Protein synthesis in the pancreas of the rat after stimulation of secretion

Kramer, M. F.; Poort, C.

doi:10.1007/bf00324859

Cited by 53 publications

(24 citation statements)

References 31 publications

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“…Several conflicting results concerning the effect of stimulation of pancreatic secretion on the rate of protein synthesis have been published in the past (Daly & Mirsky, 1953;Allfrey et al, 1954;Ferreira et al, 1955 ;Farber & Sidransky, 1956;Hokin, 1956;Busch et al, 1959;Stocker, 1962;Webster & Tyor, 1966;Peakall, 1967;Webster, 1968;Kramer & Poort, 1968;Poort & Geuze, 1969;Poort & Kramer, 1969). As pointed out by Poort & Kramer (Kramer & Poort, 1968;Poort & Kramer, 1969) it is possible to reconcile most of the discrepancies by taking into account the fact that in a protein-secreting gland the amount of protein present Values given are averages ±S.E.…”

Section: Discussionmentioning

confidence: 99%

“…Though several conflicting results have been obtained in the past, recent studies seem to indicate that a substantial increase of the rate of protein synthesis is brought about by either feeding or pharmacological stimulation of secretion only in birds and frogs (Webster & Tyor, 1966: Peakall, 1967Webster, 1968;Poort & Geuze, 1969); whereas in mammals protein synthesis proceeds at a constant rate, independently of secretion (Kramer & Poort, 1968;Poort & Kramer, 1969).…”

Section: Introductionmentioning

confidence: 99%

“…Numerous studies dealing with the effect of stimulation of enzyme secretion on the rate of protein synthesis in the pancreas have been reported (Daly & Mirsky, 1953;Allfrey, Daly & Mirsky, 1954;Ferreira Fernandez & Junqueira, 1955;Farber & Sidransky, 1956;Hokin, 1956;Busch, Allen & Anderson, 1959;Stocker, 1962;Webster & Tyor, 1966;Peakall, 1967;Webster, 1968;Kramer & Poort, 1968;Poort & Geuze, 1969;Poort & Kramer, 1969). Though several conflicting results have been obtained in the past, recent studies seem to indicate that a substantial increase of the rate of protein synthesis is brought about by either feeding or pharmacological stimulation of secretion only in birds and frogs (Webster & Tyor, 1966: Peakall, 1967Webster, 1968;Poort & Geuze, 1969); whereas in mammals protein synthesis proceeds at a constant rate, independently of secretion (Kramer & Poort, 1968;Poort & Kramer, 1969).…”

Section: Introductionmentioning

confidence: 99%

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Effect of caerulein on protein synthesis and secretion in the guinea‐pig pancreas

Meldolesi¹

1970

British J Pharmacology

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Summary1. Caerulein produced a striking increase in the rate of secretion of the guineapig pancreas. When tested in vivo with pancreatic slices its optimal concentration was found to be 2-5 ng/ml. It is concluded (a) that in the guinea-pig pancreas, stimulation of enzyme secretion does not affect per se the rate of synthesis of digestive enzymes; and (b) that the increase of protein synthesis elicited by caerulein is critically dependent both on the nature of the segretagogue (that is, it is elicited by the polypeptide but not by a cholinergic drug) and on the experimental conditions (it is evident only in fasted animals after prolonged treatment).Introduction Numerous studies dealing with the effect of stimulation of enzyme secretion on the rate of protein synthesis in the pancreas have been reported

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Effect of caerulein on protein synthesis and secretion in the guinea‐pig pancreas

Meldolesi¹

1970

British J Pharmacology

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“…These studies [ 1,21 were performed on fasting animals, fed animals and animals which were stimulated to secrete by pilocarpine. The possible influence of an altered specific radioactivity of the precursor pool in these studies was discussed but not actually measured.…”

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confidence: 99%

Relationship between Extracellular Amino Acids and Protein Synthesis in vitro in the Rat Pancreas

