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Zhou C.-H.,Wuhan University | Long Y.-M.,Wuhan Institute of Biotechnology | Qi B.-P.,Wuhan Institute of Biotechnology | Pang D.-W.,Wuhan Institute of Biotechnology | Zhang Z.-L.,Wuhan Institute of Biotechnology
Electrochemistry Communications

A novel electrochemical immunosensor based on the integration of immunomagnetic separation and bienzymatic amplification for sensitive detection of virus particles was fabricated in this work. The bienzymatic strategy was realized by using the first enzyme as tracer tagged on immunomagnetic beads which could be accumulated on the magneto controlled home-made Au electrode (m-AuE) and the second enzyme immobilized on the m-AuE by layer-by-layer (LBL) assembly technique. The proposed immunosensor not only provides a rapid, simple, cost-effective and on-site platform with high sensitivity, selectivity, and reproducibility for early diagnosis but also presents a new approach for sensitive magneto immunoassay. © 2013 Elsevier B.V. Source

Huang L.,Huazhong University of Science and Technology | Liu X.,Huazhong University of Science and Technology | Cheng B.,Central Hospital of Wuhan | Huang K.,Huazhong University of Science and Technology | Huang K.,Wuhan Institute of Biotechnology
Archives of Biochemistry and Biophysics

The process of protein aggregation from soluble amyloidogenic proteins to insoluble amyloid fibrils plays significant roles in the onset of over 30 human amyloidogenic diseases, such as Prion disease, Alzheimer's disease and type 2 diabetes mellitus. Amyloid deposits are commonly found in patients suffered from amyloidosis; however, such deposits are rarely seen in healthy individuals, which may be largely attributed to the self-regulation in vivo. A vast number of physiological factors have been demonstrated to directly affect the process of amyloid formation in vivo. In this review, physiological factors that influence amyloidosis, including biological factors (chaperones, natural antibodies, enzymes, lipids and saccharides) and physicochemical factors (metal ions, pH environment, crowding and pressure, etc.), together with the mechanisms underlying these proteostasis effects, are summarized. © 2015 Elsevier Inc. Source

Li Y.,Huazhong University of Science and Technology | Yan J.,Huazhong University of Science and Technology | Zhang X.,Huazhong University of Science and Technology | Huang K.,Huazhong University of Science and Technology | Huang K.,Wuhan Institute of Biotechnology
Proteins: Structure, Function and Bioinformatics

More than 20 human diseases, including Alzheimer's disease, Parkinson's disease, and prion disease, originate from the deposition of misfolded proteins. These proteins, referred as amyloidogenic proteins, adopt a β-sheet-rich structure when transformed from soluble state into insoluble amyloid fibrils. Amyloid formation is influenced by a number of factors that affect the intermolecular interaction, including pH, temperature, ion strength, and chemical bonds. In this review, we focus on the role of disulfide on the stability, structure, oligomerization, and amyloidogenecity of native folded or unfolded amyloidogenic proteins. The effects of introduced disulfide bonds on the amyloidogenicity of proteins lacking native disulfide are also reviewed. © 2013 Wiley Periodicals, Inc. Source

Chen H.,Huazhong University of Science and Technology | Li J.,Wuhan University | Jiao L.,Huazhong University of Science and Technology | Petersen R.B.,Case Western Reserve University | And 4 more authors.
Journal of Physiology

Diabetic nephropathy is the primary cause of end-stage renal disease. Increasing numbers of patients are suffering from this disease and therefore novel medications and therapeutic approaches are urgently needed. Here, we investigated whether apelin-13, the most active member of the adipokine apelin group, could effectively suppress the development of nephropathy in Akita mouse, a spontaneous type 1 diabetic model. Apelin-13 treatment decreased diabetes-induced glomerular filtration rate, proteinuria, glomerular hypertrophy, mesangial expansion and renal inflammation. The inflammatory factors, activation of NF-κB, histone acetylation and the enzymes involved in histone acetylation were further examined in diabetic kidneys and high glucose- or sodium butyrate-treated mesangial cells in the presence or absence of apelin-13. Apelin-13 treatment inhibited diabetes-, high glucose- and NaB-induced elevation of inflammatory factors, and histone hyperacetylation by upregulation of histone deacetylase 1. Furthermore, overexpression of apelin in mesangial cells induced histone deacetylation under high glucose condition. Thus, apelin-13 may be a novel therapeutic candidate for treatment of diabetic nephropathy via regulation of histone acetylation. © 2013 The Physiological Society. Source

Liu X.,Huazhong University of Science and Technology | Gong H.,Huazhong University of Science and Technology | Huang K.,Huazhong University of Science and Technology | Huang K.,Wuhan Institute of Biotechnology
Cancer Science

The kinesin superfamily (KIF) is a group of proteins that share a highly conserved motor domain. Except for some members, many KIF proteins have adenosine triphosphatase activity and microtubule-dependent plus-end motion ability. Kinesins participate in several essential cellular functions, including mitosis, meiosis and the transport of macromolecules. Increasing evidence indicates kinesin proteins play critical roles in the genesis and development of human cancers. Some kinesin proteins are associated with maligancy as well as drug resistance of solid tumor. Thus, targeting KIF therapy seems to be a promising anticancer strategy. Inhibitors of KIF such as kinesin spindle protein (KSP/Eg5) have entered clinical trials for monotherapy or in combination with other drugs, and kinesins other than Eg5 with various potential anticancer target characteristics are also constantly being discovered and studied. Here, we summarize the oncogenic roles of kinesin proteins and potential cancer therapy strategies that target KIF. © 2013 © 2013 Japanese Cancer Association. Source

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