دورية أكاديمية

Activity of matrix metallo proteinases (MMPs) and the tissue inhibitorof MMP (TIMP)-1 in electromagnetic field-exposed THP-1 cells.

التفاصيل البيبلوغرافية
العنوان: Activity of matrix metallo proteinases (MMPs) and the tissue inhibitorof MMP (TIMP)-1 in electromagnetic field-exposed THP-1 cells.
المؤلفون: PATRUNO, ANTONIA, PESCE, MIRKO, MARRONE, Alessandro, SPERANZA, Lorenza, GRILLI, Alfredo, DE LUTIIS, Maria Anna, FELACO, Mario, REALE, Marcella
المساهمون: Patruno, Antonia, Pesce, Mirko, Marrone, Alessandro, Speranza, Lorenza, Grilli, Alfredo, DE LUTIIS, Maria Anna, Felaco, Mario, Reale, Marcella
سنة النشر: 2012
المجموعة: ARUd'A - Archivio Istituzionale della ricerca dell'università Chieti-Pescara (IRIS)
مصطلحات موضوعية: copper zinc superoxide dismutase, inducible nitric oxide synthase, matrix metalloproteinase, nitrogen, reactive nitrogen species, tissue inhibitor of metalloproteinase 1
الوصف: Matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs (TIMPs) are the main determinants of tissue remodeling in both physiological and pathological processes. Metabolic processes, which generate oxidants and antioxidants can be influenced by environmental factors such as electromagnetic fields (EMF). We analyzed the effects of EMF on the activity and expression of MMPs in THP-1 cells. Cells were exposed to a 50 Hz, 1 mT EMF for 24 h and incubated with or without LPS. Our data indicate that THP-1 cells exposed to EMF causes a reduction of anti-oxidant enzyme activity and an enhancement of nitrogen intermediates involving the iNOS pathway. We then analyzed the role of nitration of TIMP-1 in increasing the activity of MMPs in EMF exposed cells. Molecular modeling tools were employed to identify the most plausible sites in the active conformation of TIMP-1; at least two protein sites, Y120 and Y38 and/ or Y72 were identified. Reactive nitrogen species (RNS) may affect protein targets, such as TIMP-1, which are crucial for the regulation of MMP activities by oxidation of sulfydryl groups, or by nitration of tyrosine residues. These results may suggest a pathway connecting an imbalance of MMPs and their cognate inhibitor TIMP-1.
نوع الوثيقة: article in journal/newspaper
وصف الملف: ELETTRONICO
اللغة: English
العلاقة: info:eu-repo/semantics/altIdentifier/pmid/21928345; info:eu-repo/semantics/altIdentifier/wos/WOS:000300719600049; volume:227; issue:6; firstpage:2767; lastpage:2774; numberofpages:8; journal:JOURNAL OF CELLULAR PHYSIOLOGY; http://hdl.handle.net/11564/206569Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84857499376; http://www.ncbi.nlm.nih.gov/pubmed/21928345Test
DOI: 10.1002/jcp.23024
الإتاحة: https://doi.org/10.1002/jcp.23024Test
http://hdl.handle.net/11564/206569Test
http://www.ncbi.nlm.nih.gov/pubmed/21928345Test
رقم الانضمام: edsbas.1AAA4741
قاعدة البيانات: BASE