Literature DB >> 12483248

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

Kinuko Kuwata1, Masahiko Hirota, Hiroyuki Shimizu, Masanori Nakae, Shoji Nishihara, Akio Takimoto, Kenji Mitsushima, Norihisa Kikuchi, Kazuaki Endo, Masayasu Inoue, Michio Ogawa.   

Abstract

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.

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Year:  2002        PMID: 12483248     DOI: 10.1007/s005350200156

Source DB:  PubMed          Journal:  J Gastroenterol        ISSN: 0944-1174            Impact factor:   7.527


  26 in total

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