کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5510196 1538854 2017 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
ReviewParaoxonases and infectious diseases
ترجمه فارسی عنوان
بررسی پراکسوناز و بیماری های عفونی
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
چکیده انگلیسی


- The paraoxonases are antioxidant enzymes that degrade lipid peroxides.
- Infectious diseases are associated with oxidative stress and inflammation.
- Serum paraoxonase activity is often decreased in infectious diseases.
- The implication of paraoxonase alterations in infection is an active line of research.

The paraoxonases (PON1, PON2 and PON3) are an enzyme family with a high structural homology. All of them have lactonase activity and degrade lipid peroxides in lipoproteins and cells. As such, they play a role in protection against oxidation and inflammation. Infectious diseases are often associated with oxidative stress and an inflammatory response. Infection and inflammation trigger a cascade of reactions in the host, known as the acute-phase response. This response is associated with dramatic changes in serum proteins and lipoproteins, including a decrease in serum PON1 activity. These alterations have clinical consequences for the infected patient, including an increased risk for cardiovascular diseases, and an impaired protection against the formation of antibiotic-resistant bacterial biofilms. Several studies have investigated the value of serum PON1 measurement as a biomarker of the infection process. Low serum PON1 activities are associated with poor survival in patients with severe sepsis. In addition, preliminary studies suggest that serum PON1 concentration and/or enzyme activity may be useful as markers of acute concomitant infection in patients with an indwelling central venous catheter. Investigating the associations between paraoxonases and infectious diseases is a recent, and productive, line of research.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Clinical Biochemistry - Volume 50, Issues 13–14, September 2017, Pages 804-811
نویسندگان
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