The effect of catecholamines and prostaglandins upon human and rat erythrocytes

Rasmussen, Howard; Lake, William C.; Allen, James E.

doi:10.1016/0304-4165(75)90285-8

Cited by 120 publications

(46 citation statements)

References 16 publications

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“…It possesses binding sites for insulin (Herzberg et al, 1980), growth hormone (Rubin et al, 1973), acetylcholine (Huestis & McConnell, 1974), f,-adrenergic agents (Rasmussen et al, 1975;Nelson et al, 1979) and prostaglandins (Rasmussen et al, 1975;Kury & McConnell, 1975). In many of these cases, binding at the level of only a few molecules per cell has been reported to result in macroscopically detectable (if not necessarily interpretable) changes, reflected in perturbations of the signals from fluorescent or spin labels in the membrane, as well as in metabolic changes, in particular of phosphorylation levels of intracellular proteins (see below).…”

Section: Receptor Eventsmentioning

confidence: 99%

The red cell membrane and its cytoskeleton

Gratzer¹

1981

Biochemical Journal

127

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Section: Receptor Eventsmentioning

confidence: 99%

The red cell membrane and its cytoskeleton

Gratzer¹

1981

Biochemical Journal

127

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“…These studies suggest that a functional , 8-adrenergic receptor exists in the mature human erythrocyte. INTRODUCTION Recently, with improved methodology, hormonesensitive adenylate cyclase has been detected in erythrocytes of several mammalian species, i.e., rat (1)(2)(3), mouse (1), and rabbit (4). To our knowledge only two groups have reported the presence of catecholamineresponsive adenylate cyclase in human erythrocytes (5,6).…”

mentioning

confidence: 99%

Catecholamine regulation of human erythrocyte membrane protein kinase.

Takeuchi¹,

Sonenberg²

1979

J. Clin. Invest.

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A B S T R A C T The effect of catecholamines on membrane-associated protein kinase in the mature human erythrocyte was investigated. Protein kinase activity was assayed after isolation of membranes from intact erythrocytes incubated with and without catecholamines. Activation of the enzyme is expressed as the ratio of the extent of phosphorylation of exogenous protein substrate in the absence to that in the presence of 2.5 ,M cyclic AMP (cAMP). The potent ,8-adrenergic agonist, (-)isoproterenol (2 ,uM), (-)epinephrine (10 ,uM) and (-)norepinephrine (10 uM) stimulated the cAMP-dependent protein kinase in membranes, 38±7%, 31±6%, and 30±6%, respectively. Maximal stimulation of membrane protein kinase by 10 ,uM (-)epinephrine was obtained _30 min after initiation of the incubation of erythrocytes with the hormone. The concentrations of (-)catecholamines that gave half-maximal stimulation of the membrane protein kinase were 0.17 ,M for isoproterenol, 0.35 ,M for epinephrine, and 0.63 ,uM for norepinephrine. The membrane protein kinase response to 6-adrenergic agonists was found to be stereospecific. The stimulation of membrane protein kinase by 10 ,uM (-)epinephrine was inhibited by the ,8-adrenergic antagonist, (-)propranolol with EC50 = 0.60 ,uM, and the inhibition of agonist stimulation of the cAMP-dependent protein kinase by propranolol was stereospecific. These studies suggest that a functional ,8-adrenergic receptor exists in the mature human erythrocyte.

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“…Rasmussen et al (1975) reported that the same low doses of adrenaline and isoproterenol induce a decrease of erythrocyte deformability.…”

Section: Adrenaline Noradrenaline and Dopamentioning

confidence: 98%