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Characterization of an altered membrane form of the beta-adrenergic receptor produced during agonist-induced desensitization.
Open accessAbstract
Incubation of 1321N1 human astrocytoma cells with 1 microM isoproterenol rapidly results in the conversion of a portion of the beta-adrenergic receptors to a membrane form that can be separated from markers for the plasma membrane by sucrose density gradient or differential centrifugation. This "light peak" form of the receptor reaches a maximal level within 10 min of incubation of cells with catecholamine. Two types of experiments suggest that the early phase of catecholamine-induced desensitization of the beta-adrenergic receptor-linked adenylate cyclase can be separated into at least two reactions. First, the agonist-induced loss of catecholamine-stimulated adenylate cyclase activity precedes the appearance of beta-adrenergic receptors in the light peak fraction by 1-2 min. Second, pretreatment of cells with concanavalin A prior to induction of desensitization blocks the formation of the light peak form of beta-adrenergic receptors without blocking the "uncoupling" reaction as measured by catecholamine-stimulated adenylate cyclase activity. Specificity for the reaction that converts beta-adrenergic receptors to the light peak form is indicated by the lack of a catecholamine-induced alteration in the sucrose density gradient distribution of muscarinic cholinergic receptors, adenylate cyclase or the guanine nucleotide-binding proteins, Ns and Ni. The light peak of beta-adrenergic receptors migrates at a density similar to that of at least a portion of the activity of galactosyltransferase, a marker for Golgi. Enzyme marker activities for lysosomes and endoplasmic reticulum are not associated with this population of beta-adrenergic receptors. Taken together, these and other data suggest that incubation of 1321N1 cells with isoproterenol results in a rapid uncoupling of beta-adrenergic receptors from adenylate cyclase which is followed by a change in the membrane form of the receptor. This latter step most likely represents internalization of receptors into a vesicular form which may then serve as the precursor state from which receptors are eventually lost from the cell.
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Cited by
Sibley, D. R., & Lefkowitz, R. J. (1985) · Nature · doi:10.1038/317124a0 · Cited by 734
Bouvier, M., Hausdorff, W. P., Blasi, A. D., O'Dowd, B. F., Kobilka, B. K., Caron, M. G., & Lefkowitz, R. J. (1988) · Nature · doi:10.1038/333370a0 · Cited by 438
Internalization and recycling of activated thrombin receptors
Hoxie, J. A., Ahuja, M., Belmonte, E., Pizarro, S., Parton, R., & Brass, L. F. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)86921-6 · Cited by 272
Braune, S., Albus, M., Fröhler, M., Höhn, T., & Scheibe, G. (1994) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/bf02193524 · Cited by 33
Metadata
- Authors
- Waldo, G. L., Northup, J. K., Perkins, J. P., & Harden, T. K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1983-11
- Volume
- 258
- Issue
- 22
- Pages
- 13900-13908
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1493514243
- Cited by
- 204
- References
- 0
- FWCI
- 6.75
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Waldo, G. L., Northup, J. K., Perkins, J. P., & Harden, T. K. (1983). Characterization of an altered membrane form of the beta-adrenergic receptor produced during agonist-induced desensitization. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)44003-8
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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