Gastrin

GAST
Identifiers
Aliases	GAST, GAS, gastrin
External IDs	OMIM: 137250 MGI: 104768 HomoloGene: 628 GeneCards: GAST
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q21.2 Start 41,712,326 bp[1] End 41,715,969 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 D|11 63.46 cM Start 100,334,407 bp[2] End 100,336,996 bp[2]
Gene ontology Molecular function • protein binding • hormone activity Cellular component • extracellular region • extracellular space Biological process • response to food • signal transduction • regulation of receptor activity • G-protein coupled receptor signaling pathway Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2520	14459
Ensembl	ENSG00000184502	ENSMUSG00000017165
UniProt	P01350	P48757
RefSeq (mRNA)	NM_000805	NM_010257
RefSeq (protein)	NP_000796	NP_034387
Location (UCSC)	Chr 17: 41.71 – 41.72 Mb	Chr 11: 100.33 – 100.34 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Gastrin
Identifiers
Symbol	Gastrin
Pfam	PF00918
InterPro	IPR001651
PROSITE	PDOC00232
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Gastrin is a peptide hormone that stimulates secretion of gastric acid (HCl) by the parietal cells of the stomach and aids in gastric motility. It is released by G cells in the pyloric antrum of the stomach, duodenum, and the pancreas.

Gastrin binds to cholecystokinin B receptors to stimulate the release of histamines in enterochromaffin-like cells, and it induces the insertion of K⁺/H⁺ ATPase pumps into the apical membrane of parietal cells (which in turn increases H⁺ release into the stomach cavity). Its release is stimulated by peptides in the lumen of the stomach.

Contents

• 
  1 Physiology
  
  
  
  • 
    1.1 Genetics
    
  
  
  • 
    1.2 Synthesis
    
  
  
  • 
    1.3 Release
    
  
  
  • 
    1.4 Function
    
  
  
  • 
    1.5 Factors influencing secretion
    
    
    
    • 
      1.5.1 Physiologic
      
      
      
      • 
        1.5.1.1 Gastric lumen
        
      
      
      • 
        1.5.1.2 Paracrine
        
      
      
      • 
        1.5.1.3 Nervous
        
      
      
      • 
        1.5.1.4 Circulation
        
      
      
      
      
    
    
    • 
      1.5.2 Pathophysiologic
      
      
      
      • 
        1.5.2.1 Paraneoplastic
        
      
      
      
      
    
    
    
    
  
  
  
  


• 
  2 Role in disease
  


• 
  3 History
  


• 
  4 References
  


• 
  5 Further reading
  


• 
  6 External links
  

Physiology

Genetics

In humans, the GAS gene is located on the long arm of the seventeenth chromosome (17q21).^[5]

Synthesis

Gastrin is a linear peptide hormone produced by G cells of the duodenum and in the pyloric antrum of the stomach. It is secreted into the bloodstream. The encoded polypeptide is preprogastrin, which is cleaved by enzymes in posttranslational modification to produce progastrin (an intermediate, inactive precursor) and then gastrin in various forms, primarily the following three:

• 
  gastrin-34 ("big gastrin")


• 
  gastrin-17 ("little gastrin")


• 
  gastrin-14 ("minigastrin")

Also, pentagastrin is an artificially synthesized, five amino acid sequence identical to the last five amino acid sequence at the C-terminus end of gastrin.
The numbers refer to the amino acid count.

Release

Gastrin is released in response to certain stimuli. These include:^{[citation needed]}

• 
  stomach antrum distension


• 
  vagal stimulation (mediated by the neurocrine bombesin, or GRP in humans)


• the presence of partially digested proteins, especially amino acids, in the stomach. Aromatic amino acids are particularly powerful stimuli for gastrin release.^[6]
  


• 
  hypercalcemia (via calcium-sensing receptors^[7])

Gastrin release is inhibited by:^[8][9]

• the presence of acid (primarily the secreted HCl) in the stomach (a case of negative feedback)


• 
  somatostatin also inhibits the release of gastrin, along with secretin, GIP (gastroinhibitory peptide), VIP (vasoactive intestinal peptide), glucagon and calcitonin.

