Visual outcomes for high myopic patients with or without myopic maculopathy: a 10 year follow up study

Shih, Yung‐Feng; Ho, T. C.; Hsiao, Chuhsing Kate; Lin, Longfei

doi:10.1136/bjo.2005.081992

Cited by 98 publications

(87 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our observed changes in MYPT1 subcellular distribution in the intact cerebral vasculature following G-protein coupled receptor stimulation by both confocal microscopy and traditional biochemical fractionation methods are in agreement with previously published studies (33,34). However, our observations suggest that MYPT1 phosphorylation at either Thr-696 or Thr-853 is not a prerequisite for membrane association, contrary to the model proposed by Shin et al (33) based upon data from isolated ferret portal vein smooth muscle cells.…”

Section: Discussioncontrasting

confidence: 57%

“…Coincident with the Ca 2ϩ sensitization-induced phosphorylation of MYPT1 at Thr-696, MLCP has been observed to translocate from the cytosol to the cell membrane following stimulation with prostaglandin F 2␣ and sphingosine 1-phosphate in freshly isolated ferret portal vein SMCs (33) and in hamster resistance arteries (34), suggesting that removal of MLCP from the actomyosin contractile apparatus may be an additional mechanism of Ca 2ϩ sensitization. Though presently an interesting observation associated with Ca 2ϩ sensitization, the underlying function, magnitude, and mechanism of its translocation to the membrane is presently unknown.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Thromboxane A2-induced Bi-directional Regulation of Cerebral Arterial Tone

Neppl

Lubomirov

Momotani

et al. 2009

Journal of Biological Chemistry

View full text Add to dashboard Cite

Section: Discussioncontrasting

confidence: 57%

mentioning

confidence: 99%

Thromboxane A2-induced Bi-directional Regulation of Cerebral Arterial Tone

Neppl

Lubomirov

Momotani

et al. 2009

Journal of Biological Chemistry

View full text Add to dashboard Cite

“…Native ROCK is largely membranebound when activated by RhoA, raising the question as to how ROCK can directly phosphorylate MYPT1 and myosin (27,28). Although MYPT1 has been shown to localize to the membrane in smooth muscle cells (50,51), this again begs the identity of the cytosolic kinase that induces MYPT1 phosphorylation and translocation. These previous findings in combination with data presented herein suggest that ZIPK stands squarely downstream of both Rho and ROCK signaling, forming a signal transduction module to ultimately regulate myosin phosphorylation in both smooth muscle and non-muscle cells.…”

Section: Discussionmentioning

confidence: 99%

ROCK1 Phosphorylates and Activates Zipper-interacting Protein Kinase

Hagerty

Weitzel

Chambers

et al. 2007

Journal of Biological Chemistry

View full text Add to dashboard Cite

Zipper-interacting protein kinase (ZIPK) regulates Ca2؉ -independent phosphorylation of both smooth muscle (to regulate contraction) and non-muscle myosin (to regulate non-apoptotic cell death) through either phosphorylation and inhibition of myosin phosphatase, the myosin phosphatase inhibitor CPI17, or direct phosphorylation of myosin light chain. ZIPK is regulated by multisite phosphorylation. Phosphorylation at least three sites Thr-180, Thr-225, and Thr-265 has been shown to be essential for full activity, whereas phosphorylation at Thr-299 regulates its intracellular localization. Herein we utilized an unbiased proteomics screen of smooth muscle extracts with synthetic peptides derived from the sequence of the regulatory phosphorylation sites of the enzyme to identify the protein kinases that might regulate ZIPK activity in vivo. Discrete kinase activities toward Thr-265 and Thr-299 were defined and identified by mass spectrometry as Rho kinase 1 (ROCK1). In vitro, ROCK1 showed a high degree of substrate specificity toward native ZIPK, both stoichiometrically phosphorylating the enzyme at Thr-265 and Thr-299 as well as bringing about activation. In HeLa cells, coexpression of ZIPK with ROCK1 altered the ROCK-induced phenotype of focused stress fiber pattern to a Rho-like phenotype of parallel stress fiber pattern. This effect was also dependent upon phosphorylation at Thr-265. Our findings provide a new regulatory pathway in smooth muscle and non-muscle cells whereby ROCK1 phosphorylates and regulates ZIP kinase.

