کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1982647 | 1062305 | 2009 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Direct evidence of the cyclooxygenase pathway of prostaglandin synthesis in arthropods: Genetic and biochemical characterization of two crustacean cyclooxygenases
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کلمات کلیدی
SDSPXDHHTCOXRP-HPLCMPO - DFOcyclooxygenase - آنزیم سیکلواکسیژنازEST - استhydroxyeicosatetraenoic acid - اسید هیدروکسی اسیستاترونیکArthropod - بندپایانrapid amplification of cDNA ends - تقویت سریع cDNA به پایان می رسدExpressed sequence tags - تگ های توالی بیان شدهInsect - حشرهCrustacean - خرچنگsodium dodecyl sulphate - سدیم دودسیل سولفاتendoplasmic reticulum - شبکه آندوپلاسمی Race - مسابقهUTR یا untranslated regions - منطقه ترجمه نشدهuntranslated region - منطقه غیر ترجمهmyeloperoxidase - میلوپراکسیداز HETE - هفتهPeroxidasin - پراکسیدازینProstaglandin H synthase - پروستاگلاندین H سنتازprostaglandin - پروستاگلاندینهاPeroxinectin - پروکسینکتینGene - ژن reversed-phase high pressure liquid chromatography - کروماتوگرافی مایع با فشار فاز معکوس
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش حشره شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Direct evidence of the cyclooxygenase pathway of prostaglandin synthesis in arthropods: Genetic and biochemical characterization of two crustacean cyclooxygenases Direct evidence of the cyclooxygenase pathway of prostaglandin synthesis in arthropods: Genetic and biochemical characterization of two crustacean cyclooxygenases](/preview/png/1982647.png)
چکیده انگلیسی
Prostaglandins, well-known lipid mediators in vertebrate animals, have also shown to play certain regulatory roles in insects and other arthropods acting on reproduction, immune system and ion transport. However, knowledge of their biosynthetic pathways in arthropods is lacking. In the present study, we report the cloning and expression of cyclooxygenase (COX) from amphipod crustaceans Gammarus spp and Caprella spp. The amphipod COX proteins contain key residues shown to be important for cyclooxygenase and peroxidase activities. Differently from all other known cyclooxygenases the N-terminal signal sequence of amphipod enzymes is not cleaved during protein expression in mammalian cells. The C-terminus of amphipod COX is shorter than that of mammalian isoforms and lacks the KDEL(STEL)-type endoplasmic reticulum retention/retrieval signal. Despite that, amphipod COX proteins are N-glycosylated and locate similarly to the vertebrate COX on the endoplasmic reticulum and nuclear envelope. Both amphipod COX mRNAs encode functional cyclooxygenases that catalyze the transformation of arachidonic acid into prostaglandins. Using bioinformatic analysis we identified a COX-like gene from the human body louse Pediculus humanus corporis genome that encodes a protein with about 30% sequence identity with human COX-1 and COX-2. Although the COX gene is known to be absent from genomes of Drosophila sp., Aedes aegypti, Bombyx mori, and other insects, our studies establish the existence of the COX gene in certain lineages within the insect world.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Insect Biochemistry and Molecular Biology - Volume 39, Issue 12, December 2009, Pages 851-860
Journal: Insect Biochemistry and Molecular Biology - Volume 39, Issue 12, December 2009, Pages 851-860
نویسندگان
Külliki Varvas, Reet Kurg, Kristella Hansen, Reet Järving, Ivar Järving, Karin Valmsen, Helike Lõhelaid, Nigulas Samel,