Dr. Heidi Noels and Dr. Yvonne Döring receive the W.H. Hauss Award from the DGAF
19-21 April 2018
Dr. Heidi Noels from the Institute for Molecular Cardiovascular Research at RWTH Aachen University together with Dr. Yvonne Döring from the Institute for Prophylaxis and Epidemiology of Circulatory Diseases at LMU Munich together received the DGAF W.H. Hauss Award 2018 from the German Society for Atherosclerosis Research (DGAF) during the 32nd Annual Meeting of the DGAF in Rauischholzhausen, Germany. They were awarded for their publication "Vascular CXCR4 Limits Atherosclerosis by Maintaining Arterial Integrity: Evidence From Mouse and Human Studies." (Circulation. 2017; 136: 388-403). In this work it could be shown that vascular CXCR4 has an atheroprotective function by maintaining the arterial integrity and preserving the endothelial barrier function. In addition, CXCR4 stabilizes a contractile smooth muscle cell phenotype. Targeted enhancement of these CXCR4-mediated protective functions could open up novel therapeutic options in the treatment of atherosclerosis.
The award was sponsored by a long-standing active member of the DGAF, Prof. Dr. Winfried März.
Project area Z
Administrative project
Robert Werner Mertens
MD student
University Hospital RWTH Aachen
Department of Internal Medicine
Project: The role of incretin hormone GLP-2 in septic cardiomyopathy
PI: Michael Lehrke
Robert Werner Mertens
MD student
University Hospital RWTH Aachen
Department of Internal Medicine
Project: The role of incretin hormone GLP-2 in septic cardiomyopathy
PI: Michael Lehrke
Consortium
Mechanisms of Cardiovascular Complications
in Chronic Kidney Disease
The SFB/TRR219 is supported by the German Research Foundation (DFG)
Project-ID 322900939
PhD MD TRR219-associated students
Sina Köppert
PhD student
University Hospital RWTH Aachen
Institute for Biomedical Engineering - Biointerface Laboratory
Project title: Cellular Response and Clearance Mechanisms Triggered by Protein-Mineral Complexes
PI: Willi Jahnen-Dechent
The liver-derived plasma protein fetuin-A is known as a systemic inhibitor of ectopic calcification. Fetuin-A stabilizes saturated mineral solutions initially as ion clusters to form calciprotein monomers (CPM) and then as larger multimeric consolidations containing amorphous calcium phosphate referred to as primary calciprotein particles (CPP). Time-, temperature-, pH-, and mineral saturation-dependently, primary CPP spontaneously convert into secondary CPP which are larger, oblongated, more crystalline, and less soluble. CPM and CPP mediate excess mineral stabilization, transport and clearance from the circulation and thus, prevent calcium phosphate deposition and subsequent calcification. We study CPM and CPP clearance mechanisms and the response of cells involved in these mechanisms.