times more; glucose and fats also induce PP's level increase, but on parenteral introduction of those substances, the level of hormones doesn't change. The administration of atropine, the vagotomy, blocks the PP's after-meal secretion. The excitation of the vagus nerve, the administration of gastrin, secretin or cholecystokinin induce PP secretion.

The augmentation of PP secretion has been observed in hormonal-active pancreatic tumors (insulin, glucagon), in Verner-Morrison syndrome, and in gastrinomas.

The PPY gene encodes an unusually short protein precursor that is cleaved to produce PP, as well as pancreatic icosapeptide and a 5- to 7- amino-acid oligopeptide.[3]

See also

References

  1. ↑ Lonovics J, Devitt P, Watson LC, Rayford PL, Thompson JC (Oct 1981). "Pancreatic polypeptide". Arch. Surg. 116 (10): 1256–64. doi:10.1001/archsurg.1981.01380220010002. PMID 7025798.
  2. ↑ Batterham, RL; Le Roux, CW; Cohen, MA; Park, AJ; Ellis, SM; Patterson, M; Frost, GS; Ghatei, MA; Bloom, SR (Aug 2003). "Pancreatic polypeptide reduces appetite and food intake in humans". The Journal of Clinical Endocrinology and Metabolism. 88 (8): 3989–92. doi:10.1210/jc.2003-030630. PMID 12915697.
  3. ↑ Boel, E.; Schwartz, T. W.; Norris, K. E.; Fiil, N. P. (April 1984). "A cDNA encoding a small common precursor for human pancreatic polypeptide and pancreatic icosapeptide". EMBO Journal. 3 (4): 909–912. PMC 557446. PMID 6373251.

External links

Retrieved from "https://www.wikidoc.org/index.php?title=Pancreatic_polypeptide&oldid=1529050"