Tyrosine kinase participates in vasoconstriction through a Ca<sup>2+</sup>‐ and myosin light chain phosphorylation‐independent pathway

Fang, Lian; Kwon, Seong Chun; Zhang, Yong He; Ahn, Hee Yul

doi:10.1016/s0014-5793(02)02235-4

Cited by 6 publications

(5 citation statements)

References 31 publications

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“…Various studies have demonstrated a role of tyrosine phosphorylation in vascular tone regulation, but the mechanism remains elusive. 27,28 Our data therefore offer a mechanistic insight into how tyrosine phosphorylation is involved in vascular tone regulation.…”

Section: Discussionmentioning

confidence: 83%

Salicylates dilate blood vessels through inhibiting PYK2-mediated RhoA/Rho-kinase activation

Zhao

Giachini

Tostes

et al. 2009

Cardiovascular Research

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Section: Discussionmentioning

confidence: 83%

Salicylates dilate blood vessels through inhibiting PYK2-mediated RhoA/Rho-kinase activation

Zhao

Giachini

Tostes

et al. 2009

Cardiovascular Research

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“…Several studies of nonrenal vascular beds report attenuation of adrenoceptor-induced vasoconstriction by inhibitors of tyrosine kinases (1,8,10,13,22,43,53). Although tyrosine kinases may affect contractility of VSMC unrelated to [Ca 2ϩ ] i (12), other studies suggest that tyrosine kinases act, at least in part, via control of [Ca 2ϩ ] i (22,43). In addition, tyrosine kinase inhibitors impact on control of [Ca 2ϩ ] i to attenuate ANG II-and vasopressin-induced vasoconstriction (20,44).…”

Section: Discussionmentioning

confidence: 99%

Effect of tyrosine kinase blockade on norepinephrine-induced cytosolic calcium response in rat afferent arterioles

Salomonsson

Arendshorst

2004

American Journal of Physiology-Renal Physiology

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We used genistein (Gen) and tyrphostin 23 (Tyr-23) to evaluate the importance of tyrosine phosphorylation in norepinephrine (NE)-induced changes in intracellular free calcium concentration ([Ca(2+)](i)) in rat afferent arterioles. [Ca(2+)](i) was measured in microdissected arterioles using ratiometric photometry of fura 2 fluorescence. The control [Ca(2+)](i) response to NE (1 microM) consisted of a rapid initial peak followed by a plateau phase sustained above baseline. Pretreatment with the tyrosine kinase inhibitor Tyr-23 (50 microM, 10 min) caused a slow 40% increase in baseline [Ca(2+)](i). Tyr-23 attenuated peak and plateau responses to NE, both by approximately 70%. In the absence of extracellular Ca(2+) (0 Ca), Tyr-23 reduced the immediate [Ca(2+)](i) response to NE by approximately 60%, indicative of mobilization of internal stores, and abolished the plateau phase. In other arterioles, the [Ca(2+)](i) response to depolarization induced by KCl (50 mM) was not attenuated by Tyr-23, indicating no direct effect on L-type Ca(+) channels activated by depolarization. The Ca(2+) channel blocker nifedipine (1 microM) inhibited the NE response by approximately 50%; the effects of nifedipine and Tyr-23 were not additive. Nifedipine had no inhibitory effect after Tyr-23 pretreatment, indicating Tyr-23 inhibition of Ca(2+) entry. Another tyrosine kinase inhibitor, Gen (5 and 50 microM), did not affect baseline [Ca(2+)](i). High-dose Gen inhibited the peak and plateau response to NE by 87 and 75%, respectively; low-dose Gen attenuated both responses by approximately 20%. In 0 Ca, Gen (50 microM) abolished the immediate [Ca(2+)](i) mobilization response. Combined nifedipine and Gen (50 microM) inhibited the rapid NE response by approximately 90% in the presence of extracellular Ca(2+). Gen (50 microM) also inhibited by 60% the [Ca(2+)](i) response to 50 mM KCl, indicating a direct interaction with voltage-sensitive, L-type Ca(2+) entry channels. These results indicate that tyrosine phosphorylation is an important link in the chain of events leading to alpha-adrenoceptor-induced Ca(2+) recruitment (both entry and release) in afferent arteriolar smooth muscle cells. Furthermore, different blockers of tyrosine kinase appear to have different modes of action in renal microvessels.

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“…5A, B). Recently, we reported that tyrosine kinase participates in vasoconstriction through a Ca 2+ -and MLC phosphorylation-independent pathway [11]. Because tyrosine kinase is upstream regulators of MAPK, it is obvious that MLC is not the substrate for the tyrosine kinase-MAPK signaling pathway.…”

Section: Discussionmentioning

confidence: 99%

Mitogen-Activated Protein Kinases Partially Regulate Endothelin-1-Induced Contractions through a Myosin Light Chain Phosphorylation- Independent Patyway.

