کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10771673 | 1050843 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Shedding of membrane epithin is blocked without LDLRA4 and its protease activation site
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Shedding of membrane epithin is blocked without LDLRA4 and its protease activation site Shedding of membrane epithin is blocked without LDLRA4 and its protease activation site](/preview/png/10771673.png)
چکیده انگلیسی
Epithin, a mouse type II transmembrane serine protease, is processed at Gly149 and released from the membrane. Here, we report the identification of an epithin isoform, epithin(Î), containing a 66 amino acid deletion from the full-length epithin, which is missing the 4th LDLRA domain and the protease activation sequence. This truncated isoform showed the same characteristic N-terminal processing at Gly149 as the full-length form, however, no protease activity was detected. The N-terminal processed epithin(Î) short form (Epi(Î)-S) was not released into the medium under conditions in which the processed epithin short form (Epi-S) is released. This type of epithin shedding was also prevented when serine protease inhibitors were added to cells expressing the full-length form. These results strongly suggest that the serine protease activity is involved in the shedding process. The presence of epithin(Î) message was detected in multiple tissues and its significance is discussed.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 327, Issue 1, 4 February 2005, Pages 328-334
Journal: Biochemical and Biophysical Research Communications - Volume 327, Issue 1, 4 February 2005, Pages 328-334
نویسندگان
Eun-Gyung Cho, Ronald H. Schwartz, Moon G. Kim,