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; OMA:SERPINA4 - orthologs
Gene location (Human)
Chr.	Chromosome 14 (human)
End	94,569,913 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; body of pancreas; ; gallbladder; ; islet of Langerhans; ; corpus epididymis; ; caput epididymis; ; body of stomach; ; seminal vesicula; ; tail of epididymis; ; tibialis anterior muscle;
	n/a
	More reference expression data
	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
	5267
	n/a
	ENSG00000100665
	n/a
	P29622
	n/a
	NM_006215; NM_001289032; NM_001289033
	n/a
	NP_001275961; NP_001275962; NP_006206
	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]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000100665 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ "Entrez Gene: SERPINA4 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 4".
^ 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.
^ "ABBS : The antiatherogenic function of kallistatin and its potential mechanism".

Chao J, Miao RQ, Chen V, Chen LM, Chao L (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 (inactive 2024-04-03). ISBN 978-1-4615-9548-9. PMID 2558505.{{cite book}}: CS1 maint: DOI inactive as of April 2024 (link)
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, Yang Z, Chao L (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, Chao L, Chao J (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, Crouch RK, Chao L, Chao J (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, Chao J, Harley RA (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, Chao L, Chao J (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, Bledsoe G, Juliano L, Chao J (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, Derge JG, Klausner RD, Collins FS, 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)

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000100665 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8227002-3] 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.

[entrez-4] "Entrez Gene: SERPINA4 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 4".

[pmid32393963-5] 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.

[ABBS_5835537-6] "ABBS : The antiatherogenic function of kallistatin and its potential mechanism".

[1]

[2]

[3]

[4]

[5]

[6]

v t e Serpins
inhibitory	Alpha 1-antichymotrypsin Alpha 1-antitrypsin Alpha 2-antiplasmin Antithrombin C1-inhibitor Heparin cofactor II Protein C inhibitor Plasminogen activator inhibitor-1 Plasminogen activator inhibitor-2 Protein Z-related protease inhibitor SERPINA1 SERPINA2 SERPINA3 SERPINA4 SERPINA5 SERPINA9 SERPINA14 SERPINB1 SERPINB2 SERPINB3 SERPINB4 SERPINB5 SERPINB6 SERPINB7 SERPINB8 SERPINB9 SERPINB10 SERPINB13 SERPINC1 SERPIND1 SERPINE1 SERPINE2 SERPINE2 SERPINF1 SERPING1 SERPINH1 SERPINI1 SERPINI2
Cross class inhibitory	MENT SCCA-1 CrmA
noninhibitory	Heat shock protein 47 Maspin Ovalbumin Transcortin Thyroxine-binding globulin Angiotensinogen PEDF
see also disorders of globin and globulin proteins

See also

References

Further reading

External links