Tubular reabsorption of pepsinogen isozymogens in man studied by the inhibition of tubular protein reabsorption with dibasic amino acids

1991 ◽  
Vol 80 (2) ◽  
pp. 161-166 ◽  
Author(s):  
M. A. G. J. ten Dam ◽  
A. Zwiers ◽  
J. B. A. Crusius ◽  
G. Pals ◽  
G. J. van Kamp ◽  
...  
Keyword(s):  
Body Weight ◽  
Specific Binding ◽  
Tubular Reabsorption ◽  
Radioisotope Method ◽  
Pepsinogen C ◽  
Pepsinogen A ◽  
Fractional Clearance ◽  
Arginine Hydrochloride ◽  
Identical Amino Acid Sequence ◽  
Protein Reabsorption

1. The fractional clearances of pepsinogen A (PGA), pepsinogen C (PGC) and the main PGA isozymogens, i.e. PGA-3, PGA-4 and PGA-5, were measured in 13 healthy male volunteers before and during blockade of tubular protein reabsorption by intravenous infusion of either l-arginine hydrochloride (n = 8; 0.5 g h−1 kg−1 body weight) or an equimolar amount of l-lysine hydrochloride (n = 5; 0.44 g h−1 kg−1 body weight). Glomerular filtration rate was measured by a radioisotope method. 2. The fractional baseline clearance of PGC (1 ± 1%) was lower than that of PGA (20 ± 10%). In addition, the fractional clearance of the PGA isozymogens appeared to be different: the fractional clearance of PGA-5 (7 ± 3%) was lower than that of PGA-4 (18 ± 9%), and the fractional clearance of PGA-4 was lower than that of PGA-3 (30 ± 10%). These differences in fractional clearance between PGA isozymogens decreased during infusion of both arginine and lysine. 3. Pepsinogens are freely filtered proteins. It can therefore be concluded that the differences in fractional clearance between PGA isozymogens imply differences in tubular reabsorption. This is remarkable as PGA isozymogens are proteins with an almost identical amino acid sequence and electric charge. The disappearance of the differences in tubular reabsorption during arginine and lysine infusion suggests that PGA isozymogens differ in affinity for negatively charged binding sites in the tubular cell membrane. In order to explain the low fractional clearance of PGC compared with that of PGA and the less marked effect of arginine or lysine infusion on the fractional clearance of PGC, an additional PGC-specific binding site has to be postulated.

scholarly journals Diagnostic value of serum pepsinogen C in patients with raised serum concentrations of pepsinogen A.

Gut ◽  
1993 ◽  
Vol 34 (10) ◽  
pp. 1315-1318 ◽  
Author(s):  
I Biemond ◽  
J Kreuning ◽  
J B Jansen ◽  
C B Lamers
Keyword(s):  
Diagnostic Value ◽  
Serum Pepsinogen ◽  
Serum Concentrations ◽  
Pepsinogen C ◽  
Pepsinogen A

Ultrafiltration of renin in the mouse kidney studied by inhibition of tubular protein reabsorption with lysine

1988 ◽  
Vol 75 (3) ◽  
pp. 331-336 ◽  
Author(s):  
Ingrid Mazanti ◽  
Kirstine Lintrup Hermann ◽  
Arne Høj Nielsen ◽  
Knud Poulsen
Keyword(s):  
Intraperitoneal Injection ◽  
Excretion Rate ◽  
Plasma Renin ◽  
Basic Amino Acid ◽  
Tubular Reabsorption ◽  
Renal Tubules ◽  
Plasma Renin Concentration ◽  
Protein Reabsorption ◽  
Glomerular Ultrafiltration

1. In order to study the role of the kidney in the elimination of endogenous plasma renin, renin was measured in the plasma and urine of female mice. 2. The renin concentration was two orders of magnitude lower in urine than in plasma, but it increased after intraperitoneal injection of submandibular mouse renin. No correlation between the plasma renin concentration and the urinary renin concentration and renin excretion rate could be demonstrated. 3. Blockade of the tubular reabsorption of proteins by intraperitoneal injection of the basic amino acid lysine increased the urinary renin concentration, renin excretion rate and renin clearance two to three orders of magnitude, without affecting the plasma renin concentration. 4. This finding demonstrates that ultrafiltered renin is reabsorbed almost completely in the renal tubules and that the mechanism most likely is the same as for other filtered proteins. 5. The large renal renin clearance obtained after intraperitoneal lysine is in accordance with a major role of the kidneys in the elimination of renin from the circulation, by a glomerular ultrafiltration and tubular reabsorption and metabolization of renin.

