Release of Active and Inactive Kallikrein from the Isolated Perfused Rat Kidney

1984 ◽  
Vol 66 (2) ◽  
pp. 207-215 ◽  
Author(s):  
B. H. Van Leeuwen ◽  
S. M. Grinblat ◽  
C. I. Johnston

1. The release of kallikrein into the perfusate and urine of the isolated perfused rat kidney was studied. 2. Comparison between enzymic and immunological assays for kallikrein demonstrated the presence of an enzymically inactive form of kallikrein. 3. Of kallikrein found in normal rat urine 77 ± 4% is active and 23% is in an inactive form. 4. In the isolated perfused rat kidney a similar proportion of active kallikrein (84%) was excreted into the urine but very little enzymically active kallikrein (2%) could be detected in the perfusate. 5. However, significant amounts of enzymically inactive but immunologically reactive kallikrein could be found in the kidney perfusate. The rate of release of kallikrein into the perfusate was approximately one-fifth of the rate of release into the urine. 6. Renin showed a similar pattern of release into the perfusate and urine but the lysosomal enzyme marker acid phosphatase was not detectable. 7. These results show that kallikrein is secreted from the kidney into the circulation as well as being excreted in the urine. However, in urine the enzyme is predominantly in an enzymically active form whereas it is secreted into the circulation in an inactive form.

1975 ◽  
Vol 53 (8) ◽  
pp. 930-933 ◽  
Author(s):  
P. Wadoux ◽  
T. C. Welbourne

The contribution of D-glutamyltransferase (D-GT) (EC 2.3.2.1) to total renal ammonia production was determined by employing DL-methionine-DL-sulfoximine (MSO) as an inhibitor of D-GT. Rat kidney homogenates were assayed for NH3-liberating activity under optimal D-GT or γ-glutamyltranspeptidase (γ-GTP) (EC 2.3.2.2) conditions. MSO inhibits only D-GT activity. The contribution of D-GT to total renal ammonia production was then evaluated in the isolated perfused rat kidney employing identical substrate (5 mML-glutamine) and inhibitor (15 mM MSO) concentrations as employed in the homogenate study. Under these conditions, MSO inhibits 70% of the total ammonia production by the normal kidney; in addition, the ratio of ammonia produced per glutamine taken up rose from 1.0 to 1.8. In kidneys from chronically acidotic rats, MSO reduced total ammonia production only 35% while the NH3/glutamine ratio rose from 1.0 to 1.8. D-GT appears to be the predominant source of NH3 production in the normal rat kidney; γ-GTP does not contribute significantly. The rise in the NH3/glutamine ratio after D-GT inhibition is consistent with glutamine utilization via the activated mitochondrial glutaminase (EC 3.5.1.2) – glutamate dehydrogenase (EC 1.4.1.2) pathway.


1991 ◽  
Vol 25 (3) ◽  
pp. 195-204 ◽  
Author(s):  
Takano Takehito ◽  
Nakata Kazuyo ◽  
Kawakami Tsuyoshi ◽  
Miyazaki Yoshifumi ◽  
Murakami Masataka ◽  
...  

1979 ◽  
Vol 2 (1) ◽  
pp. 1-11
Author(s):  
Richard Solomon ◽  
Patricio Silva ◽  
Franklin H. Epstein

1987 ◽  
Vol 43 (6) ◽  
pp. 795-799 ◽  
Author(s):  
David R. Luke ◽  
Bertram L. Kasiske ◽  
Gary R. Matzke ◽  
Walid M. Awni ◽  
William F. Keane

1990 ◽  
Vol 126 (3) ◽  
pp. 403-408 ◽  
Author(s):  
A. G. Ellis ◽  
W. R. Adam ◽  
T. J. Martin

ABSTRACT The isolated perfused rat kidney was used to study the effects of amino-terminal fragments of human parathyroid hormone, hPTH(1–34), bovine parathyroid hormone, bPTH(1–84) and of PTH-related proteins, PTHrP(1–34), PTHrP(1–84), PTHrP(1–108) and PTHrP(1–141) on urinary bicarbonate excretion. PTHrP(1–34) (7 nmol/l), bPTH(1–84) (5·5 nmol/l) and hPTH(1–34) (7 nmol/l) had similar effects in increasing bicarbonate excretion with respect to the control. At lower concentrations (0·7 nmol/l) all PTHrP components, but not hPTH(1–34) or bPTH(1–84) increased bicarbonate excretion significantly. Infusions of PTHrP(1–108) and PTHrP(1–141) at 0·7 nmol/l, while associated with a rise in urinary bicarbonate concentration and excretion during the early stages of perfusion, produced a sharp decline in bicarbonate concentration and excretion in the latter part of perfusion. The different peptides produced no significant differences in glomerular filtration rate, fractional excretion of sodium or urine volume. The absence of substantial differences between the effects of hPTH(1–34) and PTHrP(1–34) are as noted in previous studies. The differences between PTHrP(1–108)/PTHrP(1–141) and PTHrP(1–34) demonstrated here are consistent with (1) the clinical manifestations of acidosis in hyperparathyroidism and alkalosis in humoral hypercalcaemia of malignancy, and (2) an independent action of a component of PTHrP beyond amino acids 1–34. Journal of Endocrinology (1990) 126, 403–408


2008 ◽  
Vol 22 (S1) ◽  
Author(s):  
Patricia Fiorino ◽  
Vera Azevedo Farah ◽  
Kalebe G Darini ◽  
Iara Cristina Araujo ◽  
Ana Paula Oliveira Leite ◽  
...  

1985 ◽  
Vol 229 (2) ◽  
pp. 545-549 ◽  
Author(s):  
M Lowry ◽  
D E Hall ◽  
J T Brosnan

Isolated perfused rat kidneys removed considerable quantities of glycyltyrosine, glycylhydroxyproline, tetraglycine and prolylhydroxyproline from the perfusate. The component amino acids are released into the perfusate and, in the case of the glycine-containing peptides, there is increased synthesis of serine. Removal of peptides was more than could be accounted for on the basis of filtration, so antiluminal metabolism is indicated. Metabolism of such peptides by the kidney may contribute to renal serine synthesis in vivo.


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