Catecholamines are mitogenic in 3T3 and bovine aortic endothelial cells.

Sherline, Peter; Mascardo, Renato N.

doi:10.1172/jci111445

Cited by 41 publications

(18 citation statements)

References 16 publications

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“…While the coupling between Ca2" mobilization and mitogenesis in response to EGF remains enigmatic (6,8,10,16,74), numerous studies have implicated angiotensin II and other Ca2+/PKC-linked hormones as regulators of cell proliferation under defined conditions. Angiotensin II, vasopressin, and ac-adrenergic agonists variously stimulate DNA synthesis in adrenal cortex (27,55), mouse 3T3 fibroblasts (57,59,61), vascular smooth muscle cells (7), and hepatocytes (15). Accordingly, peptide hormones and catecholamines have been implicated as regulators of development (37,79), angiogenesis (24), and liver regeneration (15).…”

Section: Discussionmentioning

confidence: 99%

Angiotensin II stimulates protein-tyrosine phosphorylation in a calcium-dependent manner.

Huckle¹,

Prokop²,

Dy³

et al. 1990

Mol. Cell. Biol.

121

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Cellular responses to epidermal growth factor (EGF) are dependent on the tyrosine-specific protein kinase activity of the cell-surface EGF receptor. Previous studies using WB rat liver epithelial cells have detected at least 10 proteins whose phosphotyrosine (P-Tyr) content is increased by EGF. In this study, we have examined alternate modes of activating tyrosine phosphorylation. Treatment of WB cells with hormones linked to Ca2+ mobilization and protein kinase C (PKC) activation, including angiotensin II, [Arg8]vasopressin, or epinephrine, stimulated rapid (<15-s) and transient increases in the P-Tyr content of several proteins (p120/125, p75/78, and p66). These proteins, detected by anti-P-Tyr immunoblotting, were similar in molecular weight to a subset of EGF-sensitive P-Tyr-containing proteins (P-Tyr-proteins all P-Tyr-proteins in response to angiotensin II, thapsigargin, or ionophores, as well as two EGF-stimulated P-Tyr-proteins. The majority of EGF-stimulated P-Tyr-proteins were not affected by BAPTA. These studies indicate that angiotensin II can alter protein-tyrosine phosphorylation in a manner that is secondary to, and apparently dependent on, Ca2+ mobilization. Thus, ligands such as EGF and angiotensin II, which act through distinct types of receptors, may activate secondary pathways involving tyrosine phosphorylation. These results also raise the possibility that certain growth-promoting effects of Ca2+-mobilizing agents such as angiotensin H may be mediated via tyrosine phosphorylation.Reversible phosphorylation of proteins is a major mechanism by which metabolic processes are regulated. Phosphorylation on serine and threonine residues, which together account for >99% of total cellular protein phosphate, are recognized as key elements in the regulation of such diverse pathways as glycogen metabolism, protein biosynthesis, and cell surface receptor signaling (19). Phosphorylation on tyrosine residues, which accounts for <0.5% of proteinbound phosphate (12), has been linked broadly with the control of cell proliferation. Receptors for several growth factors, including epidermal growth factor (EGF) and platelet-derived growth factor, contain ligand-activated, tyrosinespecific protein kinase domains essential for biological activity (76, 78). Similarly, the protein products of several oncogenes (e.g., src and ab) exhibit tyrosine kinase activities essential for oncogenic transformation (36,41).The identities of relevant substrates for tyrosine kinases remain largely obscure because of the technical challenge of monitoring transient tyrosine phosphorylation events against high backgrounds of serine/threonine phosphorylation and because of the complex and temporally protracted nature of mitogenesis. Nevertheless, several potential substrates for tyrosine kinases in intact cells have been identified, using combinations of 32p labeling, electrophoresis, phosphoami-* Corresponding author. no acid analysis, and immunoprecipitation and immunoblotting with antiphosphotyrosine (anti-P-Tyr) antibodies. One gro...

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Section: Discussionmentioning

confidence: 99%

Angiotensin II stimulates protein-tyrosine phosphorylation in a calcium-dependent manner.

Huckle¹,

Prokop²,

Dy³

et al. 1990

Mol. Cell. Biol.

