Role of peptidases in bradykinin-induced increase in vascular permeability in vivo.

Yong, Ting Ting; Gao, Xiao Pei; Koizumi, Shinichiro; Conlon, J. Michael; Rennard, Stephen I.; Mayhan, William G.; Rubinstein, Israel

doi:10.1161/01.res.70.5.952

Cited by 50 publications

(48 citation statements)

References 20 publications

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“…The number of leaky sites was determined by counting three random microscopic fields at predetermined time intervals during each intervention. The total number of leaky sites was then averaged and expressed as the number of leaky sites per 0.11 cm 2 of cheek pouch, which corresponds to the area of one microscopic field (9,10,12,30).…”

Section: General Methodsmentioning

confidence: 99%

“…Then, two concentrations of bradykinin (0.5 and 1.0 µM) were suffused for 5 min in a nonsystematic fashion. At least 45 min elapsed between subsequent suffusions of bradykinin (8,11,13,17,30). After suffusion of bradykinin was stopped and the number of leaky sites returned to baseline, purified ACE (0.05 unit) was suffused for 30 min before and during a second suffusion of bradykinin (0.5 and 1.0 µM).…”

Section: Experimental Protocolsmentioning

confidence: 99%

“…Adenosine, like bradykinin, increases macromolecular efflux from postcapillary venules in the cheek pouch by specific receptor-mediated mechanism(s) (10,13,17,30). After buffer was suffused for 30 min (equilibration period), FITC-dextran was administered intravenously and the number of leaky sites and clearance of FITC-dextran were determined.…”

Section: Experimental Protocolsmentioning

confidence: 99%

“…They also showed that the extract elicited a significant decrease in cheek pouch activity of angiotensin I-converting enzyme (ACE; EC 3.4.15.1), a membrane-bound metalloenzyme widely distributed in the microcirculation that regulates the edemagenic effects of bradykinin in the cheek pouch by cleaving and inactivating the peptide (3,6,23,30). However, the role of tissue ACE in modulating smokeless tobacco-induced increase in macromolecular efflux from the oral mucosa is uncertain.…”

mentioning

confidence: 99%

“…We reasoned that if smokeless tobacco elicits bradykinin production in the oral mucosa while decreasing tissue ACE activity, and if ACE regulates the edemagenic effects of bradykinin in the tissue by cleaving and inactivating the peptide, then pharmacological interventions that would increase ACE activity in the oral mucosa should mitigate the increase in macromolecular efflux elicited by smokeless tobacco (12,30). The purpose of this study was to begin to address this issue by determining whether suffusion of purified ACE attenuates smokeless tobacco extract-induced increase in macromolecular efflux from the in situ hamster cheek pouch.…”

mentioning

confidence: 99%

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Purified ACE attenuates smokeless tobacco-induced increase in macromolecular efflux from the oral mucosa

Gao

Suzuki

Olopade

et al. 1997

Journal of Applied Physiology

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Purified ACE attenuates smokeless tobacco-induced increase in macromolecular efflux from the oral mucosa. J. Appl. Physiol. 83(1): 74-81, 1997.-The purpose of this study was to determine whether purified angiotensin I-converting enzyme (ACE) attenuates smokeless tobacco extract (STE)-induced increase in macromolecular efflux from the in situ oral mucosa. By using intravital microscopy, we found that suffusion of an aqueous extract of smokeless tobacco elicited significant concentration-dependent leaky site formation and increase in clearance of fluorescein isothiocyanate-labeled dextran (mol mass, 70 kDa) from the hamster cheek pouch (P , 0.05). Suffusion of purified rabbit lung ACE significantly attenuated these responses in a concentration-dependent fashion (P , 0.05). These effects were specific because purified ACE also significantly attenuated the increase in macromolecular efflux elicited by bradykinin, which is produced in the cheek pouch during suffusion of STE, but did not attenuate the increase elicted by adenosine. Moreover, suffusion of heat-inactivated purified ACE and purified superoxide dismutase had no significant effects on STE-and bradykinin-induced responses. Collectively, these data suggest that exogenous ACE attenuates STE-induced increase in macromolecular efflux from the in situ oral mucosa, in part, by promoting local bradykinin catabolism.

