Measurement of urinary kallikrein activity species differences in kinin production

Alhenc-Gélas, François; Marchetti, Jeannine; Allegrini, J; Corvol, Pierre; Ménard, Joël

doi:10.1016/0304-4165(81)90262-2

Cited by 101 publications

(30 citation statements)

References 28 publications

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“…This rat kallikrein, however, does not cleave a Met-Lys bond; instead, it releases bradykinin by cleaving the Lys-Arg and Arg-Arg bonds in bovine and rat kininogens, respectively (Alhenc-Gelas et al, 1981;Kat0 et al, 1985). Like human kininogen, bovine kininogen contains the sequence MetLys-Arg.…”

Section: Structural Basis For Altered Spec$city Of Rat Kallikreinmentioning

confidence: 99%

Crystal structure of recombinant human tissue kallikrein at 2.0 Å resolution

et al. 1998

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Human tissue kallikrein, a trypsin-like serine protease involved in blood pressure regulation and inflammation processes, was expressed in a deglycosylated form at high levels in Pichia pastoris, purified, and crystallized. The crystal structure at 2.0 8, resolution is described and compared with that of porcine kallikrein and of other trypsin-like proteases. The active and S1 sites (nomenclature of Schechter I, Berger A, 1967, Biochem Biophys Res Commun 27:157-162) are similar to those of porcine kallikrein. Compared to trypsin, the S1 site is enlarged owing to the insertion of an additional residue, cis-Pro 219. The replacement Tyr 228 -+ Ala further enlarges the S1 pocket. However, the replacement of Gly 226 in trypsin with Ser in human tissue kallikrein restricts accessibility of substrates and inhibitors to Asp 189 at the base of the SI pocket; there is a hydrogen bond between and These changes in the architecture of the S1 site perturb the binding of inhibitors or substrates from the modes determined or inferred for trypsin. The crystal structure gives insight into the structural differences responsible for changes in specificity in human tissue kallikrein compared with other trypsin-like proteases, and into the structural basis for the unusual specificity of human tissue kallikrein in cleaving both an Arg-Ser and a Met-Lys peptide bond in its natural protein substrate, kininogen. A Zn*'-dependent, small-molecule competitive inhibitor of kallikrein ( K , = 3.3 p M ) has been identified and the bound structure modeled to guide drug design.

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Section: Structural Basis For Altered Spec$city Of Rat Kallikreinmentioning

confidence: 99%

Crystal structure of recombinant human tissue kallikrein at 2.0 Å resolution

et al. 1998

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“…This also suggests that these antibodies do not cross-react with L-kininogen, which has the same heavy chain as H-kininogen [38]. For the same reason, the two antibodies TK [17][18][19][20][21][22][23][24][25][26][27].a and TK 20-4.1 that recognize the H-kininogen heavy chain probably cross-react with the L-kininogen. Antibodies specific to each of the three T-kininogen domains were identified by comparing their specificity toward different proteolytic fragments.…”

Section: Lmmunohistochemistry Of T-kininogen In Rat Liver and Kidneymentioning

confidence: 99%

“…The mAb TK [16][17][18][19][20][21][22][23][24][25][26][27][28].5b.2, tested by ELISA, did not crossreact with rat H-kininogen or bovine kininogen (up to 100 pg/ i d ) or with mouse or human plasma. This antibody recognized the 20-kDa peptide; when increasing amounts of the 20-kDa peptide (0.03-3 pg/ml) were incubated with TK 16-28.5b.2, a curve parallel to that of native T-kininogen was obtained (not shown).…”

Section: Sandwich Enzyme Immunoassaymentioning

confidence: 99%

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Immunological characterization of rat kininogens with monoclonal antibodies to T‐kininogen.

