[Human pancreatic proteins in normal and pathological states].
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Humans↗
Biomedical subjects
O Guy-Crotte
Publications and source records attributed to O Guy-Crotte.
Physiologically elevated concentration of serum trypsin-like immunoreactivity in newborns. Comparison with lipase.
Comparative measurements on the levels of immunoreactive trypsin(ogen)-1 and lipase have been performed on newborn and adult sera. Values observed for immunoreactive trypsin(ogen)-1 with newborn sera are more dispersed and significantly higher (mean +/- SD, 31.9 +/- 12.9 micrograms/l) than the values obtained with adult sera (20.2 +/- 7.3 micrograms/l). The molecular size distribution of the immunoreactive trypsin-like material in newborns was studied by gel filtration. This material was eluted with a molecular weight of 25,000 which eliminates the possibility of an increased intestinal permeability of active trypsin which would be bound to serum protease inhibitors. In contrast to trypsin values, the mean serum lipase value at birth was significantly lower (7.0 +/- 3.2 micrograms/l) than the value observed for adults (26.9 +/- 8.2 micrograms/l). The possibility of an adaptation process in newborns is evoked.
Adult↗
Characterization and N-terminal sequence of a degradation product of 14,000 molecular weight isolated from human pancreatic juice.
Chromatography of human pancreatic juice has allowed the isolation of an inactive protein of 14,000 Mr (protein X) and the determination of its amino acid composition and N-terminal sequence. Protein X was found to be immunologically identical to the protein extracted from precipitates present in the pancreatic juices of patients with chronic calcifying pancreatitis and recently shown to be a degradation product of trypsinogen 1. The same chromatography performed in the presence of lima bean trypsin inhibitor has permitted the isolation of precursors of approximately congruent to 19,000 Mr which can be transformed into protein X "in vitro" by chymotrypsin hydrolysis. These results emphasize the easy activation of human pancreatic zymogens and the possible consequences due to proteolysis in pancreatic disease.
Amino Acid Sequence↗
Proteolysis of human trypsinogen 1. Pathogenic implication in chronic pancreatitis.
SDS electrophoresis on polyacrylamide gels of purified trypsinogen 1 has shown the occurrence of a proteolysis in some molecules during long storage at -20 degrees C. This proteolyzed trypsinogen gives a positive reaction with an antiserum directed against the precipitate protein, major protein of about 14 000 molecular weight extracted from precipitates present in the pancreatic juice of patients with chronic pancreatitis. The autoactivation of proteolyzed trypsinogen 1 liberates a polypeptide of 14 000 molecular weight which is immunologically identical to the precipitate protein. These results show that the major protein present in pancreatic precipitates (and pancreatic stones) of patients with chronic pancreatitis is a degradation product of trypsinogen 1 liberated by a proteolysis which necessarily requires a premature zymogen activation in the disease.
Chronic Disease↗
Detection of the cystic fibrosis protein by isoelectric focusing of serum and plasma.
We used the isoelectric focusing method developed by Wilson to analyze serum from individuals homozygous or heterozygous for cystic fibrosis. The presence of cystic fibrosis protein (CFP) was found in 37 out of 52 homozygous and 24 out of 34 heterozygous patients, which leads to a frequency of 71% for both families. Five out of 24 controls were found positive. The same study, performed on 26 plasma samples collected from the same patients, demonstrated that the detection of CFP is possible in plasma as well as in serum. Our results confirm the presence of a protein "marker" of CF in serum, but also underlines the lack of sensitivity of the isoelectric focusing technique to be used for diagnosis.
Blood Proteins↗
Isolation and characterization of colipase from porcine and human pancreatic juice by immunoaffinity chromatography.
Pure colipase was prepared by immunoaffinity chromatography from porcine and human pancreatic juice. A single form of the porcine colipase was obtained, having the structural and biological properties of previously characterized porcine procolipase A. Two forms of activated colipase (N-terminal Gly) were isolated from human pancreatic juice by the same procedure. The existence of two forms of activated colipase might arise from rapid activation of a precursor form of human colipase during collection of the pancreatic juice.
Animals↗
Cystic fibrosis proteins detected by electrophoretic techniques.
For the detection of the cystic fibrosis protein (CFP) in serum of cystic fibrosis (CF) carriers, thin-layer polyacrylamide gel isoelectric focusing proved inappropriate as a diagnostic test, but was useful for screening fractions on purification of CFP by chromatofocusing on a Mono P column. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis an Mr 12,000 protein (P12) was found in most CFP-positive sera, indicating good correlation between these two CF-associated proteins. Detection of the P12 protein by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was well reproducible and less delicate than IEF. The technique was also used to purify P12 from serum by two successive preparative electrophoresis steps in a 7.5-15% gradient and 15% homogeneous gel. The use of silver staining revealed that P12, which was present in all sera of CF patients and carriers with variable intensities, was also present in trace amounts in normal sera.
Blood Proteins↗
Pancreatic proteins in normal state and pancreatic diseases in pancreatic juice and blood.
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Adult↗