Kallistatin

Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 4
Identifiers
Symbols	SERPINA4 ; KAL; KLST; KST; PI-4; PI4; kallistatin
External IDs	OMIM: 147935 HomoloGene: 48412 GeneCards: SERPINA4 Gene
Gene ontology Molecular function • serine-type endopeptidase inhibitor activity Cellular component • extracellular space • extracellular exosome Biological process • negative regulation of endopeptidase activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5267	n/a
Ensembl	ENSG00000100665	n/a
UniProt	P29622	n/a
RefSeq (mRNA)	NM_001289032	n/a
RefSeq (protein)	NP_001275961	n/a
Location (UCSC)	Chr 14: 94.56 – 94.57 Mb	n/a
PubMed search		n/a

Kallistatin is a protein that in humans is encoded by the SERPINA4 gene.^[1][2]

See also

• Serpin

References

1. Chai KX, Chen LM, Chao J, Chao L (Dec 1993). "Kallistatin: a novel human serine proteinase inhibitor. Molecular cloning, tissue distribution, and expression in Escherichia coli". J Biol Chem 268 (32): 24498–505. PMID 8227002.
2. "Entrez Gene: SERPINA4 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 4".

Further reading

• Chao J, Miao RQ, Chen V, et al. (2001). "Novel roles of kallistatin, a specific tissue kallikrein inhibitor, in vascular remodeling". Biol. Chem. 382 (1): 15–21. doi:10.1515/BC.2001.003. PMID 11258665.
• Zhou GX, Chao L, Chao J (1993). "Kallistatin: a novel human tissue kallikrein inhibitor. Purification, characterization, and reactive center sequence". J. Biol. Chem. 267 (36): 25873–80. PMID 1334488.
• Wang MY, Day J, Chao L, Chao J (1990). "Human kallistatin, a new tissue kallikrein-binding protein: purification and characterization". Adv. Exp. Med. Biol. 247B: 1–8. doi:10.1007/978-1-4615-9546-5_1. PMID 2558505.
• Chen LM, Song Q, Chao L, Chao J (1995). "Cellular localization of tissue kallikrein and kallistatin mRNAs in human kidney". Kidney Int. 48 (3): 690–697. doi:10.1038/ki.1995.339. PMID 7474653.
• Chai KX, Ward DC, Chao J, Chao L (1995). "Molecular cloning, sequence analysis, and chromosomal localization of the human protease inhibitor 4 (kallistatin) gene (PI4)". Genomics 23 (2): 370–378. doi:10.1006/geno.1994.1513. PMID 7835886.
• Chao J, Schmaier A, Chen LM, et al. (1996). "Kallistatin, a novel human tissue kallikrein inhibitor: levels in body fluids, blood cells, and tissues in health and disease". J. Lab. Clin. Med. 127 (6): 612–620. doi:10.1016/S0022-2143(96)90152-3. PMID 8648266.
• Wang DZ, Song Q, Chen LM, et al. (1996). "Expression and cellular localization of tissue kallikrein-kinin system in human adrenal gland". Am. J. Physiol. 271 (3 Pt 2): F709–16. PMID 8853434.
• Ma JX, King LP, Yang Z, et al. (1997). "Kallistatin in human ocular tissues: reduced levels in vitreous fluids from patients with diabetic retinopathy". Curr. Eye Res. 15 (11): 1117–1123. doi:10.3109/02713689608995143. PMID 8950506.
• Wolf WC, Harley RA, Sluce D, et al. (1999). "Cellular localization of kallistatin and tissue kallikrein in human pancreas and salivary glands". Histochem. Cell Biol. 110 (5): 477–484. doi:10.1007/s004180050309. PMID 9826127.
• Wolf WC, Harley RA, Sluce D, et al. (1999). "Localization and expression of tissue kallikrein and kallistatin in human blood vessels". J. Histochem. Cytochem. 47 (2): 221–8. doi:10.1177/002215549904700210. PMID 9889257.
• Bläckberg M, Berling R, Ohlsson K (2000). "Tissue kallikrein in severe acute pancreatitis in patients treated with high-dose intraperitoneal aprotinin". Pancreas 19 (4): 325–334. doi:10.1097/00006676-199911000-00002. PMID 10547191.
• Chen VC, Chao L, Chao J (2000). "Reactive-site specificity of human kallistatin toward tissue kallikrein probed by site-directed mutagenesis". Biochim. Biophys. Acta 1479 (1–2): 237–46. doi:10.1016/S0167-4838(00)00044-3. PMID 10862973.
• Chen VC, Chao L, Chao J (2001). "A positively charged loop on the surface of kallistatin functions to enhance tissue kallikrein inhibition by acting as a secondary binding site for kallikrein". J. Biol. Chem. 275 (51): 40371–40377. doi:10.1074/jbc.M005691200. PMID 10991942.
• Chen VC, Chao L, Pimenta DC, et al. (2001). "Identification of a major heparin-binding site in kallistatin". J. Biol. Chem. 276 (2): 1276–1284. doi:10.1074/jbc.M005791200. PMID 11016932.
• Pimenta DC, Oliveira A, Juliano MA, Juliano L (2001). "Substrate specificity of human cathepsin D using internally quenched fluorescent peptides derived from reactive site loop of kallistatin". Biochim. Biophys. Acta 1544 (1–2): 113–22. doi:10.1016/S0167-4838(00)00209-0. PMID 11341921.
• Miao RQ, Agata J, Chao L, Chao J (2002). "Kallistatin is a new inhibitor of angiogenesis and tumor growth". Blood 100 (9): 3245–3252. doi:10.1182/blood-2002-01-0185. PMID 12384424.
• 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): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Miao RQ, Chen V, Chao L, Chao J (2003). "Structural elements of kallistatin required for inhibition of angiogenesis". Am. J. Physiol., Cell Physiol. 284 (6): C1604–13. doi:10.1152/ajpgi.00524.2002. PMID 12734113.

External links

• The MEROPS online database for peptidases and their inhibitors: I04.003
• SERPINA4 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)