Phosphorylation of Cell Surface Receptors: A Mechanism for Regulating Signal Transduction Pathways

Sibley, David R.; Benovic, Jeffrey L.; Caron, Marc G.; Lefkowitz, Robert J.

doi:10.1210/edrv-9-1-38

Cited by 106 publications

(55 citation statements)

References 199 publications

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“…This may indicate the involvement of some other factors in the diminution of TK activity at this T 3 concentration. In accordance, several reports demonstrated that the EGFR activation also resulted in the phosphorylation of EGFR on threonine residues, leading to receptor internalization or TK activity inhibition (Sibley et al 1988). This biphasic T 3 effect on DNA synthesis may also be a consequence of the T 3 deiodination (Mori et al 1996) or the phosphorylation of multiple proteins including the T 3 R, an event reported to play a role in regulating the action of T 3 R as well as other nuclear hormone receptors (Sugawara et al 1994, Solomon et al 1999.…”

Section: Discussionsupporting

confidence: 85%

“…Evidence for a close functional relationship between TH and EGF in the regulation of cellular growth has been obtained in various cellular types (Hinkle & Kinsella 1986, Walker 1986, Kaji & Hinkle 1987, Matsuo et al 1993. Most of the cellular proliferative responses to growth factors are mediated by TK activity (Sibley et al 1988, Dumont et al 1992. The blockage of the T 3 -induced DNA synthesis by TK inhibitors indicated a participation of TK activity in the T 3 action.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Tri-iodothyronine induces proliferation in cultured bovine thyroid cells: evidence for the involvement of epidermal growth factor-associated tyrosine kinase activity

Fulvio

Coleoni²,

Pellizas³

et al. 2000

Journal of Endocrinology

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The effects of the tri-iodothyronine (T 3 ) secreted by thyroid cells on the growth of the thyrocyte are poorly known. In this study we analyzed the effects of T 3 on the proliferation of bovine thyroid follicles in primary culture previously depleted of endogenous T 3 . Cellular deoxiribonucleic acid (DNA) synthesis, determined by [ 3 H]thymidine incorporation, was stimulated by T 3 (0·1-5·0 nM) for 24 h in a concentration-dependent fashion with a maximal effect at 1·0 nM T 3 (P<0·01). This T 3 action was time-dependent when assayed from 12 to 72 h. The induction of mitogenic activity was corroborated by the increase in proliferating cell nuclear antigen (PCNA) measured by Western blot analysis. PCNA increased after treatment with T 3 (0·1-5·0 nM) in a concentrationdependent manner. Since T 3 modifies the activity of growth factors whose actions are mainly mediated by tyrosine kinase (TK) activation in diverse cellular types, we assayed the effects of genistein, a general TK inhibitor, and tyrphostin A25, a specific epidermal growth factor (EGF)-receptor (EGFR)-dependent TK activity inhibitor, on the proliferative effects of T 3 . The T 3 -induced [ 3 H]thymidine incorporation was inhibited by both agents in a concentration-dependent manner. A significant increase in the total TK activity measured in cellular protein extracts was induced by 0·5 and 1·0 nM T 3 (P<0·001). Tyrosine phosphorylation of the EGFR was also stimulated by T 3 (P<0·001) with no change in the EGFR expression as determined by Western blot analysis. Both, the T 3 -stimulated [3 H]thymidine incorporation and the TK activity were inhibited by a anti-mouse EGF antibody. These results lead us to propose that T 3 could operate as a proliferative agent in bovine thyroid cells through a mechanism involving an autocrine/paracrine EGF/EGFR-dependent regulation.

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Section: Discussionsupporting

confidence: 85%

Section: Discussionmentioning

confidence: 99%

Tri-iodothyronine induces proliferation in cultured bovine thyroid cells: evidence for the involvement of epidermal growth factor-associated tyrosine kinase activity

Fulvio

Coleoni²,

Pellizas³

et al. 2000

Journal of Endocrinology

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“…This desensitization of the somatostatin response is manifested by a 20-to 100-fold rightward shift in the somatostatin concentration-response curve rather than by abolition of the response; this form of desensitization also requires protein synthesis (Reisine & Takahashi, 1984 (Lefkowitz & Carron, 1987;Sibley et al 1988). Obviously, heterologous desensitization is of little practical use as a tool to elucidate a transmitter function for a neurally contained substance.…”

