کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8304068 | 1537960 | 2009 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Differential regulation of human tyrosine hydroxylase isoforms 1 and 2 in situ: Isoform 2 is not phosphorylated at Ser35
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کلمات کلیدی
DMEMERKCaMKIIBH4tetrahydrobiopterinHTHDulbecco's modified Eagle Medium - Eagle Medium اصلاح شده DulbeccoSER - برای بودنtyrosine hydroxylase - تیروزین هیدروکسیلازSerine - سرینSH-SY5Y cell - سلول SH-SY5YPhosphorylation - فسفریلاسیونcalcium/calmodulin-dependent protein kinase II - پروتئین کیناز II وابسته به کلسیم / کالودولینExtracellular signal-regulated protein kinase - پروتئین کیناز کنترل شده سیگنال غیر سلولی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The major human tyrosine hydroxylase isoforms (hTH1 and 2) differ in their ability to be phosphorylated in vitro. hTH1 is phosphorylated at Ser31 by extracellular signal-regulated kinase (ERK). This kinase is not capable of phosphorylating hTH2 at Ser35 (the residue that corresponds to Ser31 in hTH1). We have stably transfected SH-SY5Y cells with hTH1 or hTH2 to determine if hTH2 can be phosphorylated at Ser35 in situ. Forskolin increased the phosphorylation of Ser40 in hTH1 and Ser44 in hTH2. Muscarine increased the phosphorylation of both Ser19 and Ser40/44 in both hTH1 and hTH2. EGF increased the phosphorylation of Ser31 in hTH1. Phosphorylation of Ser35 in hTH2 was not detected under any of the conditions tested. Inhibition of ERK by UO126 decreased the phosphorylation of Ser31 and this lead to a 50% decrease in the basal level of phosphorylation of Ser40 in hTH1. The basal level of Ser44 phosphorylation in hTH2 was not altered by treatment with UO126. Therefore, phosphorylation of Ser31 contributes to the phosphorylation of Ser40 in hTH1 in situ; however, this effect is absent in hTH2. This represents a major difference between the two human TH isoforms, and has implications for the regulation of catecholamine synthesis in vivo.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1793, Issue 12, December 2009, Pages 1860-1867
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1793, Issue 12, December 2009, Pages 1860-1867
نویسندگان
Sarah L. Gordon, Larisa Bobrovskaya, Peter R. Dunkley, Phillip W. Dickson,