R
Regina M. Krohn
Researcher at University of Calgary
Publications - 20
Citations - 2349
Regina M. Krohn is an academic researcher from University of Calgary. The author has contributed to research in topics: Macrophage migration inhibitory factor & CXCR4. The author has an hindex of 12, co-authored 20 publications receiving 2121 citations. Previous affiliations of Regina M. Krohn include RWTH Aachen University.
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Journal ArticleDOI
MIF is a noncognate ligand of CXC chemokine receptors in inflammatory and atherogenic cell recruitment
Jürgen Bernhagen,Regina M. Krohn,Hongqi Lue,Julia L. Gregory,Alma Zernecke,Rory R. Koenen,Manfred Dewor,Ivan T. Georgiev,Andreas Schober,Lin Leng,Teake Kooistra,Gunter Fingerle-Rowson,Pietro Ghezzi,Robert Kleemann,Shaun R. McColl,Richard Bucala,Michael J. Hickey,Christian Weber +17 more
TL;DR: Targeting MIF in individuals with manifest atherosclerosis can potentially be used to treat this condition and displays chemokine-like functions and acts as a major regulator of inflammatory cell recruitment and atherogenesis.
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Protective Role of CXC Receptor 4/CXC Ligand 12 Unveils the Importance of Neutrophils in Atherosclerosis
Alma Zernecke,Ilze Bot,Yassin Djalali-Talab,Erdenechimeg Shagdarsuren,Kiril Bidzhekov,Svenja Meiler,Regina M. Krohn,Andreas Schober,Markus Sperandio,Oliver Soehnlein,Jörg Bornemann,Frank Tacke,Erik A.L. Biessen,Christian Weber +13 more
TL;DR: It is shown that interference with Cxcl12/Cxcr4 by a small-molecule antagonist, genetic CxCr4 deficiency, or lentiviral transduction with CXcr4 degrakine in bone marrow chimeras aggravated diet-induced atherosclerosis in apolipoprotein E-deficient or LDL receptor–deficient mice.
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A functional heteromeric MIF receptor formed by CD74 and CXCR4.
Verena Schwartz,Hongqi Lue,Sandra Kraemer,Joanna Korbiel,Regina M. Krohn,Kim Ohl,Richard Bucala,Christian Weber,Jürgen Bernhagen +8 more
TL;DR: It is shown that CXCR4 and CD74 colocalize by fluorescence microscopy and are related to each other by the H2O2/O2 “spiking” signal.
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NADPH oxidase activity controls phagosomal proteolysis in macrophages through modulation of the lumenal redox environment of phagosomes
TL;DR: This work found that NADPH oxidase (NOX2) negatively regulates levels of proteolysis within the maturing phagosome of macrophages, and further implicates the microbicidal effector NOX2 as a global modulator of phagosomal physiologies, particularly of those pertinent to antigen processing.
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Alternative activation of macrophages by IL-4 enhances the proteolytic capacity of their phagosomes through synergistic mechanisms
Dale R. Balce,Baoquan Li,Baoquan Li,Euan R.O. Allan,Joanna M. Rybicka,Regina M. Krohn,Robin M. Yates,Robin M. Yates +7 more
TL;DR: Together, changes initiated by IL-4 act synergistically to rapidly and dramatically enhance the macrophage's ability to degrade phagocytosed protein, which, it is reasoned, better equips this cell for its roles in wound repair and tissue remodeling.