TY  - JOUR
A1  - Ungern-Sternberg, Saskia N. I. von
A1  - Zernecke, Alma
A1  - Seizer, Peter
T1  - Extracellular matrix metalloproteinase inducer EMMPRIN (CD147) in cardiovascular disease
JF  - International Journal of Molecular Sciences
N2  - The receptor EMMPRIN is involved in the development and progression of cardiovascular diseases and in the pathogenesis of myocardial infarction. There are several binding partners of EMMPRIN mediating the effects of EMMPRIN in cardiovascular diseases. EMMPRIN interaction with most binding partners leads to disease progression by mediating cytokine or chemokine release, the activation of platelets and monocytes, as well as the formation of monocyte-platelet aggregates (MPAs). EMMPRIN is also involved in atherosclerosis by mediating the infiltration of pro-inflammatory cells. There is also evidence that EMMPRIN controls energy metabolism of cells and that EMMPRIN binding partners modulate intracellular glycosylation and trafficking of EMMPRIN towards the cell membrane. In this review, we systematically discuss these multifaceted roles of EMMPRIN and its interaction partners, such as Cyclophilins, in cardiovascular disease.
KW  - cardiovascular disease
KW  - immunoglobulin superfamily
KW  - inflammation
KW  - platelets
KW  - monocyte-platelet aggregates
Y1  - 2018
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-285014
SN  - 1422-0067
VL  - 19
IS  - 2
ER  - 
TY  - JOUR
A1  - Schneider-Schaulies, Jürgen
A1  - von Brunn, A.
A1  - Schachner, M.
T1  - Recombinant peripheral myelin protein P\(_o\) confers both adhesion and neurite outgrowth promoting properties
N2  - To probe into the functional properties of the major peripheral myelin cell surface glycoprotein P 0 , its ability to confer adhesion and neurite outgrowth-promoting properfies was studied in cell culture. Tothis aim, Po was expressed as integral membrane glycoprotein at the surface of CV -1 cells with the help of a recombinant vaccinia virus expression system. Furthermore, the immunoglobulin-like extracellular domain of P0 (P0 -ED) was expressed as soluble profein in a bacterial expression system and used as substrafe coated to plastic dishes or as competitor in cell adhesion and neurite outgrowth-promoting assays. The adhesion of P0 -expressing CV-1 cells to P0 -ED substrafe was specifically inhibitable by polyclonal Po antibodies (54% :t 6% ). In addition, the specific interaction between Po molecules could be reduced ( 49% ± 8%) by adding soluble P0 -ED to the culture medium, demonstrating that the homophilic inter~ction between recombinant Po molecules can be mediated, at least on one partner of interacting molecules, by the unglycosylated Ig-like domain. Substrate-coated p -ED also conferred adhesion and neurite outgrowth ability to dorsal root ganglion neurons with neurites of a mean length of about 150 ,_..m. This neurite outgrowth was specifically inhibitable by soluble P" (74% ± 14%) and P 0 antibodies (65% ± 9% ). These observations indicate that Po is capable of displaying two different types of functional roles in the myelination process of . peripheral nerves: The heterophilic interaction with neurons may be responsible for the recognition between axon and myelinating Schwann cell at the onset of myelination, whereas the homophilic interacton may indicate its roJe in the selfrecognition of the apposing loops of Schwann cell surface membranes during the myelination process and in the mature compact myelin sheath.
KW  - Immunologie
KW  - immunoglobulin superfamily
KW  - peripheral nervous system
KW  - vaccinia virus
KW  - Po
Y1  - 1990
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-54841
ER  -