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Articles by He Wang
Total Records ( 2 ) for He Wang
  Zhiming Shu , Akhtar Hussain Shar , Mohamed Shahen , He Wang , Mahmoud Alagawany , Mohamed E. Abd El-Hack , Shahmir Ali Kalhoro , Muhammad Rashid and Piar Ali Shar
  Globally the cardiovascular disease (CVDs) and coronary heart disease (CHD) are main cause of death. Ginkgo biloba is one of the oldest plants in the world, originating in China, science is known as the "living fossil". Ginkgo biloba leaves extract (GBLE) is a bioactive substance extracted from the Ginkgo biloba, the main active ingredients of Ginkgo flavonoids and ginkgolide compound, three or four, one of the most important Ginkgo biloba leaves extract is widely used as a drug or food additive in more than 130 countries. Thousands of years ago Asian and other region was use the traditional Chinese medicine (TCM), they verified some effective disorders. The medicinal uses of Ginkgo biloba have been widely used for various disease including cardiovascular disease and coronary heart disease. The properties of Ginkgo are mentioned here for example; improved blood flow, antioxidant, strengthens blood vessels, anti-inflammatory, relaxes the lungs, vasodilator and circulatory system tonic. Ginkgo biloba leaves extract also appears to have an anti-inflammatory impact that may make it useful in the future for situations like organ transplants and multiple sclerosis. However, due to the multi component of the herb, up to now the molecular mechanisms of action and signaling pathways leading to the therapeutic effects of GBLE remain, still, poorly understood.
  Ke Wang , Yazhou Zhang , Xiaofeng Li , Lijun Chen , He Wang , Jianguo Wu , Jie Zheng and Dianqing Wu
  Wnt signaling is involved in a wide range of developmental, physiological, and pathophysiological processes and is negatively regulated by Dickkopf1 (Dkk1). Dkk1 has been shown to bind to two transmembrane proteins, the low density lipoprotein receptor-related proteins (LRP) 5/6 and Kremen. Here, we show that Dkk1 residues Arg197, Ser198, and Lys232 are specifically involved in its binding to Kremen rather than to LRP6. These residues are localized at a surface that is at the opposite side of the LRP6-binding surface based on a three-dimensional structure of Dkk1 deduced from that of Dkk2. We were surprised to find that the Dkk1 mutants carrying a mutation at Arg197, Ser198, or Lys232, the key Kremen-binding residues, could antagonize Wnt signaling as well as the wild-type Dkk1. These mutations only affected their ability to antagonize Wnt signaling when both LRP6 and Kremen were coexpressed. These results suggest that Kremen may not be essential for Dkk1-mediated Wnt antagonism and that Kremen may only play a role when cells express a high level of LRP5/6.
 
 
 
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