S�urestabile Proteaseninhibitoren im Blutplasma bei verschiedenen Nephropathien

Hochstrasser, K; Feuth, H.; Fall, J.; Kemkes, B. M.

doi:10.1007/bf01494274

Cited by 16 publications

(4 citation statements)

References 6 publications

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“…However, chromatographic analysis of the skin of normal and anephric animals indicated that the difference was due to the release of degradation products from the kidneys. Using autoradiography, we could detect radiolabelled bikunin in the tubules of the kidneys shortly after intravenous injection (Figure 4), supporting the idea that, despite its relatively large hydrodynamic size and high negative charge, bikunin is cleared by the kidneys via glomerular filtration [36]. The fact that the ' effective radius' of extended polymers in glomerular filtration is smaller than their hydrodynamic radius [37] could account for this property of bikunin.…”

Section: Discussionsupporting

confidence: 52%

“…These results indicate that the non-renal uptake system is saturated at physiological concentrations, implying that it is a receptor-mediated process and does not occur by leakage between or through vascular cells. These findings and the observation that the plasma level of bikunin, except in renal diseases [36], is relatively constant under various conditions [42] is difficult to reconcile with the fact that bikunin seems to be a mitogen for endothelial cells and fibroblasts [12,13].…”

Section: Discussionmentioning

confidence: 99%

“…Trypsin was obtained from Boehringer-Mannheim, Mannheim, Germany, 35S04 (22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37)(38)(39)(40) Ci/mg) from Amersham International, Amersham, Bucks., U.K. and sodium 5-sec-butyl-5-ethyl-2thiobarbiturate (Inactin) from Byk-Gulden, Konstanz, Germany.…”

Section: Materials and Methods Chemicalsmentioning

confidence: 99%

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Plasma clearance of rat bikunin: evidence for receptor-mediated uptake

Sjöberg

Blom

Larsson

et al. 1995

Biochemical Journal

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Bikunin is a chondroitin sulphate-containing protease inhibitor with a molecular mass of 25 kDa. It is secreted into the blood by hepatocytes, and recent observations indicate that it may have an extravascular function. Here we have studied the plasma clearance of bikunin in rats and mice. On intravenous injection, radiolabelled bikunin was found to have a half-life of 10 min; in rats with ligated renal arteries, the clearance time was twice as long, implying that the kidneys account for half the uptake. As judged by gel filtration, the size of bikunin is similar to that of albumin. Autoradiographic analysis of kidneys removed 2 min after the injection of radiolabelled bikunin indicated that, despite its size, bikunin is cleared by glomerular filtration. On ligation of the renal arteries, the plasma concentration of bikunin increased linearly to at least four times normal. This finding shows that the non-renal uptake system is saturated and therefore presumably receptor-mediated. Most of the non-renal uptake of injected bikunin was found to occur in non-visceral tissues such as the skin. Analysis of skin samples by autoradiography after injection of radiolabelled bikunin suggested that bikunin had been transferred from the plasma to the interstitial space.

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Section: Discussionsupporting

confidence: 52%

Section: Discussionmentioning

confidence: 99%

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Plasma clearance of rat bikunin: evidence for receptor-mediated uptake

Sjöberg

Blom

Larsson

et al. 1995

Biochemical Journal

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“…The action of trypsin on the inter-a-trypsin inhibitor releases an acid-stable inhibitor with a molecular weight of 17000 (apparent molecular weight 22000) and immunological cross reaction with the precursor via an intermediate trypsin-inhibitor complex, TI-17. In addition, the physiological 1-34, liberated in an active form, can be transformed by trypsin via the trypsin-inhibitor complex TI-34 to [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17] be concluded that the first step of the degradation of inter-<x-trypsin inhibitor by trypsin is the formation of a complex between the inhibitor and trypsin. An excess of trypsin then digests that part of the inter-a-trypsin inhibitor which is not effective for the inhibitory activity of the molecule.…”

Section: Discussionmentioning

confidence: 99%

The Inter-α-Trypsin Inhibitor as Precursor of the Acid-Stable Proteinase Inhibitors in Human Serum and Urine

Hochstrasser¹,

Bretzel²,

Feuth³

et al. 1976

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

113

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A small amount of antitryptic activity is detectable in the supernatant of deproteinized human serum. Preincubation of serum with trypsin causes an increase in acid-stable antitryptic activity. This rise in activity depends on the inter--trypsin inhibitor concentration. The native inhibitor present in normal sera, and in higher concentrations in sera of patients with nephropathies, and the trypsin-liberated inhibitor show immunological cross reaction with antibodies to the serum inter-a-trypsin inhibitor. The two inhibitors differ in molecular weight and electrophoretic mobility. The physiological inhibitor (1-34), with a molecular weight of 34000 and a high carbohydrate content, can be transformed by trypsin into an inhibitor (1-17) with a molecular weight of 17 000. This inhibitor is identical with the inhibitors liberated by trypsin from serum or from purified inter-a-trypsin inhibitor. The acid-stable inhibitor from urine is identical with the physiological serum inhibitor. Analogously, this inhibitor is transformed by trypsin into the inhibitor with a molecular weight of 17000. We conclude that the inter-a-trypsin inhibitor is the precursor of both the physiological and the trypsin-liberated inhibitor. By a mechanism as yet unknown, but most likely a limited proteolysis, the secreted inhibitor is liberated from the high molecular weight precursor. In contrast to the monospecific trypsin-inhibiting precursor, the physiological and artificially liberated inhibitors are trypsin/chymotrypsin/plasmin inhibitors. Der Inter-oL-Trypsininhibitor als Vorstufe der säurestabilen Proteaseninhibitoren im menschlichen Serum und HarnZusammenfassung: Nach Enteiweißung von menschlichem Serum verbleibt im Überstand eine geringe antitryptische Aktivität. Diese Aktivität erhöht sich nach Inkubation des Serums mit Trypsin. Die Höhe der so freilegbaren Aktivität hängt von der Inter-a-Trypsininhibitor-

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