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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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Kallistatin

Introduction

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

See also

See also

References

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

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.
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