Biologically Active Catecholamines Covalently Bound to Glass Beads

Venter, J. Craig; Dixon, Jack E.; Maroko, Peter R.; Kaplan, Nathan O.

doi:10.1073/pnas.69.5.1141

Cited by 71 publications

(21 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…angiotensin (Richardson and Beaulnes, 1971) and catecholamines (Venter et ~., 1972) were shown to retain their activity wh en irreversibly attached to large molecules that prevented them from penetrating the cell membrane.…”

Section: General Introductionmentioning

confidence: 99%

Transformation of Adrenergic Receptors in the Myocardium

1973

View full text Add to dashboard Cite

·ABSTRACTThe present series of experiments provided evidence that the generally accepted distinction between a-and s-adrenergic receptors is not immutable. In frog hearts and rat atria 3H-phenoxybenzamine (3H-POB ) blocked inotropic responses to catecholamines only at temperatures below l7 0 C and potentiated responses ab ove 23 0 C, and considerably more radioactivity was bound to the myocardium at lower temperatures. The converse was true for l4C-propranolol, and the potency of a-and s-adrenergic agonists was shawn to parallel the effectiveness of the blocking agents. Alkylation of a-adrenergic receptors by POB at l4 0 c prevented the appearance of s-adrenergic receptors when the temperature was subsequently raised ta 24 o C.Phentolamine prevented block by 3H-POB and considerably reduced its binding ta the myocardium at low but not at high temperatures. After exposure ta unlabelled POB in the presence of phentolamine at low temperature and thorough washing, exposure to 3H-POB produced a IIpositive label" of the adrenergic receptors, which was localized in a 20,000 9 (ll mitochondrial ll ) and in a IIsoluble protein" fraction. Pretreatment of rats with 6-hydroxydopamine, but not with reserpine, prevented the appearance of oe-adrenergic receptor charac.teristics in left atria at low temperatures; this indicated that adrenergic innervation, but probably not stores of neurotransmitter, is necessary to allow transformation of the receptors. It is suggested that a-and S-adrenergic receptors may be different allosteric conformations of the same molecule.

show abstract

Section: General Introductionmentioning

confidence: 99%

Transformation of Adrenergic Receptors in the Myocardium

1973

View full text Add to dashboard Cite

show abstract

“…Catecholamines covalently bound to glass beads (Venter, Dixon, Maroko & Kaplan, 1972;Venter, Ross, Dixon, Mayer & Kaplan, 1973) or to agarose (Lefkowitz, O'Hara & Warshaw, 1974), exerted positive chronotropic and inotropic effects when applied to cultured heart cells or papillary muscles. However, the possibility exists that these complexes are not entirely stable and that small amounts of catecholamines, sufficient to cause the biological effects, could dissociate from glass beads or agarose (Yong, 1973).…”

Section: Localization Of Beta Adrenergic Receptorsmentioning

confidence: 99%

Localization of beta adrenergic receptors, and effects of noradrenaline and cyclic nucleotides on action potentials, ionic currents and tension in mammalian cardiac muscle

Réuter¹

1974

The Journal of Physiology

407

120

View full text Add to dashboard Cite

“…These proteins are present in target tissues in very low amounts. Much success in the investigation of these proteins and the enzymes of hormone metabolism has been achieved by introduction of affinity chromatography [3][4][5][6][7]. Contrary to animal hormones for plant hormones far less is known on receptor proteins and enzymes of hormone metabolism.…”

Section: Introductionmentioning

confidence: 99%