Function

G cell is visible near bottom left, and gastrin is labeled as the two black arrows leading from it. Note: this diagram does not illustrate gastrin's stimulatory effect on ECL cells.

The presence of gastrin stimulates parietal cells of the stomach to secrete hydrochloric acid (HCl)/gastric acid. This is done both directly on the parietal cell and indirectly via binding onto CCK2/gastrin receptors on ECL cells in the stomach, which then responds by releasing histamine, which in turn acts in a paracrine manner on parietal cells stimulating them to secrete H+ ions. This is the major stimulus for acid secretion by parietal cells.^{[citation needed]}

Along with the above-mentioned function, gastrin has been shown to have additional functions as well:

• Stimulates parietal cell maturation and fundal growth.


• Causes chief cells to secrete pepsinogen, the zymogen (inactive) form of the digestive enzyme pepsin.


• Increases antral muscle mobility and promotes stomach contractions.


• Strengthens antral contractions against the pylorus, and relaxes the pyloric sphincter, which increases the rate of gastric emptying.^[10]
  


• Plays a role in the relaxation of the ileocecal valve.^[11]
  


• Induces pancreatic secretions and gallbladder emptying.^[12]
  


• May impact lower esophageal sphincter (LES) tone, causing it to contract,^[13] - although pentagastrin, rather than endogenous gastrin, may be the cause.^[14]
  


• Gastrin contributes to the gastrocolic reflex.

Factors influencing secretion

Physiologic

Gastric lumen

• Stimulatory factors: dietary protein and amino acids (meat), hypercalcemia. (i.e. during the gastric phase)


• Inhibitory factor: acidity (pH below 3) - a negative feedback mechanism, exerted via the release of somatostatin from δ cells in the stomach, which inhibits gastrin and histamine release.

Paracrine

• Stimulatory factor: bombesin or gastrin-releasing peptide (GRP)


• Inhibitory factor: somatostatin - acts on somatostatin-2 receptors on G cells. in a paracrine manner via local diffusion in the intercellular spaces, but also systemically through its release into the local mucosal blood circulation; it inhibits acid secretion by acting on parietal cells.

Nervous

• Stimulatory factors: Beta-adrenergic agents, cholinergic agents, gastrin-releasing peptide (GRP)


• Inhibitory factor: Enterogastric reflex
  

Circulation

• Stimulatory factor: epinephrine
  


• Inhibitory factors:gastric inhibitory peptide (GIP), secretin, somatostatin, glucagon, calcitonin
  

Pathophysiologic

Paraneoplastic

• Gastrinoma paraneoplastic oversecretion (see Role in disease)

Role in disease

In the Zollinger–Ellison syndrome, gastrin is produced at excessive levels, often by a gastrinoma (gastrin-producing tumor, mostly benign) of the duodenum or the pancreas. To investigate for hypergastrinemia (high blood levels of gastrin), a "pentagastrin test" can be performed.^{[citation needed]}

In autoimmune gastritis, the immune system attacks the parietal cells leading to hypochlorhydria (low stomach acid secretion). This results in an elevated gastrin level in an attempt to compensate for increased pH in the stomach. Eventually, all the parietal cells are lost and achlorhydria results leading to a loss of negative feedback on gastrin secretion. Plasma gastrin concentration is elevated in virtually all individuals with mucolipidosis type IV (mean 1507 pg/mL; range 400-4100 pg/mL) (normal 0-200 pg/mL) secondary to a constitutive achlorhydria. This finding facilitates the diagnosis of patients with this neurogenetic disorder.^[15] Additionally, elevated gastrin levels may be present in chronic gastritis resulting from H pylori infection.^[16]

History

Its existence was first suggested in 1905 by the British physiologist John Sydney Edkins,^[17][18] and gastrins were isolated in 1964 by Hilda J. Tracy and Roderic Alfred Gregory at the University of Liverpool.^[19] In 1964 the structure of gastrin was determined.^[20]

References

1. 
   ^ ^abc GRCh38: Ensembl release 89: ENSG00000184502 - Ensembl, May 2017
   


2. 
   ^ ^abc GRCm38: Ensembl release 89: ENSMUSG00000017165 - Ensembl, May 2017
   


3. 
   ^ "Human PubMed Reference:"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
   


4. 
   ^ "Mouse PubMed Reference:".
   


