Involvement of <i>rho</i> in GTPγS‐induced enhancement of phosphorylation of 20 kDa myosin light chain in vascular smooth muscle cells: inhibition of phosphatase activity

Noda, Masakuni; Yasuda-Fukazawa, Chikako; Moriishi, Kohji; Kato, Tsuguhiko; Okuda, Takatoshi; Kurokawa, Kiyoshi; Takuwa, Yoh

doi:10.1016/0014-5793(95)00573-r

Cited by 170 publications

(121 citation statements)

References 28 publications

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“…Several proteins have been identified as effectors of Rho, including protein kinase N [PKN (PRK1)], Rho-associated protein kinases 1 and 2 (ROCK1 and ROCK2), the myosin-binding subunit of myosin phosphatase, rhophilin, rhotekin, citron, p140 mDia, and citron kinase (28 -30). Studies have shown that Rho-kinase participates in smooth muscle contraction through agonist-induced Ca 2ϩ -sensitization, and is thought to act by inhibiting myosin phosphatase activity and phosphorylating myosin light chain directly (32). In our study, ROCK2 was found to be 1.6-fold up-regulated in diabetic smooth muscle.…”

Section: Effect Of Diabetes On Detrusor Smooth Muscle In Tallyhosupporting

confidence: 52%

Tissue Specific Dysregulated Protein Subnetworks in Type 2 Diabetic Bladder Urothelium and Detrusor Muscle

Tomechko¹,

Liu

Tao

et al. 2015

Molecular & Cellular Proteomics

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Diabetes mellitus is well known to cause bladder dysfunction; however, the molecular mechanisms governing this process and the effects on individual tissue elements within the bladder are poorly understood, particularly in type 2 diabetes. A shotgun proteomics approach was applied to identify proteins differentially expressed between type 2 diabetic (TallyHo) and control (SWR/J) mice in the bladder smooth muscle and urothelium, separately. We were able to identify 1760 nonredundant proteins from the detrusor smooth muscle and 3169 nonredundant proteins from urothelium. Pathway and network analysis of significantly dysregulated proteins was conducted to investigate the molecular processes associated with diabetes. This pinpointed ERK1/2 signaling as a key regulatory node in the diabetes-induced pathophysiology for both tissue types. Diabetes mellitus is reaching epidemic proportions worldwide because of several factors, most notably obesity, which is attributed to increased sedentary lifestyles and decreased physical activity. This presents both economic and healthcare challenges; the U.S., China, and India have the highest disease prevalences and therefore are facing the greatest challenges (1). According to the Centers for Disease Control and Prevention, as of 2010, 25.8 million Americans have diabetes, and it is the seventh leading cause of death in the United States. Approximately 30% of U.S. adults 20 years or older and 50% of adults 75 years or older are afflicted with this debilitating disease (2). Based on current trends, it is expected that the number of patients diagnosed with diabetes will continue to climb at an alarming rate.Some complications of diabetes include heart disease and stroke, hypertension, blindness and eye problems, kidney disease, and nervous system disease. Recently, diabetic urological complications such as nephropathy, bladder dysfunction (3) and infection, incontinence, erectile dysfunction (4), and prostate hyperplasia have been receiving increasing attention, because they affect both type 1 and type 2 diabetic patients. Diabetic uropathy, which includes diabetic bladder dysfunction (DBD) 1 , sexual or erectile dysfunction, and urinary tract infection (5), has been found in more than 80% of patients with diabetes, a higher rate of incidence than either neuropathy or nephropathy, which affect 60 and 50% of From the ‡Center

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Section: Effect Of Diabetes On Detrusor Smooth Muscle In Tallyhosupporting

confidence: 52%

Tissue Specific Dysregulated Protein Subnetworks in Type 2 Diabetic Bladder Urothelium and Detrusor Muscle

