Kallistatin

SERPINA4
Identifiers
Aliases	SERPINA4 , KAL, KLST, KST, PI-4, PI4, kallistatin, serpin family A member 4
External IDs	OMIM: 147935 HomoloGene: 48412 GeneCards: SERPINA4
Gene location (Human) Chr. Chromosome 14 (human) [1] Band 14q32.13 Start 94,561,442 bp [1] End 94,569,913 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of liver body of pancreas gallbladder islet of Langerhans corpus epididymis caput epididymis body of stomach seminal vesicula tibialis anterior muscle kidney n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase inhibitor activity serine-type endopeptidase inhibitor activity Cellular component extracellular exosome platelet dense granule lumen extracellular space extracellular region Biological process negative regulation of peptidase activity platelet degranulation negative regulation of endopeptidase activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5267 n/a Ensembl ENSG00000100665 n/a UniProt P29622 n/a RefSeq (mRNA) NM_006215 NM_001289032 NM_001289033 n/a RefSeq (protein) NP_001275961 NP_001275962 NP_006206 n/a Location (UCSC) Chr 14: 94.56 – 94.57 Mb n/a PubMed search [2] n/a
Wikidata
View/Edit Human

Kallistatin is a protein that in humans is encoded by the SERPINA4 gene. ^{[3] [4]}

Kallistatin consists of three folded ß segments and eight helical structures and contains two functional domains, an active site and a heparin-binding site.

Kallistatin signals through several receptors, including integrin ß3, lipoprotein receptor-related protein 6 ( LRP6 ), nucleolin, and Krüppel-like factor 4 ( KLF4 ). ^{[5] [6]}

See also

• Serpin

References

1. GRCh38: Ensembl release 89: ENSG00000100665 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. 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. doi: 10.1016/S0021-9258(20)80553-5 . PMID   8227002.
4. "Entrez Gene: SERPINA4 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 4".
5. Wang G, Zou J, Yu X, Yin S, Tang C (June 2020). "The antiatherogenic function of kallistatin and its potential mechanism". Acta Biochim Biophys Sin (Shanghai). 52 (6): 583–589. doi: 10.1093/abbs/gmaa035 . PMID   32393963.
6. "ABBS : The antiatherogenic function of kallistatin and its potential mechanism".

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. S2CID   33204682.
• 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. doi: 10.1016/S0021-9258(18)35690-4 . PMID   1334488.
• Wang MY, Day J, Chao L, Chao J (1989). "Human Kallistatin, a New Tissue Kallikrein-Binding Protein: Purification and Characterization". Kinins V. Advances in Experimental Medicine and Biology. Vol. 247B. pp. 1–8. doi:10.1007/978-1-4615-9546-5_1. ISBN   978-1-4615-9548-9. 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. doi:10.1152/ajprenal.1996.271.3.F709. 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. S2CID   25547665.
• 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. S2CID   1126556.
• 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. Bibcode:2002PNAS...9916899M. 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" (PDF). Am. J. Physiol., Cell Physiol. 284 (6): C1604–13. doi:10.1152/ajpgi.00524.2002. PMID   12734113. S2CID   1753923. Archived from the original (PDF) on 2019-03-09.

External links

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