Characterization of the sulfated glycopeptide of chicken pepsinogen

1982 ◽  
Vol 47 (2) ◽  
pp. 709-718 ◽  
Author(s):  
Miroslav Baudyš ◽  
Vladimír Kostka ◽  
Karel Grüner ◽  
Jan Pohl
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein Molecule ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Sugar Moiety ◽  
Pepsinogen A ◽  
Identical Amino Acid Sequence ◽  
High Voltage Electrophoresis

S-sulfonated chicken pepsinogen was digested with TPCK-trypsin; large tryptic peptides, separated on Sephadex G-25 fine, were subjected to additional cleavage with α-chymotrypsin. The hold-up fraction of the chymotryptic digest from the Sephadex G-25 column, was resolved by high voltage electrophoresis. The three most acidic zones contained glycopeptides of identical amino acid sequence Val-Ser-Thr-Asn-Glu-Thr-Val-Tyr, yet differed in the composition of the sugar moiety. These glycopeptides, moreover, bear different numbers of sulfate groups which enabled the resolution of the peptides. The most acidic glycopeptide contains 7 glucosamine residues, 3 mannose residues and 5 sulfate groups, the second one 6 glucosamine residues, 3 mannose residues and 4 sulfate groups and the slowest, minority glycopeptide, 5 glucosamine residues, 2 mannose residues and 2 sulfate groups. The entire sugar moiety is attached to one of the chain viaasparagine. In other experiments the glycopeptides were also isolated from the thermolytic digest of chicken pepsin; their C-terminal sequence was shorter by two amino acid residues. The tentative assignment of the glycopeptides to the amino acid sequence of pepsinogen resulted from the analysis of the limited tryptic digest of the whole protein molecule. Chicken pepsinogen is glycosylated at the site of the chain occupied by a phosphoserine residue in hog pepsinogen A.

Influence of nutrition and bovine growth hormone (GH) on hepatic GH binding, insulin-like growth factor-I and growth of lambs

1991 ◽  
Vol 128 (2) ◽  
pp. 181-186 ◽  
Author(s):  
J. J. Bass ◽  
J. M. Oldham ◽  
S. C. Hodgkinson ◽  
P. J. Fowke ◽  
H. Sauerwein ◽  
...  
Keyword(s):  
Body Composition ◽  
Body Weight ◽  
Growth Factor ◽  
Plasma Glucose ◽  
Specific Binding ◽  
Plasma Concentrations ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Igf I ◽  
Growth Factor I

ABSTRACT The effect on young lambs of 0·25 mg recombinant bovine GH (bGH)/kg per day on plasma concentrations of insulin-like growth factor-I (IGF-I), glucose, specific hepatic GH binding and body composition changes was examined at two levels of nutrition (lucerne pellets; 3 and 1·7% of body weight/day). Lambs on low levels of nutrition had low plasma IGF-I (P < 0·001). Plasma concentrations of IGF-I were increased by bGH treatment at both levels of nutrition, with the high nutrition group showing the greatest IGF-I response after 3 and 40 days of bGH treatment. Plasma glucose, after 40 days, was higher overall (P < 0·05) in lambs on high nutrition. bGH treatment increased plasma glucose, with the response being greater in the well-fed lambs. Specific binding of GH to liver membranes was highest in lambs on high nutrition and on bGH treatment; no significant interaction between nutrition and bGH treatment was detected, indicating that specific binding of GH was increased proportionally by bGH at both nutritional levels. The major change in body composition was the reduced level of fatness in lambs treated with bGH. There was no significant effect of bGH on body weight although bGH treatment tended to increase weight gain of well-fed lambs and decreased weight loss of poorly nourished lambs. The results show that, although there was a significant (P < 0·05) bGH/nutrition interaction for IGF-I there was no such interaction for body weight/components or specific GH binding to the liver. The results indicate that an increase in plasma IGF-I does not necessarily result in increases in growth or changes in carcass composition. Journal of Endocrinology (1991) 128, 181–186

scholarly journals Radioimmunoassay of Human Pepsinogen A and Pepsinogen C

1989 ◽  
Vol 27 (1) ◽  
Author(s):  
I. Biemond ◽  
J. B. M. J. Jansen ◽  
L. F. S. J. Crobach ◽  
Johanna Kreuning ◽  
C. B. H. W. Lamers
Keyword(s):  
Pepsinogen C ◽  
Pepsinogen A

