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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Functional analysis of recombinant pancreatic secretory trypsin inhibitor protein with amino-acid substitution.

BACKGROUND: We hypothesized that mutation of the pancreatic secretory trypsin inhibitor ( PSTI) gene may promote a predisposition to pancreatitis, possibly by reducing the inhibition of trypsin activity. Based on this hypothesis, we performed a biochemical analysis of recombinant PSTI protein. METHODS: The trypsin inhibitory activity of the recombinant protein was analyzed. The activity of PSTI protein with a point mutation of the most common type: (34)Asn (AAT)-to-Ser (AGT)(101A>G N34S: N34S) in exon 3, was compared with that of the wild type. RESULTS: The function of N34S PSTI remained unchanged under both the usual alkaline and acidic conditions compared with the wild-type PSTI. The calcium concentration did not affect the activity of recombinant PSTI. The trypsin susceptibility of the N34S protein was not increased either. CONCLUSIONS: Mechanisms other than the conformational change of PSTI associated with amino-acid substitution, such as abnormal splicing, may underlie the predisposition to pancreatitis in patients with the N34S mutation.[1]

References

  1. Functional analysis of recombinant pancreatic secretory trypsin inhibitor protein with amino-acid substitution. Kuwata, K., Hirota, M., Shimizu, H., Nakae, M., Nishihara, S., Takimoto, A., Mitsushima, K., Kikuchi, N., Endo, K., Inoue, M., Ogawa, M. J. Gastroenterol. (2002) [Pubmed]
 
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