The intracellular localization of kallikrein, trypsin and amylase in dog pancreas

Bhoola, K. D.; Dorey, Gundula

doi:10.1113/jphysiol.1971.sp009448

Cited by 9 publications

(2 citation statements)

References 20 publications

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“…Both enzymes were completely inactive after 1 week at room temperature, but, whereas only 30% of cyclic AMP phosphodiesterase activity was lost after 1 week at 40C, cyclic GMP phosphodiesterase was completely inactivated under these conditions ( Table 2). The pancreas contains powerful proteolytic enzyme precursors (zymogens), which can be activated by autocatalytic mechanisms (Bhoola & Dorey, 1971). It is possible that such proteolytic enzymes may contribute to the lability of cyclic nucleotide phosphodiesterase activity during storage, and hence the effect of Trasylol, which inhibits trypsin-like proteolytic enzymes, was measured.…”

Section: Inactivation Of Cyclic Nucleotide Phosphodiesterase On Storagementioning

confidence: 99%

The metabolism of cyclic nucleotides in the guinea-pig pancreas. Cyclic AMP phosphodiesterase and cyclic GMP phosphodiesterase

Methven

Lemon

Bhoola

1980

Biochemical Journal

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Both cyclic AMP phosphodiesterase and cyclic GMP phosphodiesterase were recovered mainly from the supernatant fractions of guinea-pig pancreas, but a higher proportion of the activity of the former was associated with the pellet fractions. The activities in the supernatant were not separated by gel filtration, but were clearly separated by subsequent chromatography on an anion-exchange resin. The activities of cyclic AMP phosphodiesterase and cyclic GMP phosphodiesterase had high-affinity (K(m) 6.5+/-1.1mum and 31.9+/-3.9mum respectively) and low-affinity (K(m) 0.56+/-0.05mm and 0.32+/-0.03mm respectively) components. The activity of neither enzyme was affected by the pancreatic secretogens, cholecystokinin-pancreozymin, secretin and carbachol. Removal of ions by gel filtration resulted in a marked reduction in cyclic nucleotide phosphodiesterase activity, which could be restored by addition of Mg(2+). Mn(2+) (3mm) was as effective as Mg(2+) (3mm) in the case of cyclic AMP phosphodiesterase, but was less than half as effective in the case of cyclic GMP phosphodiesterase. The metal-ion chelators, EDTA and EGTA, also decreased activity. Ca(2+) (1mm) did not affect the activity of cyclic nucleotide phosphodiesterase when the concentration of Mg(2+) was 3mm. At concentrations of Mg(2+) between 0.1 and 1mm, 1mm-Ca(2+) was activatory, and at concentrations of Mg(2+) below 0.1mm, 1mm-Ca(2+) was inhibitory. These results are discussed in terms of the possible significance of cyclic nucleotide phosphodiesterase in the physiological control of cyclic nucleotide concentrations during stimulus-secretion coupling.

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Section: Inactivation Of Cyclic Nucleotide Phosphodiesterase On Storagementioning

confidence: 99%

The metabolism of cyclic nucleotides in the guinea-pig pancreas. Cyclic AMP phosphodiesterase and cyclic GMP phosphodiesterase

Methven

Lemon

Bhoola

1980

Biochemical Journal

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“…Tissue-dependent differences in kallikrein content and labelling Table 1 shows that immunoreactive kallikrein content varies widely. Higher concentrations in submaxillary gland and pancreas presumably reflect the existence of kallikrein in storage granules in these tissues (Simson et al, 1979;Bhoola & Dorey, 1971;0rstavik et al, 1975). Kallikrein specific radioactivity (kallikrein c.p.m./mg of kallikrein) also varies widely, being significantly higher (P<0.05) in colon or kidney than in submaxillary gland or pancreas (Table 1).…”

Section: Evaluation Of Antiserum Specificitymentioning

confidence: 99%

Tissue kallikrein synthesis and its modification by testosterone or low dietary sodium

Miller¹,

Chao²,

Margolius³

1984

Biochemical Journal

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A method has been developed to measure the relative rate of rat tissue kallikrein synthesis which employs a specific antiserum raised against a purified rat urinary kallikrein. Incorporation of [35S]methionine into kallikrein and protein 20 min after intraperitoneal injection was measured in submaxillary gland, pancreas, kidney and descending colon. Kallikrein content was measured with a direct radioimmunoassay, and kallikrein-specific incorporation of [35S]methionine measured after immunoprecipitation. Kallikrein specific radioactivity (c.p.m./mg of enzyme) was about 100-fold greater than that in total protein in both kidney and colon. In contrast, in pancreas the incorporation into the enzyme was only 5-fold higher than into protein, and in submaxillary gland the incorporation was equivalent. Measured as kallikrein-specific radioactivity relative to total protein radioactivity incorporated in 20 min, kallikrein represents 0.18% of total protein synthesis in the kidney, 0.34% in the pancreas, 0.41% in the colon, but 7.29% in the submaxillary gland. Dietary Na+ restriction increased the relative rate of kallikrein synthesis 1.8-fold in the kidney without a comparable effect in submaxillary gland. In contrast, testosterone increased the relative rate of synthesis 2.3-fold in submaxillary gland, but decreased it in kidney. The data show that endogenous kallikrein synthesis differs markedly in various tissues, and that interventions which are known to change kallikrein content or excretion also change the relative rate of enzyme synthesis.

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Physiologie des exokrinen Pankreas

Forell¹,

Stahlheber²,

Lehnert³

et al. 1976

Pankreas

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The intracellular localization of kallikrein, trypsin and amylase in dog pancreas

Cited by 9 publications

References 20 publications

The metabolism of cyclic nucleotides in the guinea-pig pancreas. Cyclic AMP phosphodiesterase and cyclic GMP phosphodiesterase

The metabolism of cyclic nucleotides in the guinea-pig pancreas. Cyclic AMP phosphodiesterase and cyclic GMP phosphodiesterase

Tissue kallikrein synthesis and its modification by testosterone or low dietary sodium

Physiologie des exokrinen Pankreas

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