5. 
   ^ Lund T, Geurts van Kessel AH, Haun S, Dixon JE (May 1986). "The genes for human gastrin and cholecystokinin are located on different chromosomes". Human Genetics. 73 (1): 77–80. doi:10.1007/BF00292669. PMID 3011648.
   


6. 
   ^ Blanco, Antonio; Blanco, Gustavo (2017), "Biochemical Bases of Endocrinology (II) Hormones and Other Chemical Intermediates", Medical Biochemistry, Elsevier, pp. 573–644, ISBN 9780128035504, retrieved 2018-11-02
   


7. 
   ^ Feng J, Petersen CD, Coy DH, Jiang JK, Thomas CJ, Pollak MR, Wank SA (October 2010). "Calcium-sensing receptor is a physiologic multimodal chemosensor regulating gastric G-cell growth and gastrin secretion". Proceedings of the National Academy of Sciences of the United States of America. 107 (41): 17791–6. doi:10.1073/pnas.1009078107. PMC 2955134. PMID 20876097.
   


8. 
   ^ Holst JJ, Orskov C, Seier-Poulsen S (1992). "Somatostatin is an essential paracrine link in acid inhibition of gastrin secretion". Digestion. 51 (2): 95–102. doi:10.1159/000200882. PMID 1354190.
   


9. 
   ^ Johnson LR (March 1984). "Effects of somatostatin and acid on inhibition of gastrin release in newborn rats". Endocrinology. 114 (3): 743–6. doi:10.1210/endo-114-3-743. PMID 6141932.
   


10. 
    ^ Tortora, G. J., & Grabowski, S. R. (1996). Principles of anatomy and physiology. New York, NY: HarperCollins College. 14th Ed. Pg 906
    


11. 
    ^ Vadokas B, Lüdtke FE, Lepsien G, Golenhofen K, Mandrek K (December 1997). "Effects of gastrin-releasing peptide (GRP) on the mechanical activity of the human ileocaecal region in vitro". Neurogastroenterology and Motility. 9 (4): 265–70. doi:10.1046/j.1365-2982.1997.d01-59.x. PMID 9430795.
    


12. 
    ^ Valenzuela JE, Walsh JH, Isenberg JI (September 1976). "Effect of gastrin on pancreatic enzyme secretion and gallbladder emptying in man". Gastroenterology. 71 (3): 409–11. PMID 950091.
    


13. 
    ^ Castell DO (February 1978). "Gastrin and lower esophageal sphincter tone". Archives of Internal Medicine. 138 (2): 196. doi:10.1001/archinte.138.2.196. PMID 626547.
    


14. 
    ^ Henderson JM, Lidgard G, Osborne DH, Carter DC, Heading RC (February 1978). "Lower oesophageal sphincter response to gastrin--pharmacological or physiological?". Gut. 19 (2): 99–102. doi:10.1136/gut.19.2.99. PMC 1411818. PMID 631634.
    


15. 
    ^ Schiffmann R, Dwyer NK, Lubensky IA, Tsokos M, Sutliff VE, Latimer JS, Frei KP, Brady RO, Barton NW, Blanchette-Mackie EJ, Goldin E (February 1998). "Constitutive achlorhydria in mucolipidosis type IV". Proceedings of the National Academy of Sciences of the United States of America. 95 (3): 1207–12. doi:10.1073/pnas.95.3.1207. PMC 18720. PMID 9448310.
    


16. 
    ^ "Review Article: Strategies to Determine Whether Hypergastrinaemia Is Due to Zollinger-Ellison Syndrome Rather Than a More Common Benign Cause". www.medscape.com.
    


17. 
    ^ Edkins JS (March 1906). "The chemical mechanism of gastric secretion". The Journal of Physiology. 34 (1–2): 133–44. doi:10.1113/jphysiol.1906.sp001146. PMC 1465807. PMID 16992839.
    


