Pancreatic polypeptide: Difference between revisions
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{{distinguish|Pancreatic hormone}} | {{distinguish|Pancreatic hormone}} | ||
{{ | {{More citations needed|date=June 2015}} | ||
{{infobox protein | {{infobox protein | ||
| Name = Pancreatic polypeptide | | Name = Pancreatic polypeptide | ||
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}} | }} | ||
[[File:PancreaticPolypeptide.jpg|thumb|IHC for Pancreatic polypeptide in a mouse pancreas, 200×]] | [[File:PancreaticPolypeptide.jpg|thumb|IHC for Pancreatic polypeptide in a mouse pancreas, 200×]] | ||
'''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> | '''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) | 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]]. | 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.<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. | 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. | ||
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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> | 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> | ||
==See also== | == See also == | ||
* [[Polypeptide-p]] | * [[Polypeptide-p]] | ||
* [[Pancreas]] | * [[Pancreas]] | ||
*[[List of human cell types derived from the germ layers]] | |||
==References== | == References == | ||
{{reflist}} | {{reflist}} | ||
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* http://library.usmf.md/downloads/ebooks/Endocrinology_Anestiadi_en_2003/Lecture_11_p.(167-200).pdf | * http://library.usmf.md/downloads/ebooks/Endocrinology_Anestiadi_en_2003/Lecture_11_p.(167-200).pdf | ||
{{Neuropeptides}} | {{Neuropeptides}} | ||
{{Gastrointestinal hormones}} | {{Gastrointestinal hormones}} | ||
Latest revision as of 04:49, 21 December 2018
This article needs additional citations for verification. (June 2015) (Learn how and when to remove this template message) |
| Pancreatic polypeptide | |
|---|---|
| File:Pancreatic hormone 1TZ5.png | |
| Identifiers | |
| Symbol | PPY |
| Entrez | 5539 |
| HUGO | 9327 |
| OMIM | 167780 |
| RefSeq | NM_002722 |
| UniProt | P01298 |
| Other data | |
| Locus | Chr. 17 p11.1-qter |
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
- ↑ 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.
- ↑ 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.
- ↑ 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
- Essentials of Human Physiology by Thomas M. Nosek. Section 6/6ch2/s6ch2_25.
- Pancreatic+polypeptide at the US National Library of Medicine Medical Subject Headings (MeSH)
- BBC Hope over 'obesity-busting gum' 15 January 2007
- http://library.usmf.md/downloads/ebooks/Endocrinology_Anestiadi_en_2003/Lecture_11_p.(167-200).pdf