Venrooij¹,

Poort

Kramer

et al. 1972

European Journal of Biochemistry

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1. The uptake and incorporation in vitro of radioactive leucine and lysine in rat pancreas fragments have been studied.2. The uptake and incorporation of both leucine and lysine were found t o be influenced by the concentration of leucine in the medium.3. Extracellular and intracellular free amino acids can be distinguished by washing the tissue fragments a t 0 "C.4. Though it takes some 20 min for each of both radioactive amino acids to reach maximum concentration in the intracellular soluble amino acid pool, their incorporation into protein becomes linear shortly after the start of incubation in a medium with labelled amino acids.5. I n chase-type experiments the incorporation of each of both radioactive amino acids stops immediately when the labelled medium is replaced by unlabelled medium, though the free, intracellular amino-acid radioactivity declines only slowly.6. These results indicate that in the pancreas of the fasting rat in vitro the amino acid molecules incorporated into protein are derived from the cxtracellular pool. Other molecules enter and leave the intracellular amino acid pool but do not contribute to incorporation.I n earlier studies from our laboratory it was found that the rate of protein synthesis as measured by the rate of incorporation of radioactive amino acid in the rat pancreas was not influenced by the extent to which pancreatic cells are filled with secretory granules nor by the actual process of secretion. These studies [ 1,21 were performed on fasting animals, fed animals and animals which were stimulated to secrete by pilocarpine. The possible influence of an altered specific radioactivity of the precursor pool in these studies was discussed but not actually measured. The role of the intracellular amino acid pool in cellular metabolism has not been defined, but one of its functions has been assumed to be that of an obligatory precursor pool for protein synthesis. This assumption has been seriously questioned as a result of studies with rat diaphragm I n our studies in vitro with rat pancreas fragments we measured the influx of radioactive lysine and leucine from the medium into the intracellular amino acid pool and into cellular protein. Our results suggest that the amino acids used for protein synthesis are utilized directly from the extracellular fluid and not from the intracellular pool. Unlabelled amino acids were from Sigma Chem. Co. and Fluka; cycloheximide was obtained from Sigma Chem. Co.Young adult male rats (about 200g) from the Wistar strain and obtained from TNO (Holland) were fed ad lib. until 24 h before the expcriment. IncubationAfter decapitat,ion the pancreas was cut out and fragmented with the TC-2 Sorvall Tissue Sectioner into pieces of 1 mm3 each. About 50 mg fragmented pancreas was incubated a t 37 "C for 10 min in a conical flask containing 2 ml Krebs-Ringer bicarbonate buffer in which the KC1 concentration was raised to 13 ml. I n addition, the complete medium (pH 7.6) contained all amino acids in about the same concentrations as in rat plasma [7], the fo...

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“…Possibly because of the is mediated in part by the polypeptidic hormones, different systems and techniques used to stimupancreozymin and secretin . The specific physlate secretion or measure protein biosynthesis, iological role of these two hormones is now well opposite conclusions have been reached (Hokin, established. Pancreozymin is known to promote 1953 ; Siekevitz and Palade, 1958 ; Webster and the secretion of hydrolytic enzymes from the Tyor, 1966 ;Kramer and Poort, 1968) . Taking pancreas, while secretin acts on the secretion of advantage of the methods set up in our laboratory water and salts (Harper, 1967) .…”

Section: Introductionmentioning

confidence: 99%

Effect of Pancreozymin on Rat Pancreatic Enzyme Biosynthesis

Reggio

Cailla-Deckmyn

Marchis-Mouren

1971

The Journal of Cell Biology

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Pancreatic enzyme secretion in rats anesthesized by pentobarbital was stimulated by intravenous perfusion of the hormone pancreozymin, as indicated by a decreased amylase level in the pancreas and by specific, fine structural changes observed in an electron microscope . Rates of protein synthesis were determined by pulse labeling . Amylase, total protein, and valine were purified from pancreas and counted . Pancreozymin promotes an 8 to 10 times increase in the rate of biosynthesis of pancreatic enzymes, as compared to rats similarly anesthesized but without hormone . This stimulation effect is obtained very rapidly (2 hr) and is not inhibited by actinomycin D. Secretin alone has no effect, whereas pentobarbital is inhibitory .

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Protein synthesis in the pancreas of the rat after stimulation of secretion

Cited by 53 publications

References 31 publications

Effect of caerulein on protein synthesis and secretion in the guinea‐pig pancreas

Effect of caerulein on protein synthesis and secretion in the guinea‐pig pancreas

Relationship between Extracellular Amino Acids and Protein Synthesis in vitro in the Rat Pancreas

Effect of Pancreozymin on Rat Pancreatic Enzyme Biosynthesis

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