Guanylin

Protein family From Wikipedia, the free encyclopedia

Guanylin is a 15 amino acid peptide that is secreted by goblet cells in the colon. Guanylin acts as an agonist of the guanylyl cyclase receptor GC-C and regulates electrolyte and water transport in intestinal and renal epithelia.[2][3] Upon receptor binding, guanylin increases the intracellular concentration of cGMP, induces chloride secretion and decreases intestinal fluid absorption, ultimately causing diarrhoea.[4] The peptide stimulates the enzyme through the same receptor binding region as the heat-stable enterotoxins.[3]

SymbolGUCA2A
Alt. symbolsGUCA2
Quick facts guanylate cyclase activator 2A (guanylin), Identifiers ...
guanylate cyclase activator 2A (guanylin)
Solution structure of human proguanylin.[1]
Identifiers
SymbolGUCA2A
Alt. symbolsGUCA2
NCBI gene2980
HGNC4682
OMIM139392
PDB1O8R
RefSeqNM_033553
UniProtQ02747
Other data
LocusChr. 1 p35-p34
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StructuresSwiss-model
DomainsInterPro
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Quick facts Identifiers, Symbol ...
Guanylin precursor
Identifiers
SymbolGuanylin
PfamPF02058
InterProIPR000879
SCOP21uyb / SCOPe / SUPFAM
Available protein structures:
PDB  1gnb :103-115 1gna :103-115 1o8rA:22-115

1uya :97-111 1uyb :97-111 IPR000879 PF02058 (ECOD; PDBsum)

 
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Researches have found that a loss in guanylin expression can lead to colorectal cancer due to guanylyl cyclase C's function as an intestinal tumor suppressor.[5] When guanylin expression was measured on over 250 colon cancer patients, more than 85% of patients had a loss of guanylin expression in cancerous tissue samples by 100-1000 times when compared to the same patients's nearby healthy colon tissue.[5] Another study done on genetically engineered mice found that mice on a high calorie diet had reduced guanylin expression in the colon.[6] This loss of expression then resulted in guanylyl cyclase C inhibition and the formation of tumors, therefore linking diet-induced obesity with colorectal cancer. [6]

Human proteins containing this domain

GUCA2A; GUCA2B;

Structure

This peptide has two topogies,[7] both isoforms are shown below:

Structure of the A-form of human uroguanylin.[7]
Structure of the B-form of human uroguanylin.[7]

References

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