Action of the Kallikreins on Synthetic Ester Substrates

Webster, Marion E.; Pierce, Jack V.

doi:10.3181/00379727-107-26575

Cited by 97 publications

(42 citation statements)

References 3 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Trasylol is a kallikrein, plasmin and trypsin inhibitor purified from bovine tissues (38). SBTI has been found to inhibit both plasmin and kallikrein, whereas LBTI inhibited plasmin but not plasma kallikrein (39,40). C1 inactivator, as-macroglobulin, Trasylol, and SBTI, but not the lima bean inhibitor, blocked the generation of kinin-like activity when preincubated with plasma-treated collagen before the addition of heated plasma.…”

Section: Discussionmentioning

confidence: 99%

Studies on the Interaction between Collagen and a Plasma Kallikrein-Like Activity EVIDENCE FOR A SURFACE-ACTIVE ENZYME SYSTEM

Harpel¹

1972

J. Clin. Invest.

View full text Add to dashboard Cite

A B S T R A C T This study has demonstrated that collagen particles, after exposure to platelet-poor human plasma and subsequent washing, generate a kinin-like agent when incubated with prekinin substrate. The binding of kinin-generating activity to collagen in the plasma collagen incubation mixture occurs rapidly, whereas the loss of this activity in the incubation mixture occurs relatively slowly. The Hageman factor appeared to be necessary for the surface-bound kiningenerating activity, as this activity was absent in collagen exposed to Hageman factor-deficient plasma. These studies have partially characterized the plasma-derived enzymatic activity bound to collagen. Incubation of collagen with plasma caused a concentration-dependent reduction in the kinin-producing activity which was generated by the addition of ellagic acid, a known activator of plasma kallikrein. The kinin-inducing activity bound to collagen is inhibited by soybean trypsin inhibitor, Trasylol, serum C1 inactivator and the plasma a2-macroglobulin, but not by lima bean trypsin inhibitor. An eluate prepared from plasma-treated collagen, when compared with purified plasma kallikrein, shared a similar inhibitor profile. Selective chemical blockage of the free carboxyl groups on the collagen molecule, or heat denaturation, inactivated the ability of the collagen to generate kinin-like activity after incubation with plasma. Removal of the collagen telopeptides or blockage of the free amino groups failed to affect the collagen-plasma interaction. The binding of This study was presented in part at the 44th Scientific

show abstract

Section: Discussionmentioning

confidence: 99%

Studies on the Interaction between Collagen and a Plasma Kallikrein-Like Activity EVIDENCE FOR A SURFACE-ACTIVE ENZYME SYSTEM

Harpel¹

1972

J. Clin. Invest.

View full text Add to dashboard Cite

show abstract

“…These properties, together with the effects on permeability, suggested that the enzyme might be kallikrein, which will hydrolyse arginine esters (Contzen, Holts & Raudonat, 1959;Habermann, 1959;Werle & Kaufmann-Boetsch, 1960;Webster & Pierce, 1961) and increase permeability by the formations of plasma kinins.…”

Section: Esterase Activity Of Y-globulinsmentioning

confidence: 99%

Presence of Kallikrein in the Γ‐globulin Permeability Factor of Guinea‐pig Serum

Davies¹,

Lowe²

1963

British Journal of Pharmacology and Chemotherapy

View full text Add to dashboard Cite

y-Globulin fractions isolated from guinea-pig serum by chromatography on diethylaminoethyl cellulose exhibited all the properties of kallikrein. From a range of amino acid esters tested, only esters of arginine and lysine were hydrolysed; the esterase and capillary permeability-increasing activities of different samples were correlated. Both esterase and permeability-increasing activities could be increased by the addition of certain albumin-rich fractions or of glass beads previously treated with guinea-pig serum.

show abstract

“…Kallikrein also possesses esterolytic activity for TAMe, similar to PF/dil, and acts upon an a-globulin substrate to release the nonapeptide, bradykinin (40,41). Kallikrein, like PF/dil, is inhibited by soybean trypsin inhibitor and DFP.…”

Section: Discussionmentioning

confidence: 99%

Effect of C′1 esterase on vascular permeability in man: studies in normal and complement-deficient individuals and in patients with hereditary angioneurotic edema

Klemperer¹,

Donaldson²,

Rosen³

1968

J. Clin. Invest.

View full text Add to dashboard Cite

A B S T R A C T When purified human C'1 esterase is injected intradermally in man, increased vascular permeability results. This effect is not blocked by soybean trypsin inhibitor and is not abolished by pretreatment with the antihistamine, pyribenzamine, or by compound 48/80. Thus, the effect is not due to the release of endogenous histamine. The decreased permeability response of individuals with a specific hereditary deficiency of C'2 is evidence for the complement-dependent nature of this reaction. The apparently normal response to intradermal C'1 esterase developed by individuals with an acquired specific deficiency of C'3 suggests that the vasoactive substance may be derived from one of the early reacting complement components. Characteristic attacks of angioedema have been provoked by the intradermal injection of human C'1 esterase in two individuals with hereditary angioneurotic edema. Patients with hereditary angioneurotic edema are unresponsive to intradermal injections of C'1 esterase immediately after attacks.

show abstract

Action of the Kallikreins on Synthetic Ester Substrates

Cited by 97 publications

References 3 publications

Studies on the Interaction between Collagen and a Plasma Kallikrein-Like Activity EVIDENCE FOR A SURFACE-ACTIVE ENZYME SYSTEM

Studies on the Interaction between Collagen and a Plasma Kallikrein-Like Activity EVIDENCE FOR A SURFACE-ACTIVE ENZYME SYSTEM

Presence of Kallikrein in the Γ‐globulin Permeability Factor of Guinea‐pig Serum

Effect of C′1 esterase on vascular permeability in man: studies in normal and complement-deficient individuals and in patients with hereditary angioneurotic edema

Contact Info

Product

Resources

About