Renal handling of pepsinogens A and C in man

1988 ◽  
Vol 75 (6) ◽  
pp. 649-654 ◽  
Author(s):  
Reinier W. ten Kate ◽  
Gerard Pals ◽  
Jan C. Pronk ◽  
Ruud A. Bank ◽  
Aldur W. Eriksson ◽  
...  
Keyword(s):  
Healthy Subjects ◽  
Fractional Excretion ◽  
Renal Diseases ◽  
Sharp Rise ◽  
Renal Handling ◽  
Pepsinogen C ◽  
Pepsinogen A ◽  
Glomerular Filtrate ◽  
The Mean ◽  
Positively Charged

1. Fractional excretions of pepsinogens A and C in the urine were investigated in 21 healthy subjects and in 38 patients with chronic renal insufficiency. In eight of the healthy subjects fractional excretions were measured again after oral administration of omeprazole for 9 days. 2. The mean fractional excretion of pepsinogen A was 27.6% (range 4.4–73.9%) in healthy subjects and remained unchanged after omeprazole administration. In patients with renal failure the mean fractional excretion of pepsinogen A was 37.9% (range 7.0–81.9%). The mean fractional excretion of pepsinogen C was 1.0% (range 0.04–6.8%) in healthy subjects and decreased after omeprazole. In patients with chronic renal diseases a sharp rise in fractional excretion of pepsinogen C was observed once glomerular filtration rate was less than 40 ml/min. 3. Fractional excretion of pepsinogen A was unexpectedly high for a negatively charged protein with a molecule mass of 40 000 daltons. This might be explained by the presence of the positively charged activation peptide. Furthermore, pepsinogen C seemed to be almost entirely reabsorbed from the glomerular filtrate and a tubular reabsorption maximum appeared to be present. Pepsinogen C may, therefore, be a new marker of tubular function. The cause of the remarkable difference in tubular handling of two quite similar low-molecular-mass proteins remains to be elucidated.

The Effect of a Carbohydrate-Arginine Supplement on Postexercise Carbohydrate Metabolism

1999 ◽  
Vol 9 (3) ◽  
pp. 241-250 ◽  
Author(s):  
Ben B. Yaspelkis ◽  
John L. lvy
Keyword(s):  
Body Weight ◽  
Carbohydrate Metabolism ◽  
Blood Lactate ◽  
Body Mass ◽  
Plasma Glucose ◽  
Muscle Glycogen ◽  
Exercise Bout ◽  
Glycogen Storage ◽  
Arginine Hydrochloride ◽  
Glycogen Stores

The effect of a carbohydrate-arginine supplement on postexercise muscle glycogen storage was investigated. Twelve well-trained cyclists rode for 2 hr on two separate occasions to deplete theirmuscle glycogen stores. At 0, l, 2, and 3 hr after each exercise bout, the subjects ingested either a carbohydrate (CHO) supplement (1 g carbohydrate/kg body weight) or a carbohydrate-arginine (CHO/AA) supplement (1 g carbohydrate/kg body mass and 0.08 g arginine-hydrochloride/kg body weight). No difference in rate of glycogen storage was found between the CHO/AA and CHO treatments, although significance was approached. There were also no differences in plasma glucose, insulin, or blood lactate responses between treatments. Postexercise carbohydrate oxidation during the CHO/AA treatment was significantly reduced compared to the CHO treatment. These results suggest that the addition of arginine to a CHO supplement reduces the rate of CHO oxidation postexercise and therefore may increase the availability of glucose for muscle glycogen storage during recovery.

scholarly journals Pepsinogen A, pepsinogen C, and gastrin as markers of atrophic chronic gastritis in European dyspeptics

2003 ◽  
Vol 88 (8) ◽  
pp. 1239-1247 ◽  
Author(s):  
N Broutet ◽  
◽  
M Plebani ◽  
C Sakarovitch ◽  
P Sipponen ◽  
...  
Keyword(s):  
Chronic Gastritis ◽  
Pepsinogen C ◽  
Pepsinogen A
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