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Thursday, December 05, 2019 3:24:16 PM
Hold those shares because some will stop at John Springs Stafford....I mean nothing, to delay the inevitable.
PS Targeting truly will turn Big Pharma upside down ...hell, if you have it you have it....and ALL stressed / inflamed / cancerous diseased cell HAS flipped PS
Mr Hancock can feed us whatever he wants....the more resistance and reaction that takes place ....the easier it is to track
Mr Alex Azar (ex Eli Lilly / now DHHS ) to Joseph Grogan ( ex Amgen / Gilead / US advisor now) to others .... this is like HD TV with slow replay ....all are going to see PS Targeting engaged FIRST
Maybe Stan Fleming can make another billion on this play
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Molecular anatomy and pathogenic actions of Helicobacter pylori CagA that underpin gastric carcinogenesis
Atsushi Takahashi-Kanemitsu, Christopher T. Knight &
Masanori Hatakeyama
Dec 5, 2019
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Translocation of CagA into host gastric epithelial cells by H. pylori is achieved via a specific interaction between surface adhesins of the bacteria and receptors for the bacterial component on the host cells. In recent studies, carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) have been identified as a set of protein receptors on epithelial cells that are essential for CagA delivery, which is mediated by specific binding of CEACAMs with the outer membrane adhesin HopQ of the bacteria.50,51,59,60 The CagL protein, a pilus surface component of the T4SS, has also been reported to be an adhesin that mediates CagA delivery by interacting with and thereby activating É?5β1 integrin on target gastric epithelial cells in an arginine-glycine-aspartate (RGD) motif-dependent manner.61 CagL stimulates SRC family kinase (SFK) activity, which in turn phosphorylates the delivered CagA.61 The É?5β1 integrin also interacts with other components of the T4SS, including CagY and CagI, which may cooperatively stabilize the T4SS-host cell interaction.62
To further facilitate the delivery of CagA, H. pylori induces the membrane phospholipid phosphatidylserine (PS) found in the inner membrane leaflet of epithelial cells to be exposed on the outer membrane.63 CagA interacts with the exposed PS to initiate its secretion into the host epithelial cell.63
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https://www.nature.com/articles/s41423-019-0339-5?utm_source=feedburner&utm_medium=feed&utm_campaign=Feed%3A+cmi%2Frss%2Fcurrent+%28Cellular+%26+Molecular+Immunology+-+Issue%29
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Dr. Masanori Hatekeyama
Portrait of Dr. Hatekeyama
Symposium Presentation:
Helicobacter pylori CagA as a bacterial oncoprotein
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Chronic infection with Helicobacter pylori cagA-positive strainsis the strongest risk factor for the development of gastric carcinoma. The cagA gene-encoded CagA is delivered into gastric epithelial cells by the bacterial type IV secretion system, although the underlying mechanisms remain uncertain. Recently, we found that direct contact of H. pylori with epithelial cells induces rapid externalization of phosphatidylserine (PS) to the outer leaflet of the plasma membrane. CagA, which is also exposed on the bacterial surface via type IV secretion, interacts with the membrane-externalized PS. The CagA-PS interaction triggers the entry of CagA into host epithelial cells, which also requires energy-dependent host cell processes distinct from known endocytic pathways. In polarized epithelial cells, delivered CagA is tethered to the inner leaflet of the plasma membrane again through interaction with PS. Thus, host membrane PS plays a key role in delivery and intracellular localization of H. pylori CagA.
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http://www.tmd.ac.jp/TMDU-e/isc/isp2010/abstracts/hatekeyama.html
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