Publications by authors named "Hiroyuki Imaki"

A 53-year-old Japanese female developed a fever about two months after a tick bite. She also exhibited blurred vision, central scotoma in the left eye, left facial paresis and mild ataxia. A fundus examination revealed left disc swelling in the left eye.

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Purpose: To evaluate the individualized, optical coherence tomography-guided facedown posturing after macular hole (MH) surgery in minimizing the burden and maximizing outcome.

Methods: A retrospective comparative study. One hundred and seven consecutive eyes with an MH (<500 μm) received vitrectomy and gas tamponade.

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Background: Neovascular glaucoma (NVG) is a serious complication for patients with proliferative diabetic retinopathy (PDR). Bevacizumab is a full-length humanized monoclonal antibody that binds all isoforms of vascular endothelial growth factor (VEGF). Recently, encouraging results regarding the off-label use of intravitreal bevacizumab (IVB) for the treatment of NVG have been reported.

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The F-box protein Skp2 mediates c-Myc ubiquitylation by binding to the MB2 domain. However, the turnover of c-Myc is largely dependent on phosphorylation of threonine-58 and serine-62 in MB1, residues that are often mutated in cancer. We now show that the F-box protein Fbw7 interacts with and thereby destabilizes c-Myc in a manner dependent on phosphorylation of MB1.

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Article Synopsis
  • The cyclin-dependent kinase inhibitor p57Kip2 is regulated by the SCFSkp2 ubiquitin ligase complex, which targets it for degradation through ubiquitylation.
  • Without Skp2, there's an abnormal buildup of p57Kip2, affecting cell-cycle progression.
  • Phosphorylation of a specific residue (Thr-310) on p57Kip2 is necessary for its degradation, indicating a link between cyclin E-CDK2 and SCFSkp2 action.
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Skp2 is the F-box protein component of an SCF-type ubiquitin ligase that interacts specifically with p27(Kip1) and thereby promotes its ubiquitylation and degradation. The abundance of Skp2 mRNA oscillates in a cell cycle-dependent manner, being maximal in S and G(2) phases. The regulation of Skp2 transcription was investigated by cloning the promoter region of the mouse gene and determination of its activity in a luciferase reporter assay.

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Protein kinase C (PKC), which comprises 11 closely related isoforms, has been implicated in a wide variety of cellular processes, such as growth, differentiation, secretion, apoptosis and tumour development. Among the PKC isotypes, PKC-delta is unique in that its overexpression results in inhibition of cell growth. Here we show that mice that lack PKC-delta exhibit expansion of the B-lymphocyte population with the formation of numerous germinal centres in the absence of stimulation.

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Background: The ubiquitin-proteasome pathway of proteolysis controls the abundance of specific regulatory proteins. The SCF complex is a type of ubiquitin-protein ligase (E3) that contributes to this pathway in many biological systems. In yeast and mammals, the SCF complex consists of common components, including Skp1, Cdc53/Cul1, and Rbx1, as well as variable components known as F-box proteins.

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