18. 
    ^ Modlin IM, Kidd M, Marks IN, Tang LH (February 1997). "The pivotal role of John S. Edkins in the discovery of gastrin". World Journal of Surgery. 21 (2): 226–34. doi:10.1007/s002689900221. PMID 8995084.
    


19. 
    ^ Gregory RA, Tracy HJ (1964). "The constitution and properties of two gastrins extracted from hog antral mucosa: Part I the isolation of two gastrins from hog antral mucosa". Gut. 5 (2): 103–107. doi:10.1136/gut.5.2.103. PMC 1552180.
    


20. 
    ^ Gregory H, Hardy PM, Jones DS, Kenner GW, Sheppard RC (December 1964). "The antral hormone gastrin. Structure of gastrin". Nature. 204: 931–3. doi:10.1038/204931a0. PMID 14248711.
    

Further reading

.mw-parser-output .refbegin{font-size:90%;margin-bottom:0.5em}.mw-parser-output .refbegin-hanging-indents>ul{list-style-type:none;margin-left:0}.mw-parser-output .refbegin-hanging-indents>ul>li,.mw-parser-output .refbegin-hanging-indents>dl>dd{margin-left:0;padding-left:3.2em;text-indent:-3.2em;list-style:none}.mw-parser-output .refbegin-100{font-size:100%}

• 
  Rozengurt E, Walsh JH (2001). "Gastrin, CCK, signaling, and cancer". Annual Review of Physiology. 63: 49–76. doi:10.1146/annurev.physiol.63.1.49. PMID 11181948.
  


• 
  Dockray GJ (December 2004). "Clinical endocrinology and metabolism. Gastrin". Best Practice & Research. Clinical Endocrinology & Metabolism. 18 (4): 555–68. doi:10.1016/j.beem.2004.07.003. PMID 15533775.
  


• 
  Anlauf M, Garbrecht N, Henopp T, Schmitt A, Schlenger R, Raffel A, Krausch M, Gimm O, Eisenberger CF, Knoefel WT, Dralle H, Komminoth P, Heitz PU, Perren A, Klöppel G (September 2006). "Sporadic versus hereditary gastrinomas of the duodenum and pancreas: distinct clinico-pathological and epidemiological features". World Journal of Gastroenterology. 12 (34): 5440–6. doi:10.3748/wjg.v12.i34.5440. PMID 17006979.
  


• 
  Polosatov MV, Klimov PK, Masevich CG, Samartsev MA, Wünsch E (April 1979). "Interaction of synthetic human big gastrin with blood proteins of man and animals". Acta Hepato-Gastroenterologica. 26 (2): 154–9. PMID 463490.
  


• 
  Fritsch WP, Hausamen TU, Scholten T (April 1977). "[Gastrointestinal hormones. I. Hormones of the gastrin group]". Zeitschrift für Gastroenterologie. 15 (4): 264–76. PMID 871064.
  


• 
  Higashimoto Y, Himeno S, Shinomura Y, Nagao K, Tamura T, Tarui S (May 1989). "Purification and structural determination of urinary NH2-terminal big gastrin fragments". Biochemical and Biophysical Research Communications. 160 (3): 1364–70. doi:10.1016/S0006-291X(89)80154-8. PMID 2730647.
  


• 
  Pauwels S, Najdovski T, Dimaline R, Lee CM, Deschodt-Lanckman M (June 1989). "Degradation of human gastrin and CCK by endopeptidase 24.11: differential behaviour of the sulphated and unsulphated peptides". Biochimica et Biophysica Acta. 996 (1–2): 82–8. doi:10.1016/0167-4838(89)90098-8. PMID 2736261.
  


• 
  Lund T, Geurts van Kessel AH, Haun S, Dixon JE (May 1986). "The genes for human gastrin and cholecystokinin are located on different chromosomes". Human Genetics. 73 (1): 77–80. doi:10.1007/BF00292669. PMID 3011648.
  


• 
  Kariya Y, Kato K, Hayashizaki Y, Himeno S, Tarui S, Matsubara K (1986). "Expression of human gastrin gene in normal and gastrinoma tissues". Gene. 50 (1–3): 345–52. doi:10.1016/0378-1119(86)90338-0. PMID 3034736.
  


