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[−215G>A; IVS3+2T>C] mutation in the SPINK1 gene causes exon 3 skipping and loss of the trypsin binding site
  1. K Kume*,
  2. A Masamune*,
  3. K Kikuta,
  4. T Shimosegawa
  1. Division of Gastroenterology, Tohoku University Graduate School of Medicine, Sendai, Japan
  1. Correspondence to:
    Dr A Masamune
    Division of Gastroenterology, Tohoku University Graduate School of Medicine, 1-1 Seiryo-machi, Aoba-ku, Sendai 980-8574 Japan; amasamune{at}int3.med.tohoku.ac.jp

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Previous studies have shown an association between chronic pancreatitis (CP) and mutations, especially the N34S mutation, in the serine protease inhibitor Kazal type 1 (SPINK1) gene.1,2 The human SPINK1 gene is approximately 7.5 kb long and consists of four exons.3 The gene product consists of 79 amino acids, including a 23 amino acid signal peptide. In exon 3, SPINK1 possesses a reactive site that serves as a specific target substrate for trypsin.4 It has been suggested that SPINK1 mutations might result in altered interaction between SPINK1 and trypsin, thus affecting the protease/antiprotease balance within the pancreas.1,2 But the underlying molecular mechanisms remain unclear. Splicing defects are estimated to account for approximately 10–15% of disease causing mutations in humans.5 Changes in the splicing patterns and in levels of normal transcripts lead to phenotypic differences. The prevalence of splicing mutations …

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