Gastricsin

Progastricsin (pepsinogen C)
PDB rendering based on 1avf.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1AVF​, 1HTR​
Identifiers
Symbols	PGC ; PEPC; PGII
External IDs	OMIM: 169740 MGI: 98909 HomoloGene: 55669 ChEMBL: 2136 GeneCards: PGC Gene
EC number	3.4.23.3
Gene ontology Molecular function • aspartic-type endopeptidase activity Cellular component • extracellular space • extracellular exosome Biological process • proteolysis • digestion • protein catabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5225	109820
Ensembl	ENSG00000096088	ENSMUSG00000023987
UniProt	P20142	Q9D7R7
RefSeq (mRNA)	NM_001166424	NM_025973
RefSeq (protein)	NP_001159896	NP_080249
Location (UCSC)	Chr 6: 41.74 – 41.75 Mb	Chr 17: 47.73 – 47.73 Mb
PubMed search

Gastricsin also known as pepsinogen C is an enzyme that in humans is encoded by the PGC gene.^[1][2][3][4]

Function

Gastricsin is an aspartic proteinase that belongs to the peptidase family A1. The encoded protein is a digestive enzyme that is produced in the stomach and constitutes a major component of the gastric mucosa. This protein is also secreted into the serum. This protein is synthesized as an inactive zymogen that includes a highly basic prosegment. This enzyme is converted into its active mature form at low pH by sequential cleavage of the prosegment that is carried out by the enzyme itself.^[4]

Clinical significance

Polymorphisms in this gene are associated with susceptibility to gastric cancers. Serum levels of this enzyme are used as a biomarker for certain gastric diseases including Helicobacter pylori related gastritis.^[4]

See also

• pepsinogen

References

1. Hayano T, Sogawa K, Ichihara Y, Fujii-Kuriyama Y, Takahashi K (January 1988). "Primary structure of human pepsinogen C gene". J. Biol. Chem. 263 (3): 1382–5. PMID 3335549.
2. Pals G, Azuma T, Mohandas TK, Bell GI, Bacon J, Samloff IM, Walz DA, Barr PJ, Taggart RT (February 1989). "Human pepsinogen C (progastricsin) polymorphism: evidence for a single locus located at 6p21.1-pter". Genomics 4 (2): 137–48. doi:10.1016/0888-7543(89)90292-9. PMID 2567697.
3. Taggart RT, Cass LG, Mohandas TK, Derby P, Barr PJ, Pals G, Bell GI (January 1989). "Human pepsinogen C (progastricsin). Isolation of cDNA clones, localization to chromosome 6, and sequence homology with pepsinogen A". J. Biol. Chem. 264 (1): 375–9. PMID 2909526.
4. "Entrez Gene: PGC progastricsin (pepsinogen C)".

Further reading

• Richter C, Tanaka T, Yada RY (1998). "Mechanism of activation of the gastric aspartic proteinases: pepsinogen, progastricsin and prochymosin.". Biochem. J. 335 (3): 481–90. PMC 1219805. PMID 9794784.
• Sánchez LM, Freije JP, Merino AM, et al. (1992). "Isolation and characterization of a pepsin C zymogen produced by human breast tissues.". J. Biol. Chem. 267 (34): 24725–31. PMID 1280267.
• Ichinose M, Miki K, Wong RN, et al. (1991). "Methylation and expression of human pepsinogen genes in normal tissues and their alteration in stomach cancer.". Jpn. J. Cancer Res. 82 (6): 686–92. doi:10.1111/j.1349-7006.1991.tb01904.x. PMID 1906854.
• Athauda SB, Tanji M, Kageyama T, Takahashi K (1990). "A comparative study on the NH2-terminal amino acid sequences and some other properties of six isozymic forms of human pepsinogens and pepsins.". J. Biochem. 106 (5): 920–7. PMID 2515193.
• Westerveld BD, Pals G, Bosma A, et al. (1987). "Gastric proteases in Barrett's esophagus.". Gastroenterology 93 (4): 774–8. PMID 3305135.
• Foltmann B, Jensen AL (1983). "Human progastricsin. Analysis of intermediates during activation into gastricsin and determination of the amino acid sequence of the propart.". Eur. J. Biochem. 128 (1): 63–70. doi:10.1111/j.1432-1033.1982.tb06931.x. PMID 6816595.
• Moore SA, Sielecki AR, Chernaia MM, et al. (1995). "Crystal and molecular structures of human progastricsin at 1.62 A resolution.". J. Mol. Biol. 247 (3): 466–85. doi:10.1006/jmbi.1994.0154. PMID 7714902.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Aabakken L, Axelsson CK, Szecsi PB (1993). "Pepsinogen A and C serum levels in relation to acute NSAID-associated mucosal lesions in healthy volunteers.". Scand. J. Gastroenterol. 28 (6): 557–60. doi:10.3109/00365529309098266. PMID 8322031.
• Aoki T, Tomaki E, Morikawa J, et al. (1997). "Purification of pepsinogens from human urine and electrophoretic analysis by caseogram print.". Biochem. Mol. Biol. Int. 39 (6): 1147–56. doi:10.1080/15216549600201332. PMID 8876968.
• Diamandis EP, Nadkarni S, Bhaumik B, et al. (1997). "Immunofluorometric assay of pepsinogen C and preliminary clinical applications.". Clin. Chem. 43 (8 Pt 1): 1365–71. PMID 9267315.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Khan AR, Cherney MM, Tarasova NI, James MN (1998). "Structural characterization of activation 'intermediate 2' on the pathway to human gastricsin.". Nat. Struct. Biol. 4 (12): 1010–5. doi:10.1038/nsb1297-1010. PMID 9406551.
• Plebani M, Basso D, Navaglia F, DiMario F (1998). "Helicobacter pylori genotypes influence serum pepsinogen C levels.". Helicobacter 2 (4): 172–5. doi:10.1111/j.1523-5378.1997.tb00082.x. PMID 9421118.
• Rojo JV, Merino AM, González LO, Vizoso F (2003). "Expression and clinical significance of pepsinogen C in epithelial ovarian carcinomas.". Eur. J. Obstet. Gynecol. Reprod. Biol. 104 (1): 58–63. doi:10.1016/S0301-2115(01)00610-8. PMID 12128264.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.