• 
  Gregory RA, Tracy HJ, Agarwal KL, Grossman MI (August 1969). "Aminoacid constitution of two gastrins isolated from Zollinger-Ellison tumour tissue". Gut. 10 (8): 603–8. doi:10.1136/gut.10.8.603. PMC 1552899. PMID 5822140.
  


• 
  Bentley PH, Kenner GW, Sheppard RC (February 1966). "Structures of human gastrins I and II". Nature. 209 (5023): 583–5. doi:10.1038/209583b0. PMID 5921183.
  


• 
  Ito R, Sato K, Helmer T, Jay G, Agarwal K (August 1984). "Structural analysis of the gene encoding human gastrin: the large intron contains an Alu sequence". Proceedings of the National Academy of Sciences of the United States of America. 81 (15): 4662–6. doi:10.1073/pnas.81.15.4662. PMC 391550. PMID 6087340.
  


• 
  Wiborg O, Berglund L, Boel E, Norris F, Norris K, Rehfeld JF, Marcker KA, Vuust J (February 1984). "Structure of a human gastrin gene". Proceedings of the National Academy of Sciences of the United States of America. 81 (4): 1067–9. doi:10.1073/pnas.81.4.1067. PMC 344765. PMID 6322186.
  


• 
  Kato K, Hayashizaki Y, Takahashi Y, Himeno S, Matsubara K (December 1983). "Molecular cloning of the human gastrin gene". Nucleic Acids Research. 11 (23): 8197–203. doi:10.1093/nar/11.23.8197. PMC 326575. PMID 6324077.
  


• 
  Boel E, Vuust J, Norris F, Norris K, Wind A, Rehfeld JF, Marcker KA (May 1983). "Molecular cloning of human gastrin cDNA: evidence for evolution of gastrin by gene duplication". Proceedings of the National Academy of Sciences of the United States of America. 80 (10): 2866–9. doi:10.1073/pnas.80.10.2866. PMC 393933. PMID 6574456.
  


• 
  Kato K, Himeno S, Takahashi Y, Wakabayashi T, Tarui S, Matsubara K (December 1983). "Molecular cloning of human gastrin precursor cDNA". Gene. 26 (1): 53–7. doi:10.1016/0378-1119(83)90035-5. PMID 6689486.
  


• 
  Koh TJ, Wang TC (November 1995). "Molecular cloning and sequencing of the murine gastrin gene". Biochemical and Biophysical Research Communications. 216 (1): 34–41. doi:10.1006/bbrc.1995.2588. PMID 7488110.
  


• 
  Rehfeld JF, Hansen CP, Johnsen AH (January 1995). "Post-poly(Glu) cleavage and degradation modified by O-sulfated tyrosine: a novel post-translational processing mechanism". The EMBO Journal. 14 (2): 389–96. PMC 398093. PMID 7530658.
  


• 
  Rehfeld JF, Johnsen AH (August 1994). "Identification of gastrin component I as gastrin-71. The largest possible bioactive progastrin product". European Journal of Biochemistry. 223 (3): 765–73. doi:10.1111/j.1432-1033.1994.tb19051.x. PMID 8055952.
  


• 
  Varro A, Dockray GJ (November 1993). "Post-translational processing of progastrin: inhibition of cleavage, phosphorylation and sulphation by brefeldin A". The Biochemical Journal. 295 (Pt 3): 813–9. doi:10.1042/bj2950813. PMC 1134634. PMID 8240296.
  

External links

• Overview at colostate.edu


• 
  Essentials of Human Physiology by Thomas M. Nosek. Section 6/6ch4/s6ch4_14.

