Induction of ER stress protects gastric cancer cells against apoptosis induced by cisplatin and doxorubicin through activation of p38 MAPK |
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Authors: | Feng Ruo Zhai Wen Long Yang Hai Yan Jin Hui Zhang Qin Xian |
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Institution: | aUniversity of Wroc?aw, Department of Chemistry, F. Joliot-Curie 14 Street, 50-383 Wroc?aw, Poland;bUniversity of Wroc?aw, Faculty of Biotechnology, Tamka 2, 50-137 Wroc?aw, Poland;cUniversity of Liverpool, Department of Clinical Infection, Microbiology and Immunology, Institute of Infection and Global Health, Daulby Street, Liverpool L69 3GA, UK |
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Abstract: | Porphyromonas gingivalis acquires heme through an outer-membrane heme transporter HmuR and heme-binding hemophore-like lipoprotein HmuY. Here, we compare binding of iron(III) mesoporphyrin IX (mesoheme) and iron(III) deuteroporphyrin IX (deuteroheme) to HmuY with that of iron(III) protoporphyrin IX (protoheme) and protoporphyrin IX (PPIX) using spectroscopic methods. In contrast to PPIX, mesoheme and deuteroheme enter the HmuY heme cavity and are coordinated by His134 and His166 residues in a fully analogous way to protoheme binding. However, in the case of deuteroheme two forms of HmuY–iron porphyrin complex were observed differing by a 180° rotation of porphyrin about the α-γ-meso-carbon axis. Since the use of porphyrins either as active photosensitizers or in combination with antibiotics may have therapeutic value for controlling bacterial growth in vivo, it is important to compare the binding of heme derivatives to HmuY. |
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Keywords: | Porphyromonas gingivalis HmuY Heme-binding protein Iron Metalloporphyrin |
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