Tomechko¹,

Liu

Tao

et al. 2015

Molecular & Cellular Proteomics

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“…Other data were accumulated using skinned smooth muscle strips to show that MLCP can be inhibited through a rho pathway (Kitazawa et al, 1991;Hirata et al, 1992;Somlyo and Somlyo, 1994;Gong et al, 1996). Inhibition of MLCP by rho also was shown with cultured vascular SMCs (Noda et al, 1995). Phosphorylation of M130 was shown to inhibit phosphatase activity in skinned muscle (Trinkle-Mulcahy et al, 1995).…”

Section: Localization Of Mlcp In Migrating Fibroblastsmentioning

confidence: 99%

Differential localization of myosin and myosin phosphatase subunits in smooth muscle cells and migrating fibroblasts.

Murata

Hirano

Villa-Moruzzi

et al. 1997

MBoC

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Myosin II light chains (MLC20) are phosphorylated by a Ca2+/calmodulin-activated kinase and dephosphorylated by a phosphatase that has been purified as a trimer containing the 8 isoform of type 1 catalytic subunit (PP1C6), a myosin-binding 130-kDa subunit (M130) and a 20-kDa subunit. The distribution of M130 and PP1C as well as myosin II was examined in smooth muscle cells and fibroblasts by immunofluorescence microscopy and immunoblotting after differential extraction. Myosin and M130 colocalized with actin stress fibers in permeabilized cells. However, in nonpermeabilized cells the staining for myosin and M130 was different, with myosin mostly at the periphery of the cell and the M130 appearing diffusely throughout the cytoplasm. Accordingly, most M130 was recovered in a soluble fraction during permeabilization of cells, but the conditions used affected the solubility of both M130 and myosin. The PPlCa isoform colocalized with M130 and also was in the nucleus, whereas the PP1C6 isoform was localized prominently in the nucleus and in focal adhesions. In migrating cells, M130 concentrated in the tailing edge and was depleted from the leading half of the cell, where double staining showed myosin II was present. Because the tailing edge of migrating cells is known to contain phosphorylated myosin, inhibition of myosin LC20 phosphatase, probably by phosphorylation of the M130 subunit, may be required for cell migration.

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“…Rho kinase is also implicated in the regulation of MLC phosphorylation (10,11). Activated by the small GTP-binding protein RhoA, Rho kinase phosphorylates the myosin-binding subunit of myosin phosphatase and inhibits its activity.…”

mentioning

confidence: 99%

P2X1-mediated ERK2 Activation Amplifies the Collagen-induced Platelet Secretion by Enhancing Myosin Light Chain Kinase Activation

Tóth-Zsámboki

Oury

Cornelissen

et al. 2003

Journal of Biological Chemistry

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The ATP-gated P2X 1 ion channel is the only P2X subtype expressed in human platelets. Via transmission electron microscopy, we found that P2X 1 mediates fast, reversible platelet shape change, secretory granule centralization, and pseudopodia formation. In washed human platelets, the stable P2X 1 agonist ␣,␤-methylene ATP (␣,␤-meATP) causes rapid, transient (2-5 s), and dosedependent myosin light chain (MLC) phosphorylation, requiring extracellular Ca 2؉. Phosphorylation was inhibited by the calmodulin (CaM) inhibitor W-7, but not by the Rho kinase inhibitor HA-1077, i.e. it is exclusively regulated by Ca 2؉

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Involvement of rho in GTPγS‐induced enhancement of phosphorylation of 20 kDa myosin light chain in vascular smooth muscle cells: inhibition of phosphatase activity

Cited by 170 publications

References 28 publications

Tissue Specific Dysregulated Protein Subnetworks in Type 2 Diabetic Bladder Urothelium and Detrusor Muscle

Tissue Specific Dysregulated Protein Subnetworks in Type 2 Diabetic Bladder Urothelium and Detrusor Muscle

Differential localization of myosin and myosin phosphatase subunits in smooth muscle cells and migrating fibroblasts.

P2X1-mediated ERK2 Activation Amplifies the Collagen-induced Platelet Secretion by Enhancing Myosin Light Chain Kinase Activation

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