Lesage

Bouhnik

Richoux

et al. 1992

European Journal of Biochemistry

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A panel of 16 monoclonal antibodies (mAb) were produced against rat T‐kininogen to characterize this family of proteins. These mAbs bound 125I‐T‐kininogen by radioimmunoassay as well as reacting strongly with immobilized T‐kininogen in an enzyme‐linked immunosorbent assay (ELISA). The reactivity of these antibodies with proteolytic fragments of T‐kininogen demonstrated the recognition of several different epitopes. One antibody was specific for the domain 1 of the heavy chain and/or the light chain, twelve antibodies were specific for domain 2 and three antibodies were specific for domain 3. All monoclonal antibodies recognized the two forms of T‐kininogen encoded by the two different T‐kininogen genes, TI and TII kininogen, except antibody TK 16–3.1 which uniquely reacted with TII kininogen. Two antibodies recognizing domain 2 cross‐reacted with the high‐molecular‐mass kininogen (H‐kininogen), whereas all the other monoclonal antibodies were specific to T‐kininogen and did not recognize the heavy chain of H‐kininogen. None of the antibodies tested altered the thiol protease inhibitory activity of T‐kininogen, its partial proteolysis by rat mast cell chymase or the hydrolysis of H‐kininogen by rat urinary kallikrein. The use of these antibodies in the development of sensitive ELISA to measure T‐kininogen levels in plasma, urine, liver microsomes and hepatocytes is described. Two different forms of T‐kininogen were distinguished by these monoclonal antibodies in Western blotting using rat plasma. The localization of T‐kininogen was defined using these monoclonal antibodies by immunohistochemistry in rat liver hepatocytes and rat kidney.

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“…After measurement of urinary rate, samples were frozen until assay. Bradykinin concentration was measured by RIA as described previously (15).…”

Section: Urinary Excretion Of Bradykininmentioning

confidence: 99%

Differential Regulation of Collecting Duct Na+,K+-ATPase and K+ Excretion by Furosemide and Piretanide

Buffin-Meyer¹,

Younes-Ibrahim²,

Mernissi³

et al. 2004

Journal of the American Society of Nephrology

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Abstract. In response to chronic treatment with furosemide, collecting ducts adapt their function to the initial loss of Na ϩ to prevent further Na ϩ loss and extracellular volume decrease. This adaptation, which includes the overexpression of Na ϩ ,K ϩ -ATPase, is thought to account for most of the kaliuretic effect of furosemide. Because piretanide is reported to be less kaliuretic than equidiuretic doses of furosemide, the authors compared the effects of 1-wk treatment with the two loop diuretics on urinary potassium excretion and on Na ϩ ,K ϩ -ATPase activity in the collecting duct. At equidiuretic and equinatriuretic doses, furosemide increased urinary potassium excretion as well as collecting duct Na ϩ ,K ϩ -ATPase activity, whereas piretanide had no effect on either parameter. These effects of furosemide were curtailed by concomitant administration of the angiotensin-converting enzyme inhibitor enalapril, but they were not altered either by clamping changes in plasma aldosterone or by blocking type I angiotensin receptors. Treatment with the antagonist of bradykinin B2 receptors Hoe140 mimicked the two effects of furosemide. In addition, the effects of Hoe140 and furosemide were not additive. Finally, piretanide increased urinary bradykinin excretion, whereas furosemide did not. These results suggest that induction of collecting duct Na ϩ ,K ϩ -ATPase (a) accounts for the kaliuretic effect of furosemide, (b) is independent of the renin/ angiotensin/aldosterone system, (c) results from increased Na ϩ delivery to the collecting duct and enhanced intracellular Na ϩ concentration, and (d) is prevented in piretanide treated rats by increased bradykinin production that may limit apical Na ϩ entry in collecting duct principal cells.

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Measurement of urinary kallikrein activity species differences in kinin production

Cited by 101 publications

References 28 publications

Crystal structure of recombinant human tissue kallikrein at 2.0 Å resolution

Crystal structure of recombinant human tissue kallikrein at 2.0 Å resolution

Immunological characterization of rat kininogens with monoclonal antibodies to T‐kininogen.

Differential Regulation of Collecting Duct Na+,K+-ATPase and K+ Excretion by Furosemide and Piretanide

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