scholarly journals Unsaturated Aldehyde Acrolein Promotes Retinal Glial Cell Migration

2019 ◽  
Vol 60 (13) ◽  
pp. 4425 ◽  
Author(s):  
Miyuki Murata ◽  
Kousuke Noda ◽  
Shiho Yoshida ◽  
Michiyuki Saito ◽  
Akio Fujiya ◽  
...  
Keyword(s):  
Cell Migration ◽  
Glial Cell ◽  
Unsaturated Aldehyde ◽  
Retinal Glial Cell

scholarly journals ROCK1 Mediates Retinal Glial Cell Migration Promoted by Acrolein

2021 ◽  
Vol 8 ◽  
Author(s):  
Kanae Fukutsu ◽  
Miyuki Murata ◽  
Kasumi Kikuchi ◽  
Shiho Yoshida ◽  
Kousuke Noda ◽  
...  
Keyword(s):  
Diabetic Retinopathy ◽  
Cell Migration ◽  
Glial Cell ◽  
Western Blotting ◽  
Glial Cells ◽  
Light Chain ◽  
Migration Rate ◽  
Myosin Light Chain ◽  
Rock Inhibitor ◽  
Retinal Glial Cell

Objective: Acrolein is a highly reactive aldehyde that covalently binds to cellular macromolecules and subsequently modulates cellular function. Our previous study demonstrated that acrolein induces glial cell migration, a pathological hallmark of diabetic retinopathy; however, the detailed cellular mechanism remains unclear. The purpose of this study was to investigate the role of acrolein in retinal glial cell migration by focusing on rho-associated coiled-coil-containing protein kinases (ROCKs).Methods: Immunofluorescence staining for ROCK isoforms was performed using sections of fibrovascular tissue obtained from the eyes of patients with proliferative diabetic retinopathy (PDR). Rat retinal Müller glial cell line, TR-MUL5, was stimulated with acrolein and the levels of ROCK1 were evaluated using real-time PCR and western blotting. Phosphorylation of the myosin-binding subunit of myosin light chain phosphatase [myosin phosphatase target subunit 1, (MYPT1)] and myosin light chain 2 (MLC2) was assessed. The cell migration rate of TR-MUL5 cells exposed to acrolein and/or ripasudil, a non-selective ROCK inhibitor, was measured using the Oris cell migration assay.Results: ROCK isoforms, ROCK1 and ROCK2, were positively stained in the cytosol of glial cells in fibrovascular tissues. In TR-MUL5 cells, the mRNA expression level of Rock1, but not Rock2, was increased following acrolein stimulation. In line with the PCR data, western blotting showed increase in ROCK1 and cleaved ROCK1 protein in TR-MUL5 cells stimulated with acrolein. N-acetylcysteine (NAC) suppressed acrolein-associated Rock1 upregulation in TR-MUL5 cells. Acrolein augmented the phosphorylation of MYPT1 and MLC2 and increased the cell migration rate of TR-MUL5 cells, both of which were abrogated by ripasudil.Conclusions: Our study demonstrated that ROCK1 mediates the migration of retinal glial cells promoted by the unsaturated aldehyde acrolein.

Retinal glial cell responses and Fas/FasL activation in rats with chronic ocular hypertension

2006 ◽  
Vol 1122 (1) ◽  
pp. 209-221 ◽  
Author(s):  
Kwang Ro Ju ◽  
Hwa Sun Kim ◽  
Jie Hyun Kim ◽  
Na Young Lee ◽  
Chan Kee Park
Keyword(s):  
Ocular Hypertension ◽  
Glial Cell ◽  
Cell Responses ◽  
Retinal Glial Cell

RACK1 (receptor for activated C-kinase 1) interacts with FBW2 (F-box and WD-repeat domain-containing 2) to up-regulate GCM1 (glial cell missing 1) stability and placental cell migration and invasion

2013 ◽  
Vol 453 (2) ◽  
pp. 201-208 ◽  
Author(s):  
Chang-Chun Wang ◽  
Hsiao-Fan Lo ◽  
Shu-Yu Lin ◽  
Hungwen Chen
Keyword(s):  
Cell Migration ◽  
Glial Cell ◽  
Affinity Purification ◽  
Migration And Invasion ◽  
Placental Development ◽  
Placental Cell ◽  
Cell Migration And Invasion ◽  
Repeat Domain ◽  
Wd Repeats ◽  
Wd Repeat

