Assay Methods in the Kinin System

Trautschold, I.

doi:10.1007/978-3-642-46222-1_5

Cited by 23 publications

(9 citation statements)

References 88 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The purpose of these studies was to attempt to purify and characterize the basophil TAMe esterase and kinin-generating activities, and determine whether the two activities were subserved by the same protease. It is reasonable to assume that the kiningenerating protease and the basophil arginine esterase activity might be subserved by the same protease, since, like all known kallikreins (7,8), the basophil enzyme activity is an arginine esterase, and, like many kallikreins, it is inhibited by plasma, DFP, and Trasylol (Figs. 7 and 8, Table III).…”

Section: Discussionmentioning

confidence: 99%

Anaphylactic release of a basophil kallikrein-like activity. I. Purification and characterization.

Newball¹,

Berninger²,

Talamo³

et al. 1979

J. Clin. Invest.

View full text Add to dashboard Cite

A B S T R A C T These studies describe the IgE-mediated release of a basophil kallikrein-like enzyme that is an arginine esterase and is inhibited by plasma, diisopropylphosphofluoridate, and Trasylol. The substrate specificity for the synthetic amino acid ester substrates p-toluenesulfonyl-L-arginine methyl ester, benzoyl-arginine methyl ester, and acetyl-tyrosine methyl ester is similar for the basophil enzyme and plasma kallikrein. The interaction of arginine esteraseactive fractions from ion-exchange (DEAE-Sephacel) and gel filtration (Sepharose 6B) chromatography, with human plasma kininogen, generates immunoreactive kinin. The basophil arginine esterase and kiningenerating activities co-chromatograph on Sepharose 6B and the quantity of kinin generated is, in general, proportional to the arginine esterase activity of the column fractions, suggesting that these two activities are subserved by the same protease. The ability of this protease to generate kinin equally well from heat-and acid-treated plasma, as from fresh human plasma, suggests that this protease has kallikrein-like activity. These data suggest that kallikrein-like activity can be generated from human basophils as a direct result of a primary IgE-mediated immune reaction, thus providing a potential link between reactions of immediate hypersensitivity and the plasma and(or) tissue kiningenerating systems.

show abstract

Section: Discussionmentioning

confidence: 99%

Anaphylactic release of a basophil kallikrein-like activity. I. Purification and characterization.

Newball¹,

Berninger²,

Talamo³

et al. 1979

J. Clin. Invest.

View full text Add to dashboard Cite

show abstract

“…Samples to be assessed for angiotensin II-generating protease activity were incubated in duplicate with partially purified or purified angiotensinogen (3) for 30 min at 370C. The reactions were stopped by immersion of the tubes in ice, and each reaction mixture was bioassayed directly for angiotensin II contractile activity on isolated, atropinized, guinea pig terminal ileum suspended in Tyrode's solution and standardized with synthetic angiotensin II (10). The results are expressed as the mean contractile activity in angiotensin II equivalents.…”

Section: Methodsmentioning

confidence: 99%

Identification of a human neutrophil angiotension II-generating protease as cathepsin G.

Tonnesen¹,

Klempner²,

Austen³

et al. 1982

J. Clin. Invest.

View full text Add to dashboard Cite

A B S T R A C T A human neutrophil protease, initially termed neutral peptide-generating protease, has been shown to cleave angiotensin II directly from angiotensinogen and has been identified as leukocyte cathepsin G. When purified neutrophils were disrupted by nitrogen cavitation and fractionated by differential centrifugation, 44 and 24% of the angiotensin II-generating activity was in the lysosomal and undisrupted cell fractions, respectively. Cytochalasin B-treated human neutrophils stimulated with N-formyl-L-methionyl-L-leucyl-L-phenylalanine released #-glucuronidase, lysozyme, and angiotensin II-generating protease in a dose-dependent fashion, consistent with localization of this protease to the neutrophil granule. Individually purified angiotensin II-generating protease and cathepsin G had similar proteolytic and esterolytic activity for angiotensinogen and N-benzoyl-L-tyrosine ethyl ester on a weight basis, exhibited identical mobilities by SDS-gradient polyacrylamide gel electrophoresis and pH 4.3 disc-gel electrophoresis, and gave precipitin lines of antigenic identity on Ouchterlony analysis with goat antibody to the angiotensin II-generating protease. Thus, the angiotensin II-generating protease of human neutrophils has been identified as cathepsin G on the basis of subcellular localization, substrate specificity, physicochemical characteristics, and antigenic identity.

show abstract

“…An aqueous extract of the freeze-dried gland was centrifuged and the supernatant solution again freeze-dried. The kallikrein concentrations of this powder were measured chemically in esterase units using benzoyl-Larginine ethyl ester (BAEe) as substrate (Trautschold, 1970).…”

Section: Methodsmentioning

confidence: 99%

Studies on kallikrein in the duct systems of the salivary glands of the cat

Shnitka

Maranda

Rodrigues

et al. 1978

The Journal of Physiology

View full text Add to dashboard Cite

SUMMARYBy correlating immunofluorescence light microscopy with electron microscope studies and with kallikrein concentrations under various conditions, we have made the following observations and conclusions about kallikrein in the submandibular and other salivary glands.1. In the submandibular gland, specific immunofluorescence to kallikrein was observed in the luminal region of the striated ducts particularly, but also in the outer epithelial cells of the stratified epithelial collecting ducts. Sympathetic nerve stimulation resulted in a reduction in intensity of specific fluorescence and in its increased localization towards the lumen. The nearly complete elimination of kallikrein from the gland by duct obstruction for four days resulted in complete disappearance of specific fluorescence in the gland. Prolonged parasympathetic nerve stimulation at frequencies which did not reduce the kallikrein concentration of the gland failed to alter the specific immunofluorescence despite copious secretion of saliva. Our results failed to reveal evidence of secretion of kallikrein either into or towards the interstitium of the gland.The luminal layer of stratified epithelial cells in the collecting ducts contained small secretary granules closely resembling those in the striated ducts. Our results are not conclusive, but do suggest that kallikrein is located in these granules whence it is secreted into the lumen of the duct.2. The parotid gland was found to contain much lower concentrations of kallikrein than the submandibular gland. This finding was associated with the presence of far fewer striated ducts in the parotid gland. Otherwise, specific fluorescence and the response to sympathetic nerve stimulation was like that of the submandibular gland.Small secretary granules in the striated and collecting ducts resembled those of the submandibular gland.3. The sublingual gland, like the parotid, had a low concentration of kallikrein and very few striated ducts. These ducts were unevenly distributed and were concentrated in only a few lobules of the gland. Specific immunofluorescence was seen only in sections containing striated ducts.4. The possible physiological role of kallikrein in the salivary glands is discussed.

show abstract

Assay Methods in the Kinin System

Cited by 23 publications

References 88 publications

Anaphylactic release of a basophil kallikrein-like activity. I. Purification and characterization.

Anaphylactic release of a basophil kallikrein-like activity. I. Purification and characterization.

Identification of a human neutrophil angiotension II-generating protease as cathepsin G.

Studies on kallikrein in the duct systems of the salivary glands of the cat

Contact Info

Product

Resources

About