Another piece of the complex puzzle of how inflammation is involved in heart attacks and strokes has been discovered by researchers at the University of California, San Diego (UCSD) School of Medicine.
Mi-Kyung Chang, M.D., first author
Joseph Witztum, M.D., and Mi-Kyung Chang, M.D.
Their findings demonstrate that C-reactive protein (CRP) binds to oxidized low density lipoprotein (LDL), implicating the interaction of CRP and oxidized LDL as a potential trigger for the cascade of events leading to atherosclerosis. This form of artery disease is characterized by the buildup of fatty deposits and chronic inflammation along the artery wall, eventually leading to heart attack.
Published in the online edition of Proceedings of the National Academy of Sciences (PNAS) the week of Sept. 9, 2002, the study by the UCSD researchers pinpoints how CRP attaches itself to oxidized LDL, the so-called "bad cholesterol" that accumulates in the artery wall and generates atherosclerotic plaques. LDL is the major cholesterol carrying particles. When they enter the artery wall from the circulation, they are believed to be modified by oxidation. It is this "oxidized LDL" that is thought to be the culprit leading to inflammation and cholesterol accumulation.
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Hamburg and the European Molecular Biology Laboratory (EMBL) outstation in the city have developed a new method to watch biomolecules at work. This method dramatically simplifies starting enzymatic reactions by mixing a cocktail of small amounts of liquids with protein crystals. Determination of the protein structures at different times after mixing can be assembled into a time-lapse sequence that shows the molecular foundations of biology.
The functions of biomolecules are determined by their motions and structural changes. Yet it is a formidable challenge to understand these dynamic motions.
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Potsdam (both in Germany) and the University of Toronto (Canada) have pieced together a detailed time-lapse movie revealing all the major steps during the catalytic cycle of an enzyme. Surprisingly, the communication between the protein units is accomplished via a water-network akin to a string telephone. This communication is aligned with a ‘breathing’ motion, that is the expansion and contraction of the protein.
This time-lapse sequence of structures reveals dynamic motions as a fundamental element in the molecular foundations of biology.
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