GCM1 (glial cell missing 1) is a short-lived transcription factor essential for placental development. The F-box protein, FBW2 (F-box and WD-repeat domain-containing 2), which contains five WD (tryptophan–aspartate) repeats, recognizes GCM1 and mediates its ubiquitination via the SCFFBW2 E3 ligase complex. Although the interaction between GCM1 and FBW2 is facilitated by GCM1 phosphorylation, it is possible that this interaction might be regulated by additional cellular factors. In the present study, we perform tandem-affinity purification coupled with MS analysis identifying RACK1 (receptor for activated C-kinase 1) as an FBW2-interacting protein. RACK1 is a multifaceted scaffold protein containing seven WD repeats. We demonstrate that the WD repeats in both RACK1 and FBW2 are required for the interaction of RACK1 and FBW2. Furthermore, RACK1 competes with GCM1 for FBW2 and thereby prevents GCM1 ubiquitination, which is also supported by the observation that GCM1 is destabilized in RACK1-knockdown BeWo placental cells. Importantly, RACK1 knockdown leads to decreased expression of the GCM1 target gene HTRA4 (high-temperature requirement protein A4), which encodes a serine protease crucial for cell migration and invasion. As a result, migration and invasion activities are down-regulated in RACK1-knockdown BeWo cells. The present study reveals a novel function for RACK1 to regulate GCM1 activity and placental cell migration and invasion.

scholarly journals Live Imaging of Glial Cell Migration in the Drosophila Eye Imaginal Disc

10.3791/1155 ◽  
2009 ◽  
Author(s):  
Patrick Cafferty ◽  
Xiaojun Xie ◽  
Kristen Browne ◽  
Vanessa J. Auld
Keyword(s):  
Cell Migration ◽  
Glial Cell ◽  
Imaginal Disc ◽  
Live Imaging ◽  
Drosophila Eye ◽  
Eye Imaginal Disc

scholarly journals Kallikrein Gene Transfer Protects Against Ischemic Stroke by Promoting Glial Cell Migration and Inhibiting Apoptosis

Hypertension ◽  
2004 ◽  
Vol 43 (2) ◽  
pp. 452-459 ◽  
Author(s):  
Chun-Fang Xia ◽  
Hang Yin ◽  
Cesar V. Borlongan ◽  
Lee Chao ◽  
Julie Chao
Keyword(s):  
Cell Migration ◽  
Ischemic Stroke ◽  
Gene Transfer ◽  
Glial Cell

Kir4.1 and AQP4 associate with Dp71- and utrophin-DAPs complexes in specific and defined microdomains of Müller retinal glial cell membrane

Glia ◽  
2008 ◽  
Vol 56 (6) ◽  
pp. 597-610 ◽  
Author(s):  
Patrice E. Fort ◽  
Abdoulaye Sene ◽  
Thomas Pannicke ◽  
Michel J. Roux ◽  
Valerie Forster ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Glial Cell ◽  
Retinal Glial Cell

scholarly journals Polysialic Acid-Directed Migration and Differentiation of Neural Precursors Are Essential for Mouse Brain Development

2007 ◽  
Vol 27 (19) ◽  
pp. 6659-6668 ◽  
Author(s):  
Kiyohiko Angata ◽  
Valerie Huckaby ◽  
Barbara Ranscht ◽  
Alexey Terskikh ◽  
Jamey D. Marth ◽  
...  
Keyword(s):  
Cell Migration ◽  
Brain Development ◽  
Glial Cell ◽  
Neural Development ◽  
Apoptotic Cell ◽  
Polysialic Acid ◽  
Neural Cell ◽  
Neural Precursors

ABSTRACT Polysialic acid, which is synthesized by two polysialyltransferases, ST8SiaII and ST8SiaIV, plays an essential role in brain development by modifying the neural cell adhesion molecule (NCAM). It is currently unclear how polysialic acid functions in different processes of neural development. Here we generated mice doubly mutant in both ST8SiaII and ST8SiaIV to determine the effects of loss of polysialic acid on brain development. In contrast to NCAM-deficient, ST8SiaII-deficient, or ST8SiaIV-deficient single mutant mice, ST8SiaII and ST8SiaIV double mutants displayed severe defects in anatomical organization of the forebrain associated with apoptotic cell death. Loss of polysialic acid affected both tangential and radial migration of neural precursors during cortical development, resulting in aberrant positioning of neuronal and glial cells. Glial cell differentiation was aberrantly increased in vivo and in vitro in the absence of polysialic acid. Consistent with these findings, polysialic acid-deficient mice exhibited increased expression of the glial cell marker glial fibrillary acidic protein and a decrease in expression of Pax6, a transcription factor regulating neural cell migration. These results indicate that polysialic acid regulates cell migration and differentiation of neural precursors crucial for brain development.

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