Kwon

Lee

Fang

et al. 2003

The Journal of Veterinary Medical Science

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ABSTRACT. Endothelin (ET), derived from the endothelium of blood vessels, is a potent vasoactive peptide. Although it has been reported to be involved in cardiovascular diseases, such as hypertension, the mechanism by which ET evokes vasoconstriction is still unclear. On the other hand, p42/p44 mitogen-activated protein kinase (MAPK) and p38 MAPK are activated by a variety of growth factors and cellular stresses, respectively. However, the role of p42/p44 MAPK and p38 MAPK on the ET-1-induced vasoconstriction is not fully understood. This study was undertaken to determine whether p42/p44 MAPK and p38 MAPK participate in the regulation of vascular smooth muscle contraction by ET-1. The isometric vasoconstriction and intracellular Ca 2+ ([Ca 2+ ] i ) were simultaneously measured using CAF-100. Phosphorylation of myosin light chain (MLC) and p42/p44 MAPK, p38 MAPK were determined by Western blots. In rat thoracic aorta, ET-1 induced a sustained contraction. In contrast, [Ca 2+ ] i was decreased with time. Both PD98059, an inhibitor of p42/ p44 MAPK, and SB203580, an inhibitor of p38 MAPK, partially attenuated ET-1-induced contractions in concentration-dependent manners. ET-1 increased phosphorylation of both p42/p44 MAPK and p38 MAPK, and PD98059 and SB203580 completely decreased phosphorylation of p42/p44 MAPK and p38 MAPK in response to ET-1 stimulation, respectively. On the other hand, PD98059 and SB203580 did not affect MLC phosphorylation in response to ET-1 stimulation. These results indicate that p38 MAPK, as well as p42/ p44 MAPK, may partially regulate the ET-1-induced contraction through a MLC phosphorylation-independent pathway. KEY WORDS: endothelin, mitogen-activated protein kinase, vasoconstriction.J. Vet. Med. Sci. 65(2): 225-230, 2003 Endothelin (ET) is a potent vasoactive peptide particularly derived from the endothelium of blood vessels [38]. ET is composed of 21-amino acids, and is classified into ET-1, ET-2 and ET-3 according to their amino acid composition [19]. ET-1 is the major ET generated in the endothelium. ET acts via specific plasma membrane receptors. ET A and ET B receptors have distinctive characteristics for ET [1,32]. ET A and ET B receptors on smooth muscle induce contraction and stimulate proliferation and cell hypertrophy [6]. Endothelial ET B receptors stimulate the production of nitric oxide and prostacyclin [33]. ET is known to be involved in cardiovascular diseases, including hypertension, myocardial infarction, congestive heart failure, restenosis and atherosclerosis [24].Many studies have evaluated ET-induced vasoconstriction. ET-1 evokes a long-lasting contraction, slow in onset, of isolated arteries, veins and in microcirculatory vessels from experimental animals and humans [2,4,25,38]. The mechanism by which contractions are evoked by ET-1 in isolated vascular preparations is complicated. The increase in the sensitivity of the contractile apparatus to intracellular Ca 2+ ([Ca 2+ ] i ), as well as the increase of [Ca 2+ ] i concentration, may be involved in ET-1-...

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Tyrosine kinase participates in vasoconstriction through a Ca²⁺‐ and myosin light chain phosphorylation‐independent pathway

Cited by 6 publications

References 31 publications

Salicylates dilate blood vessels through inhibiting PYK2-mediated RhoA/Rho-kinase activation

Salicylates dilate blood vessels through inhibiting PYK2-mediated RhoA/Rho-kinase activation

Effect of tyrosine kinase blockade on norepinephrine-induced cytosolic calcium response in rat afferent arterioles

Mitogen-Activated Protein Kinases Partially Regulate Endothelin-1-Induced Contractions through a Myosin Light Chain Phosphorylation- Independent Patyway.

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Tyrosine kinase participates in vasoconstriction through a Ca2+‐ and myosin light chain phosphorylation‐independent pathway

Cited by 6 publications

References 31 publications

Salicylates dilate blood vessels through inhibiting PYK2-mediated RhoA/Rho-kinase activation

Salicylates dilate blood vessels through inhibiting PYK2-mediated RhoA/Rho-kinase activation

Effect of tyrosine kinase blockade on norepinephrine-induced cytosolic calcium response in rat afferent arterioles

Mitogen-Activated Protein Kinases Partially Regulate Endothelin-1-Induced Contractions through a Myosin Light Chain Phosphorylation- Independent Patyway.

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Tyrosine kinase participates in vasoconstriction through a Ca²⁺‐ and myosin light chain phosphorylation‐independent pathway