Immunovisualization of high (HK) and low (LK) molecular weight kininogens on isolated human neutrophils

Cd, Figueroa; Henderson, L. M.; Kaufmann, Jörg; Cadena, RA De La; Colman, Roberta F.; Esterl, W Muller; Bhoola, K. D.

doi:10.1182/blood.v79.3.754.754

Cited by 75 publications

(8 citation statements)

References 28 publications

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“…Only few organs have been identified where a tissue‐specific kininogen synthesis takes place. Kininogen immunoreactivity has been detected in salivary and sweat glands, neutrophils and specific regions of the brain (Chao et al , 1988; Poblete et al , 1991; Richoux et al , 1991; Figueroa et al , 1992). However, the only locations where a kininogen mRNA expression has been shown are liver, kidney and the lung (Iwai et al , 1988; Chao et al , 1993).…”

Section: Introductionmentioning

confidence: 99%

Synthesis of kininogen and degradation of bradykinin by PC12 cells

Dendorfer

Wellhöner

Braun

et al. 1997

British J Pharmacology

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1 In this study, the abilities of PC12 cells to synthesize and degrade kinins were investigated. Kinin formation was assessed as kinin and kininogen content of cells and supernatants in serum-free incubations by use of a bradykinin-speci®c radioimmunoassay. Expression of kininogen mRNA was demonstrated by reverse-transcriptase PCR. Kinin degradation pathways of intact PC12 cells were characterized by identi®cation of the kinin fragments generated from tritiated bradykinin either in the absence or presence of the angiotensin I-converting enzyme inhibitor ramiprilat. 2 Kinin immunoreactivity in the supernatant of PC12 cell cultures accumulated in a time-dependent fashion during incubations in serum-free media. This e ect was solely due to de novo synthesis and release of kininogen (35 pg bradykinin h 71 mg 71 protein) since it could be suppressed by cycloheximide. Continuous synthesis of kininogen was a speci®c property of PC12 cells, as it was not observed in cultured macro-or microvascular endothelial cells. PC12 cells contained only minor amounts of stored kininogen. The rate of kininogen synthesis was not a ected by ramiprilat, bacterial lipopolysaccharide, nerve growth factor or dexamethasone, but was stimulated 1.4 fold when cells were pretreated for 1 day with 1 mM desoxycorticosterone. 3 By use of cDNA probes speci®c for kininogen subtype mRNAs, expression of low-molecular-weight kininogen and T-kininogen in PC12 cells was con®rmed. Expression of high molecular weight kininogen mRNA was also shown, though only at the lowest limit of detection of the assay. 5 Along with previous ®ndings of B 2 -receptor-mediated catecholamine release, these results now con®rm the hypothesis that a cellular kinin system is expressed in PC12 cells. The presence of such a system may re¯ect a role of kinins as local neuromodulatory mediators in the peripheral sympathetic system.

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Section: Introductionmentioning

confidence: 99%

Synthesis of kininogen and degradation of bradykinin by PC12 cells

Dendorfer

Wellhöner

Braun

et al. 1997

British J Pharmacology

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“…Similar clustered patterns of neutrophil‐bound proteins have been reported for HK and LK present in patchy spots on the outer surface of the neutrophil membrane [11]. Both kininogens are multifunctional plasma proteins with a common heavy chain and kinin moiety, respectively, but LK is devoid of the specific light chain sequences that reside in HK [7].…”

Section: Introductionmentioning

confidence: 56%

High‐molecular‐weight kininogen is a binding protein for tissue prokallikrein

Raab

Kemme

2000

FEBS Letters

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Human tissue prokallikrein, a zymogen of the kallikrein-kinin system, circulates in plasma bound to neutrophils. Because plasma kininogens contribute to the assembly of kinin-generating components on blood cells, these proteins were assessed for their ability to complex the kallikrein precursor. Using ligand blot and direct binding assays, biotinylated prokallikrein was found to bind only to high-molecular-weight kininogen and not to the low-molecular-weight form. The interaction was specific, reversible, and saturable yielding an estimated dissociation constant K D = 690 nM and a 1 :1 stoichiometry. Specific kininogen binding of tissue prokallikrein also occurred at physiological plasma protein concentrations. These results provide the first evidence for a novel function of high-molecular-weight kininogen as a binding protein for tissue prokallikrein that could serve to localize the kallikrein precursor on the neutrophil surface.z 2000 Federation of European Biochemical Societies.

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“…It is now clear that neutrophils stimulated by soluble IgG aggregates release their granule enzymes into the SF of RA patients [15,16]. Work from our laboratory [13] has also revealed the presence of TK within the granules of the human neutrophil, and of kininogen substrates on the surface of the same cell [17,18]. It is therefore possible that TK may act to release kinins locally on the neutrophil surface rather than in the general synovial compartment.…”

Section: Discussionmentioning

confidence: 98%

Inhibitor Regulation of Tissue Kallikrein Activity in the Synovial Fluid of Patients With Rheumatoid Arthritis

Rahman

Worthy²,

Elson³

et al. 1994

Rheumatology

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Tissue kallikrein (TK) and alpha 1-antitrypsin (AT)/TK complexes can be detected in SF from patients with RA if components of the fluids which interfere with the detection of TK are removed. alpha 2-Macroglobulin (alpha 2-M) in SF was demonstrated to contain trapped proteases which were still active in amidase assays. Removal of alpha 2-M from RA SF reduced their amidase activity. However, at least some of the remaining activity was due to TK because it was soya bean trypsin inhibitor resistant and trasylol sensitive and was partly removed by affinity chromatography on anti-TK sepharose. Removal of RF from the fluids reduced the values obtained for TK levels by ELISA. Addition of SF to human urinary kallikrein (HUK) considerably reduced the levels of TK detected suggesting the presence of a TK ELISA inhibitor in the fluids. Removal of components of > 300 kDa from SF markedly reduced the TK ELISA inhibitory activity and increased the values for both the TK and alpha 1-AT/TK levels in fluids as measured by ELISA. It is considered this novel inhibitor does not bind to the active site of TK but rather binds to the site reactive with anti-TK antibodies.

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Immunovisualization of high (HK) and low (LK) molecular weight kininogens on isolated human neutrophils

Cited by 75 publications

References 28 publications

Synthesis of kininogen and degradation of bradykinin by PC12 cells

Synthesis of kininogen and degradation of bradykinin by PC12 cells

High‐molecular‐weight kininogen is a binding protein for tissue prokallikrein

Inhibitor Regulation of Tissue Kallikrein Activity in the Synovial Fluid of Patients With Rheumatoid Arthritis

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