v t e Physiology of the gastrointestinal system
GI tract	Upper Exocrine Chief cells Pepsinogen Parietal cells Gastric acid Intrinsic factor Foveolar cells HCO3− Mucus Goblet cells Mucus Processes Swallowing Vomiting Fluids Saliva Gastric acid Gastric acid secretion: Gastrin G cells Histamine ECL cells Somatostatin D cells Lower Endocrine/paracrine Bile and pancreatic secretion: Enterogastrone Cholecystokinin I cells Secretin S cells Glucose homeostasis (incretins): GIP K cells GLP-1 L cells Endocrine cell types: Enteroendocrine cells Enterochromaffin cell APUD cell Fluids Intestinal juice Processes Segmentation contractions Migrating motor complex Borborygmus Defecation Enteric nervous system Submucous plexus Myenteric plexus Either/both Processes Peristalsis (Interstitial cell of Cajal Basal electrical rhythm) Gastrocolic reflex Digestion Enterocyte
Accessory	Fluids Bile Pancreatic juice Processes Enterohepatic circulation
Abdominopelvic	Peritoneal fluid

v t e Hormones
Endocrine glands	Hypothalamic- pituitary Hypothalamus GnRH TRH Dopamine CRH GHRH Somatostatin (GHIH) MCH Posterior pituitary Oxytocin Vasopressin Anterior pituitary FSH LH TSH Prolactin POMC CLIP ACTH MSH Endorphins Lipotropin GH Adrenal axis Adrenal cortex Aldosterone Cortisol Cortisone DHEA DHEA-S Androstenedione Adrenal medulla Epinephrine Norepinephrine Thyroid Thyroid hormones T3 T4 Calcitonin Thyroid axis Parathyroid PTH Gonadal axis Testis Testosterone AMH Inhibin Ovary Estradiol Progesterone Activin Inhibin Relaxin GnSAF Placenta hCG HPL Estrogen Progesterone Pancreas Glucagon Insulin Amylin Somatostatin Pancreatic polypeptide Pineal gland Melatonin N,N-Dimethyltryptamine 5-Methoxy-N,N-dimethyltryptamine
Other	Thymus Thymosins Thymosin α1 Beta thymosins Thymopoietin Thymulin Digestive system Stomach Gastrin Ghrelin Duodenum CCK Incretins GIP GLP-1 Secretin Motilin VIP Ileum Enteroglucagon Peptide YY Liver/other Insulin-like growth factor IGF-1 IGF-2 Adipose tissue Leptin Adiponectin Resistin Skeleton Osteocalcin Kidney Renin EPO Calcitriol Prostaglandin Heart Natriuretic peptide ANP BNP

v t e Peptides: neuropeptides
Hormones	see hormones
Opioid peptides	Dynorphins Dynorphin A Dynorphin A1–8 Dynorphin B Big dynorphin Leumorphin α-Neoendorphin β-Neoendorphin Endomorphins Endomorphin-1 Endomorphin-2 Endorphins α-Endorphin β-Endorphin γ-Endorphin Enkephalins Met-enkephalin Leu-enkephalin Others Adrenorphin Amidorphin Hemorphin Hemorphin-4 Nociceptin Opiorphin Spinorphin Valorphin
Other neuropeptides	Kinins Bradykinins Tachykinins: mammal Substance P Neurokinin A Neurokinin B amphibian Kassinin Physalaemin Neuromedins B N S U Orexins A B Other Angiotensin Bombesin Calcitonin gene-related peptide Carnosine Cocaine- and amphetamine-regulated transcript Delta sleep-inducing peptide FMRFamide Galanin Galanin-like peptide Gastrin-releasing peptide Ghrelin Neuropeptide AF Neuropeptide FF Neuropeptide SF Neuropeptide VF Neuropeptide S Neuropeptide Y Neurophysins Neurotensin Pancreatic polypeptide Pituitary adenylate cyclase-activating peptide RVD-Hpα VGF

