Enterokinase and Trypsin Activities in Pancreatic Insufficiency and Diseases of the Small Intestine

Lebenthal, Emanuel; Antonowicz, Irena; Shwachman, Harry

doi:10.1016/s0016-5085(76)80486-6

Cited by 48 publications

(11 citation statements)

References 17 publications

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“…Trypsin activity in a duodenal-juice sample was low but was restored to normal when isolated enteropeptidase was added. Several similar cases were described subsequently (Polonovski et al 1970, Haworth et al 1971Pardou et al 1975;Follett and Macdonald 1976;Lebenthal et al 1976;Ghishan et al 1983;Green et al 1984;Marshall et al 1989). These reports consider two families with affected siblings (Tarlow et al 1970;Haworth et al 1975), including one family with affected individuals of either gender, a finding suggesting autosomal recessive inheritance (Haworth et al 1975).…”

Section: Introductionmentioning

confidence: 65%

Mutations in the Proenteropeptidase Gene Are the Molecular Cause of Congenital Enteropeptidase Deficiency

Holzinger

Maier

Bück

et al. 2002

The American Journal of Human Genetics

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Enteropeptidase (enterokinase [E.C.3.4.21.9]) is a serine protease of the intestinal brush border in the proximal small intestine. It activates the pancreatic proenzyme trypsinogen, which, in turn, releases active digestive enzymes from their inactive pancreatic precursors. Congenital enteropeptidase deficiency is a rare recessively inherited disorder leading, in affected infants, to severe failure to thrive. The genomic structure of the proenteropeptidase gene (25 exons, total gene size 88 kb) was characterized in order to perform DNA sequencing in three clinically and biochemically proved patients with congenital enteropeptidase deficiency who were from two families. We found compound heterozygosity for nonsense mutations (S712X/R857X) in two affected siblings and found compound heterozygosity for a nonsense mutation (Q261X) and a frameshift mutation (FsQ902) in the third patient. In accordance with the biochemical findings, all four defective alleles identified are predicted null alleles leading to a gene product not containing the active site of the enzyme. These data provide first evidence that proenteropeptidase-gene mutations are the primary cause of congenital enteropeptidase deficiency.

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Section: Introductionmentioning

confidence: 65%

Mutations in the Proenteropeptidase Gene Are the Molecular Cause of Congenital Enteropeptidase Deficiency

Holzinger

Maier

Bück

et al. 2002

The American Journal of Human Genetics

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“…Enterokinase has therefore a key permissive role in protein digestion and plays an essential part in the zymogen mechanism that prevents the pancreas destroying itself. Despite its apparent importance, the origin and distribution of the enzyme in human intestine has not been precisely defined (Lebenthal et al, 1976).…”

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confidence: 99%

Immunofluorescent localisation of enterokinase in human small intestine.

Hermon‐Taylor¹,

Perrin²,

Grant³

et al. 1977

Gut

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SUMMARY The distribution of enterokinase in human intestine was studied in operative mucosal biopsies using specific antiserum to human enterokinase, previously purified to apparent homogeneity by affinity chromatography and immunoabsorption. Fluorescence was observed in the brush-border and glycocalyx of the duodenum and proximal 15 cm of jejunum distal to the D/J flexure. Distal jejunum and ileum as well as stomach and colon were consistently negative. Brunner's glands and goblet cells were never stained by specific antibody. Preliminary evidence was obtained that the human enterokinase molecule contains a specific antigenic determinant in its polypeptide component and a second determinant in the oligosaccharide moiety which cross-reacts with blood group A. Preliminary evidence was also obtained that mucosal synthesis of enterokinase may be impaired in jaundice due to carcinoma of the pancreas and induced in the small intestine distal to the normal limit of synthesis after pancreatico-duodenectomy.

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“…This and other evidence has led to the conclusion that entefokinase is not a brush border enzyme but a secretory enzyme which originates in the Brunner glands or the goblet cells (44,45,46,47), which are scarcely involved in the atrophy in celiac disease.…”

Section: Constipationmentioning

confidence: 99%