Mutations in the gene encoding the serine protease inhibitor, Kazal type 1 are associated with chronic pancreatitis

Nature Genetics

Volumn 25, Issue 2, 2000, Pages 213-216

  Witt, Heiko ^a   Luck, Werner ^a   Hennies, Hans Christian ^b   Claßen, Martin ^c   Kage, Andreas ^a   Laß, Ulrich ^d   Landt, Olfert ^d   Becker, Michael ^a  

^a CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^b MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^c Zentralkrankenhaus 'Links der Weser' ^*  (Germany)

^d TIB MOLBIOL   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

APROTININ; SERINE PROTEINASE INHIBITOR;

ADOLESCENT; ARTICLE; CHILD; CHRONIC PANCREATITIS; ENZYME INHIBITION; GENE STRUCTURE; GENETIC ANALYSIS; GENETIC POLYMORPHISM; HUMAN; MAJOR CLINICAL STUDY; MISSENSE MUTATION; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN DEGRADATION; SCREENING;

ADOLESCENT; CHILD; CHROMOSOMES, HUMAN, PAIR 5; CHRONIC DISEASE; DNA MUTATIONAL ANALYSIS; EXONS; FEMALE; GENOTYPE; HAPLOTYPES; HUMANS; INTRONS; LINKAGE DISEQUILIBRIUM; LOD SCORE; MALE; MODELS, BIOLOGICAL; MUTATION; MUTATION, MISSENSE; PANCREATITIS; POLYMORPHISM, GENETIC; TRYPSIN INHIBITOR, KAZAL PANCREATIC;

EID: 0034039578     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/76088     Document Type: Article

References (16)

1. Whitcomb, D.C. et al. Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene. Nature Genet. 14, 141-145 (1996).
2. Gorry, M.C. et al. Mutations in the cationic trypsinogen gene are associated with recurrent acute and chronic pancreatitis. Gastroenterology 113, 1063-1068 (1997).
3. Ferec, C. et al. Mutations in the cationic trypsinogen gene and evidence for genetic heterogeneity in hereditary pancreatitis. J. Med. Genet. 36, 228-232 (1999).
4. Witt, H., Luck, W. & Becker, M. A signal peptide cleavage site mutation in the cationic trypsinogen gene is strongly associated with chronic pancreatitis. Gastroenterology 117, 7-10 (1999).
5. Horii, A. et al. Primary structure of human pancreatic secretory trypsin inhibitor (PSTI) gene. Biochem. Biophys. Res. Commun. 149, 635-641 (1987).
6. Bartelt, D.C., Shapanka, R. & Greene, L.J. The primary structure of the human pancreatic secretory trypsin inhibitor. Amino acid sequence of the reduced S-aminoethylated protein. Arch. Biochem. Biophys. 179, 189-199 (1977).
7. Marchbank, T., Freeman, T.C. & Playford, R.J. Human pancreatic secretory trypsin inhibitor. Digestion 59, 167-174 (1998).
8. Rinderknecht, H. Pancreatic secretory enzymes. in The Pancreas: Biology, Pathobiology, and Disease (eds Go, V.L.W. et al.) 219-251 (Raven, New York, 1993).
9. Spielman, R.S., McGinnis, R.E. & Ewens, W.J. Transmission test for linkage disequilibrium: the insulin gene region and insulin-dependent diabetes mellitus (IDDM). Am. J. Hum. Genet. 52, 506-516 (1993).
10. Falk, C.T. & Rubinstein, P. Haplotype relative risks: an easy reliable way to construct a proper control sample for risk calculations. Ann. Hum. Genet. 51, 227-233 (1987).
11. Terwilliger, J.D. A powerful likelihood method for the analysis of linkage disequilibrium between trait loci and one or more polymorphic marker loci. Am. J. Hum. Genet. 56, 777-787 (1995).
12. Laskowski, M. Jr & Kato, I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 49, 593-626 (1980).
13. Rinderknecht, H. Activation of pancreatic zymogens. Normal activation, premature intrapancreatic activation, protective mechanisms against inappropriate activation. Dig. Dis. Sci. 31, 314-321 (1986).
14. Sharer, N. et al. Mutations of the cystic fibrosis gene in patients with chronic pancreatitis. N. Engl. J. Med. 339, 645-652 (1998).
15. Cohn, J.A. et al. Relation between mutations of the cystic fibrosis gene and idiopathic pancreatitis. N. Engl. J. Med. 339, 653-658 (1998).
16. Dib, C. et al. A comprehensive genetic map of the human genome based on 5,264 microsatellites. Nature 380, 152-154 (1996).