Kallistatin is a protein that in humans is encoded by the SERPINA4 gene.34
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).56
See also
See also
References
References
- 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.
- Wang G, Zou J, Yu X, Yin S, Tang C (20 June 2020). "ABBS : The antiatherogenic function of kallistatin and its potential mechanism". Acta Biochimica et Biophysica Sinica. 52 (6): 583–589. doi:10.1093/abbs/gmaa035. PMID 32393963.
Further reading
Further reading
- 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 12 July 2025). ISBN 978-1-4615-9548-9. PMID 2558505.
{{cite book}}: CS1 maint: DOI inactive as of July 2025 (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
External links