v t e Signaling peptide/protein receptor modulators
Adiponectin	AdipoR1 Agonists: Peptide: Adiponectin ADP-355 ADP-399; Non-peptide: AdipoRon (–)-Arctigenin Arctiin Gramine Matairesinol Antagonists: Peptide: ADP-400 AdipoR2 Agonists: Peptide: Adiponectin ADP-355 ADP-399; Non-peptide: AdipoRon Deoxyschizandrin Parthenolide Syringing Taxifoliol Antagonists: Peptide: ADP-400
Angiotensin	See here instead.
Bradykinin	Agonists: Bradykinin Kallidin Antagonists: FR-173657 Icatibant LF22-0542
CGRP	Agonists: Amylin CGRP Pramlintide Antagonists: Atogepant BI 44370 TA CGRP (8-37) MK-3207 Olcegepant Rimegepant SB-268262 Telcagepant Ubrogepant Antibodies: Eptinezumab Erenumab Fremanezumab Galcanezumab
Cholecystokinin	CCKA Agonists: Cholecystokinin Antagonists: Amiglumide Asperlicin Devazepide Dexloxiglumide Lintitript Lorglumide Loxiglumide Pranazepide Proglumide Tarazepide Tomoglumide CCKB Agonists: Cholecystokinin CCK-4 Gastrin Pentagastrin (CCK-5) Antagonists: Ceclazepide CI-988 (PD-134308) Itriglumide L-365,360 Netazepide Proglumide Spiroglumide Unsorted Antagonists: Nastorazepide
CRH	CRF1 Agonists: Cortagine Corticorelin Corticotropin releasing hormone Sauvagine Stressin I Urocortin Antagonists: Antalarmin Astressin-B CP-154,526 Emicerfont Hypericin LWH-234 NBI-27914 NBI-74788 Pexacerfont R-121919 TS-041 Verucerfont CRF2 Agonists: Corticorelin Corticotropin releasing hormone Sauvagine Urocortin Antagonists: Astressin-B
Cytokine	See here instead.
Endothelin	Agonists: Endothelin 1 Endothelin 2 Endothelin 3 IRL-1620 Antagonists: A-192621 ACT-132577 Ambrisentan Aprocitentan Atrasentan Avosentan Bosentan BQ-123 BQ-788 Clazosentan Darusentan Edonentan Enrasentan Fandosentan Feloprentan Macitentan Nebentan Sitaxentan Sparsentan Tezosentan Zibotentan
Galanin	GAL1 Agonists: Galanin Galanin (1-15) Galanin-like peptide Galmic Galnon NAX 810-2 Antagonists: C7 Dithiepine-1,1,4,4-tetroxide Galantide (M15) M32 M35 M40 SCH-202596 GAL2 Agonists: Galanin Galanin (1-15) Galanin (2-11) Galanin-like peptide Galmic Galnon J18 NAX 810-2 Antagonists: C7 Galantide (M15) M32 M35 M40 M871 GAL3 Agonists: Galanin Galanin (1-15) Galmic Galnon Antagonists: C7 Galantide (M15) GalR3ant HT-2157 M32 M35 M40 SNAP-37889 SNAP-398299
Ghrelin/GHS	See here instead.
GH	See here instead.
GHRH	See here instead.
GLP	GLP-1 Agonists: Albiglutide Beinaglutide Dulaglutide Efpeglenatide Exenatide GLP-1 Langlenatide Liraglutide Lixisenatide Oxyntomodulin Pegapamodutide Semaglutide Taspoglutide GLP-2 Agonists: Apraglutide Elsiglutide Glepaglutide GLP-2 Teduglutide Others Propeptides: Preproglucagon Proglucagon
Glucagon	Agonists: Dasiglucagon Glucagon Oxyntomodulin Antagonists: Adomeglivant L-168,049 LGD-6972 Propeptides: Preproglucagon Proglucagon
GnRH	See here instead.
Gonadotropin	See here instead.
Growth factor	See here instead.
Insulin	Agonists: Chaetochromin (4548-G05) Insulin-like growth factor 1 Insulin-like growth factor 2 Insulin Insulin aspart Insulin degludec Insulin detemir Insulin glargine Insulin glulisine Insulin lispro Mecasermin Mecasermin rinfabate Antagonists: BMS-754807 S661 S961 Kinase inhibitors: Linsitinib Antibodies: Xentuzumab (against IGF-1 and IGF-2)
Kisspeptin	Agonists: Kisspeptin Kisspeptin-10 Antagonists: Kisspeptin-234