121

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“…Of potential relevance is the finding that stimulation of the a,- (40), and mouse 3T3 and bovine endothelial cells (41); and it induces expression of the c-myc proto-oncogene in cultured cardiac myocytes (42). It will be interesting to see whether these diverse effects on contractility, cell growth, and gene expression are mediated through common or distinct intracellular pathways.…”

Section: Discussionmentioning

confidence: 99%

Induction of the skeletal alpha-actin gene in alpha 1-adrenoceptor-mediated hypertrophy of rat cardiac myocytes.

1987

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Myocardial hypertrophy in vivo is associated with reexpression of contractile protein isogenes characteristic of fetal and neonatal development. The molecular signals for hypertrophy and isogene switching are unknown. We studied a (sarcomeric)-actin messenger RNA (mRNA) expression in cultured cardiac myocytes from the neonatal rat. In the cultured cells, as in the adult heart in vivo, expression of cardiac a-actin (cACT) predominated over that of skeletal a-actin (sACr) mRNA, the fetal/neonatal isoform. a1-Adrenergic receptor stimulation induced hypertrophy of these cells, increasing total RNA and cytoskeletal actin mRNA by 1.8-fold over control, and total a-actin mRNA by 43 fold. This disproportionate increase in total a-actin mRNA was produced by a preferential induction of sACT mRNA, which increased by 10.64old over control versus only 2.6-fold for cACT mRNA. The a1-adrenoceptor is the first identified molecular mediator of early developmental isogene reexpression in cardiac myocyte hypertrophy.

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“…However, there are at least two possibilities. One is that TXA 2 potentiates various humoral substances that participate in the regulatory mechanism for cell proliferation, such as catecholamines, 4 steroids, 3 platelet-derived growth factor, 6 or insulin. 7 The other possibility is a direct action of TXA 2 on VSMC growth.…”

Section: Discussionmentioning

confidence: 99%

“…'- 3 Thickening of the vascular wall increases the wall's stiffness and narrows the vascular lumens, thereby producing an elevation of peripheral vascular resistance. Because some humoral substances, such as catecholamines, 4 steroids, 5 platelet-derived growth factor, 6 and insulin, 7 are reported to influence cell proliferation in various cell lines, these factors may be responsible to some extent for the vascular thickness observed in SHR. However, since vascular smooth muscle cells (VSMCs) of SHR sustain an enhanced proliferative activity even if they are cultured in an artificial medium, alterations of the biological properties of VSMCs are assumed to elicit the thickening of the vascular wall.…”

Section: S Pontaneously Hypertensive Rats (Shr)mentioning

confidence: 99%

Thromboxane and vascular smooth muscle cell growth in genetically hypertensive rats.

et al. 1988

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SUMMARYThe vascular wall has the capacity to produce thromboxane A 2 . However, the role of vascular thromboxane A 2 is still uncertain. In this study, we examined the relationship between vascular thromboxane A 2 generation and vascular smooth muscle cell growth in spontaneously hypertensive rats (SHR). Vascular thromboxane A 2 generation was significantly enhanced by 49% in 5-week-old and by 117% in 15-week-old SHR as compared with age-matched Wistar-Kyoto rats (WKY). Thromboxane in the prehypertensive stage show hyperplasia or hypertrophy in the cardiovascular system. '-3 Thickening of the vascular wall increases the wall's stiffness and narrows the vascular lumens, thereby producing an elevation of peripheral vascular resistance. Because some humoral substances, such as catecholamines, 4 steroids, 5 platelet-derived growth factor, 6 and insulin, 7 are reported to influence cell proliferation in various cell lines, these factors may be responsible to some extent for the vascular thickness observed in SHR. However, since vascular smooth muscle cells (VSMCs) of SHR From the

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Catecholamines are mitogenic in 3T3 and bovine aortic endothelial cells.

Cited by 41 publications

References 16 publications

Angiotensin II stimulates protein-tyrosine phosphorylation in a calcium-dependent manner.

Angiotensin II stimulates protein-tyrosine phosphorylation in a calcium-dependent manner.

Induction of the skeletal alpha-actin gene in alpha 1-adrenoceptor-mediated hypertrophy of rat cardiac myocytes.

Thromboxane and vascular smooth muscle cell growth in genetically hypertensive rats.

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