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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2002-11-19
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pubmed:databankReference |
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pubmed:abstractText |
R122, the primary autolysis site of the human cationic trypsinogen (PRSS1), constitutes an important "self-destruct" or "fail-safe" defensive mechanism against premature trypsin activation within the pancreas. Disruption of this site by a missense mutation, R122H, was found to cause hereditary pancreatitis. In addition to a c.365G>A (CGC>CAC) single nucleotide substitution, a c.365 through 366GC>AT (CGC>CAT) gene conversion event in exon 3 of PRSS1 was also found to result in a R122H mutation. This imposes a serious concern on the genotyping of pancreatitis by a widely used polymerase chain reaction-restriction fragment length polymorphism assay, which could only detect the commonest c.365G>A variant.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-10464646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-10649497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-10909845,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-10928834,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-11013445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-11073545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-11156648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-11379874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-11385705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-11514397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-11702203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-1861999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11734061-8841182
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1471-2156
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
19
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11734061-Amino Acid Substitution,
pubmed-meshheading:11734061-Chromatography, High Pressure Liquid,
pubmed-meshheading:11734061-DNA,
pubmed-meshheading:11734061-DNA Mutational Analysis,
pubmed-meshheading:11734061-Gene Conversion,
pubmed-meshheading:11734061-Genetic Predisposition to Disease,
pubmed-meshheading:11734061-Humans,
pubmed-meshheading:11734061-Mutation, Missense,
pubmed-meshheading:11734061-Nucleic Acid Denaturation,
pubmed-meshheading:11734061-Pancreatitis,
pubmed-meshheading:11734061-Trypsin,
pubmed-meshheading:11734061-Trypsinogen
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pubmed:year |
2001
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pubmed:articleTitle |
Discrimination of three mutational events that result in a disruption of the R122 primary autolysis site of the human cationic trypsinogen (PRSS1) by denaturing high performance liquid chromatography.
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pubmed:affiliation |
INSERM-EMI 0115, Génétique Moléculaire et Génétique Epidémiologique, Etablissement Français du Sang-Bretagne, Université de Bretagne Occidentale, Centre Hospitalier Universitaire, Brest, France. cedric.lemarechal@univ-brest.fr
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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