Leptin	Agonists: Leptin Metreleptin
MCH	MCH1 Agonists: Melanin concentrating hormone Antagonists: ATC-0065 ATC-0175 GW-803430 NGD-4715 SNAP-7941 SNAP-94847 MCH2 Agonists: Melanin concentrating hormone
Melanocortin	See here instead.
Neuropeptide FF	Agonists: Neuropeptide AF Neuropeptide FF Neuropeptide SF (RFRP-1) Neuropeptide VF (RFRP-3) Antagonists: BIBP-3226 RF9
Neuropeptide S	Agonists: Neuropeptide S Antagonists: ML-154 SHA-68
Neuropeptide Y	Y1 Agonists: Neuropeptide Y Peptide YY Antagonists: BIBO-3304 BIBP-3226 BVD-10 GR-231118 PD-160170 Y2 Agonists: 2-Thiouridine 5'-triphosphate Neuropeptide Y Neuropeptide Y (13-36) Peptide YY Peptide YY (3-36) Antagonists: BIIE-0246 JNJ-5207787 SF-11 Y4 Agonists: GR-231118 Neuropeptide Y Pancreatic polypeptide Peptide YY Antagonists: UR-AK49 Y5 Agonists: BWX-46 Neuropeptide Y Peptide YY Antagonists: CGP-71683 FMS-586 L-152,804 Lu AA-33810 MK-0557 NTNCB Velneperit (S-2367)
Neurotensin	NTS1 Agonists: Neurotensin Neuromedin N Antagonists: Meclinertant SR-142948 NTS2 Agonists: Neurotensin Antagonists: Levocabastine SR-142948
Opioid	See here instead.
Orexin	OX1 Agonists: Orexin (A, B) Antagonists: ACT-335827 ACT-462206 Almorexant Filorexant Lemborexant Nemorexant RTIOX-276 SB-334867 SB-408124 SB-649868 Suvorexant TCS-1102 OX2 Agonists: Orexin (A, B) SB-668875 Antagonists: ACT-335827 ACT-462206 Almorexant EMPA Filorexant JNJ-10397049 Lemborexant MK-1064 SB-649868 Seltorexant Suvorexant TCS-1102 TCS-OX2-29
Oxytocin	See here instead.
Prolactin	Agonists: Growth hormone Human placental lactogen Placental growth hormone (growth hormone variant) Prolactin S179D-hPRL Somatotropin Antagonists: Δ1–9-G129R-hPRL Δ1–14-G129R-hPRL G120K-hGH G129R-hPRL Prolactin modulators: Prolactin inhibitors: D2 receptor agonists (e.g., bromocriptine, cabergoline); Prolactin releasers: D2 receptor antagonists (e.g., domperidone, metoclopramide, risperidone) Estrogens (e.g., estradiol) Progestogens (e.g., progesterone)
PTH	Agonists: Abaloparatide Parathyroid hormone Parathyroid hormone-related protein (PTHrP) Semparatide Teriparatide
Relaxin	Agonists: Insulin-like factor 3 Relaxin (1, 2, 3) Serelaxin
Somatostatin	See here instead.
Tachykinin	See here instead.
TRH	Agonists: Azetirelin Fertirelin Montirelin Orotirelin Posatirelin Protirelin Rovatirelin Taltirelin TRH (TRF)
TSH	Agonists: Thyrotropin alfa TSH (thyrotropin)
Vasopressin	See here instead.
VIP/PACAP	VIPR1 Agonists: Peptide: Bay 55-9837 LBT-3393 PACAP VIP VIPR2 Agonists: Peptide: LBT-3627 PACAP VIP PAC1 Agonists: PACAP PACAP (1-27) PACAP (1-38) Antagonists: PACAP (6-38) Unsorted PHI PHM PHV
Others	Endogenous: Adrenomedullin Apelin Asprosin Bombesin Calcitonin Carnosine CART CLIP DSIP Enteroglucagon Formyl peptide GALP GIP GRP Integrin ligands (collagens, fibrinogen, fibronectin, laminins, ICAM-1, ICAM-2, osteopontin, VCAM-1, vitronectin) Kininogens Motilin Natriuretic peptides (ANP, BNP, CNP, urodilatin) Nesfatin-1 Neuromedin B Neuromedin N Neuromedin S Neuromedin U Obestatin Osteocalcin Resistin Secretin Thymopoietin Thymosins Thymulin Urotensin-II VGF Exogenous: Lifitegrast (LFA-1 antagonist)
See also Receptor/signaling modulators

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