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Section: General Methodsmentioning

confidence: 99%

Section: Experimental Protocolsmentioning

confidence: 99%

Section: Experimental Protocolsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Purified ACE attenuates smokeless tobacco-induced increase in macromolecular efflux from the oral mucosa

Gao

Suzuki

Olopade

et al. 1997

Journal of Applied Physiology

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Filamin translocation is an early endothelial cell inflammatory response to bradykinin: Regulation by calcium, protein kinases, and protein phosphatases

et al. 1996

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Endothelial cell (EC) cytoskeletal proteins are one of the earliest primary targets of second messenger cascades generated in response to inflammatory agonists. Actin binding proteins, by modulating actin gelation-solation state and membrane-cytoskeleton interactions, in part regulate cell motility and cell-cell apposition. This in turn can also modulate interendothelial junctional diameter and permeability. Nonmuscle filamin (ABP-280), a dimeric actin-crosslinking protein, promotes orthogonal branching of F-actin and links microfilaments to membrane glycoproteins. In the present study, immunoblot analysis demonstrates that filamin protein levels are low in sparse EC cultures, increase once cell-cell contact is initiated and then decrease slightly at post-confluency. Both bradykinin and ionomycin cause filamin redistribution from the peripheral cell border to the cytosol of confluent EC. Forskolin, an activator of adenylate cyclase, blocks filamin translocation. Bradykinin activation of EC is not accompanied by significant proteolytic cleavage of filamin. Instead, intact filamin is recycled back to the membrane within 5-10 min of bradykinin stimulation. Inhibitors of calcium/calmodulin dependent protein kinase (KT-5926 and KN-62) attenuate bradykinin-induced filamin translocation. H-89, an inhibitor of cAMP-dependent protein kinase, causes translocation of filamin in unstimulated cells. Calyculin A, an inhibitor of protein phosphatases, also causes translocation of filamin in the absence of an inflammatory agent. ML-7, an inhibitor of myosin light chain kinase and phorbol myristate acetate, an activator of protein kinase C, do not cause filamin movement into the cytosol, indicating that these pathways do not modulate the translocation. Pharmacological data suggest that filamin translocation is initiated by the calcium/calmodulin-dependent protein kinase whereas the cAMP-dependent protein kinase pathway prevents translocation. Inflammatory agents therefore may increase vascular junctional permeability by increasing cytoplasmic calcium, which disassembles the microfilament dense peripheral band by releasing filamin from F-actin.

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B2 bradykinin receptor immunoreactivity in rat brain

et al. 2000

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Bradykinin has long been known to exist in the central nervous system and has been hypothesized to mediate specific functions. Despite an increasing understanding of the functions of bradykinin, little is known about the cell types expressing the bradykinin receptor within the brain. The present investigation employed a monoclonal antibody directed against the 15-amino-acid portion of the C-terminal of the human bradykinin B2 receptor to establish the cellular distribution of bradykinin B2 receptor immunoreactivity in the rat brain. Bradykinin B2 receptor immunoreactivity was ubiquitously and selectively observed in neurons, including those within the olfactory bulb, cerebral cortex, hippocampus, basal forebrain, basal ganglia, thalamus, hypothalamus, cerebellum, and brainstem nuclei. Bradykinin B2 receptor immunoreactivity was also present in the circumventricular organs including choroid plexus, subfornical organ, median eminence, and area postrema. Double-labeling experiments colocalizing the bradykinin B2 receptor with the neuronal marker NeuN or the astrocytic marker glial fibrillary acidic protein revealed that virtually 100% of the bradykinin B2 receptor-immunoreactive positive cells were neurons. The widespread distribution of bradykinin B2 receptor immunoreactivity in neuronal compartments suggests a greater than previously appreciated role for this peptide in neuronal function.

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Role of peptidases in bradykinin-induced increase in vascular permeability in vivo.

Cited by 50 publications

References 20 publications

Purified ACE attenuates smokeless tobacco-induced increase in macromolecular efflux from the oral mucosa

Purified ACE attenuates smokeless tobacco-induced increase in macromolecular efflux from the oral mucosa

Filamin translocation is an early endothelial cell inflammatory response to bradykinin: Regulation by calcium, protein kinases, and protein phosphatases

B2 bradykinin receptor immunoreactivity in rat brain

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