show abstract

“…Recent data suggest that phosphorylation of MBS may play a role in the regulation of MLCP localization within the cell (33,34). Studies have shown that MBS can bind to actin-myosin stress fibers, supporting a potential role for MBS in the cellular localization of the heterotrimeric phosphatase (20,31,35).…”

mentioning

confidence: 99%

M-RIP Targets Myosin Phosphatase to Stress Fibers to Regulate Myosin Light Chain Phosphorylation in Vascular Smooth Muscle Cells

Surks

Riddick

Ohtani

2005

Journal of Biological Chemistry

View full text Add to dashboard Cite

Vascular smooth muscle cell contraction and relaxation are directly related to the phosphorylation state of the regulatory myosin light chain. Myosin light chains are dephosphorylated by myosin phosphatase, leading to vascular smooth muscle relaxation. Myosin phosphatase is localized not only at actin-myosin stress fibers where it dephosphorylates myosin light chains, but also in the cytoplasm and at the cell membrane. The mechanisms by which myosin phosphatase is targeted to these loci are incompletely understood. We recently identified myosin phosphatase-Rho interacting protein as a member of the myosin phosphatase complex that directly binds both the myosin binding subunit of myosin phosphatase and RhoA and is localized to actin-myosin stress fibers. We hypothesized that myosin phosphatase-Rho interacting protein targets myosin phosphatase to the contractile apparatus to dephosphorylate myosin light chains. We used RNA interference to silence the expression of myosin phosphatase-Rho interacting protein in human vascular smooth muscle cells. Myosin phosphatase-Rho interacting protein silencing reduced the localization of the myosin binding subunit to stress fibers. This reduction in stress fiber myosin phosphatase-Rho interacting protein and myosin binding subunit increased basal and lysophosphatidic acid-stimulated myosin light chain phosphorylation. Neither cellular myosin phosphatase, myosin light chain kinase, nor RhoA activities were changed by myosin phosphataseRho interacting protein silencing. Furthermore, myosin phosphatase-Rho interacting protein silencing resulted in marked phenotypic changes in vascular smooth muscle cells, including increased numbers of stress fibers, increased cell area, and reduced stress fiber inhibition in response to a Rho-kinase inhibitor. These data support the importance of myosin phosphatase-Rho interacting protein-dependent targeting of myosin phosphatase to stress fibers for regulating myosin light chain phosphorylation state and morphology in human vascular smooth muscle cells.Blood vessel tone is important in the regulation of blood pressure and tissue perfusion. Disorders of blood vessel tone play a prominent role in the pathogenesis of hypertension, vascular spasm, and acute coronary syndromes (1-5). Blood vessel tone is itself controlled by the contraction and relaxation of vascular smooth muscle cells (VSMCs) 2 in the media of the blood vessel wall. VSMC contraction is determined by the phosphorylation state of the regulatory myosin light chain (MLC) (6). Phosphorylation of MLC at serine 19 leads to actin-activated myosin ATPase activity, cross-bridge cycling, and contraction (7,8). MLC is phosphorylated by the calcium/ calmodulin-regulated myosin light chain kinase (MLCK), which phosphorylates MLC leading to VSMC contraction (9, 10). Myosin light chain phosphatase (MLCP) dephosphorylates MLC causing VSMC relaxation (11). The counter regulatory activities of MLCK and MLCP control MLC phosphorylation state in response to contractile agonists and vasodilators.MLCP...

show abstract

Visual outcomes for high myopic patients with or without myopic maculopathy: a 10 year follow up study

Abstract: Clearly, prognosis for patients with maculopathy is poorer than for those without maculopathy. Refractive status, axial length, and ageing are the main factors involved in determining the visual outcomes. The macular grading also affects the visual outcome for high myopic patients.

Cited by 98 publications

References 35 publications

Thromboxane A2-induced Bi-directional Regulation of Cerebral Arterial Tone

Thromboxane A2-induced Bi-directional Regulation of Cerebral Arterial Tone

ROCK1 Phosphorylates and Activates Zipper-interacting Protein Kinase

M-RIP Targets Myosin Phosphatase to Stress Fibers to Regulate Myosin Light Chain Phosphorylation in Vascular Smooth Muscle Cells

Contact Info

Product

Resources

About