Implications of protease M/neurosin in myelination during experimental demyelination and remyelination

Bandô, Yoshio; Ito, Shinji; Nagai, Yoshiko; Terayama, Ryuji; Kishibe, Mari; Jiang, Ying; Mitrovic, Branislava; Takahashi, Takayuki; Yoshida, Shigetaka

doi:10.1016/j.neulet.2006.06.030

Cited by 35 publications

(45 citation statements)

References 33 publications

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“…Reports have shown that siRNA and RNAi were able to knockdown kallikrein gene and protein expression (Bando et al, 2006;Klokk et al, 2007;Shinoda et al, 2007). It should be noted, however, that the endogenous or exogenous siRNAs and synthetic RNAi do not function exactly similar to miRNAs (Yousef, 2008).…”

Section: Discussionmentioning

confidence: 99%

Three dysregulated miRNAs control kallikrein 10 expression and cell proliferation in ovarian cancer

et al. 2010

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BACKGROUND: Kallikrein-related peptidases (KLKs) are a family of serine proteases that have been shown to be dysregulated in several malignancies including ovarian cancer. The control of kallikrein genes and their physiological function in cancer is not well understood. We hypothesized that microRNAs (miRNAs) represent a novel mechanism for post-transcriptional control of KLK expression in cancer. METHODS: We first analysed miRNA expression in ovarian cancer in silico. A total of 98 miRNAs were reported to have altered expression in ovarian cancer. Three of these miRNAs were predicted to target KLK10. We experimentally verified the predicted miR -KLK10 interaction using two independent techniques, a luciferase assay with a construct containing the KLK10 3 0 untranslated region (UTR), pMIR -KLK10, and measuring KLK10 protein levels after transfection with miRNA. RESULTS: When we co-transfected cells with pMIR -KLK10 and either let-7f, miR-224, or mR-516a, we saw decreased luciferase signal, suggesting that these miRNAs can target KLK10. We then examined the effect of these three miRNAs on KLK10 protein expression and cell growth. Transfection of all miRNAs, let-7f, miR-224, and miR-516a led to a decrease in protein expression and cellular growth. This effect was shown to be dose dependent. The KLK10 protein levels were partially restored by co-transfecting let-7f and its inhibitor. In addition, there was a slight decrease in KLK10 mRNA expression after transfection with let-7f. CONCLUSIONS: Our results confirm that KLKs can be targeted by more than one miRNA. Increased expression of certain miRNAs in ovarian cancer can lead to decreased KLK protein expression and subsequently have a negative effect on cell proliferation. This dose-dependent effect suggests that a 'tweaking' or 'fine-tuning' mechanism exists in which the expression of one KLK can be controlled by multiple miRNAs. These data together suggest that miRNA may be used as potential therapeutic options and further studies are required.

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Section: Discussionmentioning

confidence: 99%

Three dysregulated miRNAs control kallikrein 10 expression and cell proliferation in ovarian cancer

et al. 2010

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“…These studies suggest that neurosin is involved in the pathogenesis of multiple sclerosis. In contrast, Bando et al [64] suggest that neurosin is important for the maintenance of myelination after brain in-…”

Section: Neurosinmentioning

confidence: 90%

“…A C H T U N G T R E N N U N G dendrocytes during demyelination in mice fed with cuprizone, but neurosin is increased during remyel-A C H T U N G T R E N N U N G inaA C H T U N G T R E N N U N G tion when mice are returned to the normal diet [64]. Abnormal expression of neurosin in the brain has also been observed in animal models of other neurodegenerative disorders.…”

Section: A C H T U N G T R E N N U N G Sults Under That Condition Nmentioning

confidence: 97%

Trypsin and trypsin-like proteases in the brain: Proteolysis and cellular functions

Wang

Luo

Reiser

2007

Cell. Mol. Life Sci.

120

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Several serine proteases including thrombin, tissue-type plasminogen activator and urokinase-type plasminogen activator have been well characterized in the brain. In this article, we review the brain-related trypsin and trypsin-like serine proteases. Accumulating evidence demonstrates that trypsin and trypsin-like serine proteases play very important roles in neural development, plasticity, neurodegeneration and neuroregeneration in the brain. Neuropsin is able to hydrolyze the extracellular matrix components by its active site serine, and regulates learning and memory in normal brain. The mutant neurotrypsin contributes to mental retardation in children. Neurosin seems to be involved in the pathogenesis of neurodegenerative disorders, like Alzheimer's disease, Parkinson's disease or multiple sclerosis. Although mesotrypsin/trypsin IV is also implicated in neurodegeneration, its functional significance still remains largely unknown. Particularly, mesotrypsin/trypsin IV, P22 and neurosin exert their physiological and pathological functions through activation of certain protease-activated receptors (PARs). In the brain, the presence of serpins controls the activity of serine proteases. Therefore, understanding the interaction among brain trypsin, serpins and PARs will provide invaluable tools for regulating normal brain functions and for the clinical treatment of neural disorders.

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“…To introduce demyelination in the corpus callosum, female B6 mice (n = 3-4 animals/ experimental group), aged 6-8 weeks, were fed chow containing 0.2% cuprizone for 6 weeks as previously described (Bando et al, 2006;Tanaka et al, 2013). After 6 weeks of cuprizone treatment, remyelination was initiated by returning the mice to a normal diet (Nihon SLC.…”

Section: Cuprizone-induced Demyelination/remyelinationmentioning

confidence: 99%

Abnormal morphology of myelin and axon pathology in murine models of multiple sclerosis

Bandô

Nomura

Bochimoto

et al. 2015

Neurochemistry International

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Implications of protease M/neurosin in myelination during experimental demyelination and remyelination

Cited by 35 publications

References 33 publications

Three dysregulated miRNAs control kallikrein 10 expression and cell proliferation in ovarian cancer

Three dysregulated miRNAs control kallikrein 10 expression and cell proliferation in ovarian cancer

Trypsin and trypsin-like proteases in the brain: Proteolysis and cellular functions

Abnormal morphology of myelin and axon pathology in murine models of multiple sclerosis

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