Section: The Somatostatin Responsementioning

confidence: 99%

“…3) but the somatostatin response is occluded during application of noradrenaline because they open common channels (Surprenant & North, 1988). Thus, we were able to compare the time course of recovery of sensitivity to somatostatin after somatostatin desensitization (@, We examined the effects of a number of substances which are known to alter properties of desensitization in other receptor systems, such as the ,6-adrenoceptor (Lefkowitz & Caron, 1987;Sibley, Benovic, Caron & Lefkowitz, 1988). We measured three parameters: (1) the time course of tachyphylaxis to somatostatin, (2) the concentration of somatostatin producing tachyphylaxis and (3) the degree of tachyphylaxis produced by 2 /M somatostatin (as a percentage of peak current remaining at 3 min in somatostatin).…”

Section: Introductionmentioning

confidence: 99%

Somatostatin‐mediated inhibitory postsynaptic potential in sympathetically denervated guinea‐pig submucosal neurones.

Shen

Surprenant

1993

The Journal of Physiology

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SUMMARY1. Intracellular recordings were made from submucosal neurones in guinea-pig ileum. In some animals, the extrinsic (sympathetic) nerves to the submucosal plexus were severed 5-7 days previously. 4. Recovery from desensitization was rapid and followed the time course of agonist wash-out. Forskolin, phorbol esters, dithiothreitol, hydrogen peroxide, concanavalin A, or reducing temperature from 35 to 29°C did not alter the time course, degree of, or recovery from desensitization.5. The somatostatin-induced desensitization was of the homologous type; no cross-desensitization to opiate or a2-adrenoceptor agonists (which activate the same potassium conductance) occurred.6. Somatostatin desensitization did not alter the adrenergic IPSP seen in sympathetically innervated preparations but abolished the non-adrenergic IPSP recorded from normal preparations and from preparations in which the extrinsic sympathetic nerve supply had been surgically removed.7. The selective blockade of the non-adrenergic IPSP by the homologous-type somatostatin desensitization characterized in the present study provides strong support for the hypothesis that somatostatin is the neurotransmitter underlying the non-adrenergic IPSP in both normal and extrinsically denervated submucosal neurones.

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“…The mechanism of desensitization is in general thought to involve phosphorylation of receptors, which causes uncoupling of receptors from the G proteins and results in a decrease in their affinity to agonists (12). Muscarinic receptors are phosphorylated by protein kinase A, protein kinase C and muscarinic-receptor-specific kinase (13).…”

mentioning

confidence: 99%

Changes in 3H-Quinuclidinyl Benzilate Binding and Protein Synthesis in the Striatum Following Chronic Administrations of Muscarinic Agonist

Honda

Takáno

Kamiya

1995

Japanese Journal of Pharmacology

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Injection of the muscarinic agonist oxotremorine into rat striatum for seven consecutive days resulted in a 44 076 in 3H-quinuclidinyl benzilate (3H-QNB) binding, and it caused decreases in binding affinity to agonists. Furthermore, it eliminated the shift from the high affinity site to the low affinity site that occurs in the presence of 5 guanylyl imidodiphosphate (Gpp (NH)p). In addition, oxotremorine caused a 1.5-fold increase in the incorporation of 3H-leucine into the striatum, suggesting that it increased the syntheses of proteins other than the muscarinic receptor protein. The present results show that chronic treatment of the striatum with oxotremorine causes alterations in not only the quantity, but also the sensitivity of muscarinic receptors to guanine nucleotide.

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Phosphorylation of Cell Surface Receptors: A Mechanism for Regulating Signal Transduction Pathways

Cited by 106 publications

References 199 publications

Tri-iodothyronine induces proliferation in cultured bovine thyroid cells: evidence for the involvement of epidermal growth factor-associated tyrosine kinase activity

Tri-iodothyronine induces proliferation in cultured bovine thyroid cells: evidence for the involvement of epidermal growth factor-associated tyrosine kinase activity

Somatostatin‐mediated inhibitory postsynaptic potential in sympathetically denervated guinea‐pig submucosal neurones.

Changes in 3H-Quinuclidinyl Benzilate Binding and Protein Synthesis in the Striatum Following Chronic Administrations of Muscarinic Agonist

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