Key Laboratory of Marine Drugs

Key Laboratory of Marine Drugs

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Wu Y.-L.,Ocean University of China | Wu Y.-L.,Key Laboratory of Marine Drugs | Xin X.-J.,Weifang Medical University | Xin X.-L.,CAS Shanghai Institute of Materia Medica | And 3 more authors.
Chinese Pharmacological Bulletin | Year: 2011

As a key factor of Alzheimer's disease(AD), β-amyloid(Aβ) has emerged as an attractive drug target. Aβ species produced inhibitor is one of the most important aspects in anti-AD drug research and developement. Recent advances showed that some Aβ-related proteins, including β-amyloid precursor protein (APP), γ-secretase complex PS-1 and APH-1, have a special structure in transmembrane sequence (TMS) , an amino-acid motif GXXXG, which has a regulatory impact on Aβ species production and aggregation. This paper describes the regulation of GXXXG structure to the function of AD-related proteins, which may hold the promise for the development of anti-AD drugs.


Wang X.-L.,Ocean University of China | Wang X.-L.,Key Laboratory of Marine Drugs | Fang Y.-C.,Ocean University of China | Fang Y.-C.,Key Laboratory of Marine Drugs | And 2 more authors.
Chinese Pharmacological Bulletin | Year: 2012

The inhibitor kappa B kinase β (IKKβ) is the crucial catalytic subunit of the IKK complex in the course of the nuclear transcription factor kappa B (NF-κB) activation via classical (or canonical) pathway. Not IKKβ is only regulated by various upstream kinases, but also it regulates the expression of multiple target genes related to many diseases. Especially, it plays a cru-cial role in the development of inflammatory response and cancer, providing a molecular link between inflammation and cancer. To sum up, this article reviews the structure, function of IKKβ, as well as the development of inhibitors in these years.


Ma L.,Key Laboratory of Marine Drugs | Liu J.,Qingdao University | Zhang X.,Key Laboratory of Marine Drugs | Qi J.,Key Laboratory of Marine Drugs | And 2 more authors.
Medical Oncology | Year: 2015

Temozolomide (TMZ) is an effective agent for clinical glioma treatment, but the innate and acquired resistance of glioma always limits its application. Although some advances have been achieved to elucidate the molecular mechanism underlying TMZ resistance, the role of Nrf2 (a principle regulator of cellular defense against drugs and oxidative stress) has not been well established in the acquisition of this phenotype. Our data showed that TMZ treatment induces the activation of Nrf2 and p38 MAPK signaling in glioma cells, while p38 inhibition abolished the effect of TMZ on Nrf2. Further study revealed that Nrf2 silencing was able to enhance the response of glioma cells to TMZ. Additionally, Nrf2 overexpression overrides the effect of p38 MAPK activation on Temozolomide resistance. In conclusions, we identified a p38 MAPK/Nrf2 signaling as a key molecular network contributing to TMZ resistance of glioma, and provided evidence that suppressing this signaling may be a promising strategy to improve TMZ’s therapeutic efficiency. © 2015, Springer Science+Business Media New York.


Ma L.,Key Laboratory of Marine Drugs | Liu J.,Key Laboratory of Marine Drugs | Zhang X.,Key Laboratory of Marine Drugs | Qi J.,Key Laboratory of Marine Drugs | And 2 more authors.
Medical oncology (Northwood, London, England) | Year: 2015

Temozolomide (TMZ) is an effective agent for clinical glioma treatment, but the innate and acquired resistance of glioma always limits its application. Although some advances have been achieved to elucidate the molecular mechanism underlying TMZ resistance, the role of Nrf2 (a principle regulator of cellular defense against drugs and oxidative stress) has not been well established in the acquisition of this phenotype. Our data showed that TMZ treatment induces the activation of Nrf2 and p38 MAPK signaling in glioma cells, while p38 inhibition abolished the effect of TMZ on Nrf2. Further study revealed that Nrf2 silencing was able to enhance the response of glioma cells to TMZ. Additionally, Nrf2 overexpression overrides the effect of p38 MAPK activation on Temozolomide resistance. In conclusions, we identified a p38 MAPK/Nrf2 signaling as a key molecular network contributing to TMZ resistance of glioma, and provided evidence that suppressing this signaling may be a promising strategy to improve TMZ's therapeutic efficiency.


Wang L.,Key Laboratory of Marine Drugs | Li S.,Key Laboratory of Marine Drugs | Yu W.,Key Laboratory of Marine Drugs | Gong Q.,Key Laboratory of Marine Drugs
Biotechnology Letters | Year: 2015

Using site-finding PCR and degenerate PCR, a gene (designated oalS17) encoding a new oligoalginate lyase was cloned from Shewanella sp. Kz7 and expressed in Escherichia coli. The gene consisted of 2,292 bp with deduced amino acid size of 763 including a putative signal peptide of 44 amino acid residues belonging to polysaccharide lyase (PL) family 17. The recombinant protein was most active at 50 °C and pH 6.2 in 50 mM phosphate buffer. It degraded alginate more efficiently than polyM and polyG block into a monomeric sugar acid, with a specific activity of 32 U mg−1 toward alginate, 24 U mg−1 toward polyM and 5 U mg−1 toward polyG. With the high-level expression and high enzymatic activity, the recombinant oligoalginate lyase OalS17 could be a potential enzyme for further research on alginate saccharification and biofuels production.Purpose of work: Is to report an oligoalginate lyase with high enzymatic activity and high-level expression. © 2014, Springer Science+Business Media Dordrecht.


Zhang X.,Key Laboratory of Marine Drugs | Ma L.,Key Laboratory of Marine Drugs | Qi J.,Key Laboratory of Marine Drugs | Shan H.,Key Laboratory of Marine Drugs | And 2 more authors.
Molecular and Cellular Biochemistry | Year: 2015

Dysregulated MAPK/ERK signaling is implicated in one-third of human tumors and represents an attractive target for the development of anticancer drugs. Similarly, elevated protein O-GlcNAcylation and O-GlcNAc transferase (OGT) are detected in various cancers and serve as attractive novel cancer-specific therapeutic targets. However, the potential connection between them remains unexplored. Here, a positive correlation was found between the activated MAPK/ERK signaling and hyper-O-GlcNAcylation in various cancer types and inhibition of the MAPK/ERK signaling by 10 µM U0126 significantly decreased the expression of OGT and O-GlcNAcylation in H1299, BPH-1 and DU145 cells; then, the pathway analysis of the potential regulators of OGT obtained from the UCSC Genome Browser was done, and ten downstream targets of ERK pathway were uncovered; the following results showed that ELK1, one of the ten targets of ERK pathway, mediated ERK signaling-induced OGT upregulation; finally, the MTT assay and the soft agar assay showed that the inhibition of MAPK/ERK signaling reduced the promotion effect of hyper-O-GlcNAcylation on cancer cell proliferation and anchorage-independent growth. Taken together, our data originally provided evidence for the regulatory mechanism of hyper-O-GlcNAcylation in tumors, which will be helpful for the development of anticancer drugs targeting to hyper-O-GlcNAcylation. This study also provided a new mechanism by which MAPK/ERK signaling-enhanced cancer malignancy. Altogether, the recently discovered oncogenic factor O-GlcNAc was linked to the classical MAPK/ERK signaling which is essential for the maintenance of malignant phenotype of cancers. © 2015, Springer Science+Business Media New York.

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