این سایت در حال حاضر پشتیبانی نمی شود و امکان دارد داده های نشریات بروز نباشند
Iranian Biomedical Journal، جلد ۲، شماره ۱، صفحات ۹-۱۳
عنوان فارسی Effects of Antiproliferative Protein (APP) on Modulation of Cytosolic Protein Phosphorylation of Prostatic Carcinoma Cell Line LNCaP
چکیده فارسی مقاله Antiproliferative protein (APP) isolated from conditioned media of two androgen-independent prostatic carcinoma cell lines, PC3 and Du-145 was shown to inhibit selectively cell proliferation of androgen-dependent prostate cancer cell line LNCaP in a dose dependent manner. This protein was further purified with HPLC using hydrophobic interaction column (phenyl 5PW) and was used to study the modulation of protein phosphorylation of LNCaP cells. The data indicated that antiprolif-erative protein could partially change the cytosolic protein phosphorylation. When compared with control LNCaP cells, in APP-treated cells 4 new proteins (88, 46, 30 and 18 kDa) were phosphory-lated, while a 72 kDa phosphoprotein was de-phosphorylated. The same results were obtained when two types of protein kinase activators were used. Protein kinase activators showed that the above changes of protein phosphorylation are not due to the protein kinase C or DNA protein kinase activ‌ity. These data may indicate the inhibition of LNCaP cell's proliferation by APP may be is due to the modulation of protein kinases and as a result due to interference on second messenger pathway.
کلیدواژه‌های فارسی مقاله
عنوان انگلیسی Effects of Antiproliferative Protein (APP) on Modulation of Cytosolic Protein Phosphorylation of Prostatic Carcinoma Cell Line LNCaP
چکیده انگلیسی مقاله Antiproliferative protein (APP) isolated from conditioned media of two androgen-independent prostatic carcinoma cell lines, PC3 and Du-145 was shown to inhibit selectively cell proliferation of androgen-dependent prostate cancer cell line LNCaP in a dose dependent manner. This protein was further purified with HPLC using hydrophobic interaction column (phenyl 5PW) and was used to study the modulation of protein phosphorylation of LNCaP cells. The data indicated that antiprolif-erative protein could partially change the cytosolic protein phosphorylation. When compared with control LNCaP cells, in APP-treated cells 4 new proteins (88, 46, 30 and 18 kDa) were phosphory-lated, while a 72 kDa phosphoprotein was de-phosphorylated. The same results were obtained when two types of protein kinase activators were used. Protein kinase activators showed that the above changes of protein phosphorylation are not due to the protein kinase C or DNA protein kinase activ‌ity. These data may indicate the inhibition of LNCaP cell's proliferation by APP may be is due to the modulation of protein kinases and as a result due to interference on second messenger pathway.
کلیدواژه‌های انگلیسی مقاله
نویسندگان مقاله محسن ابولحسنی | mohsen abolhassani


نشانی اینترنتی http://ibj.pasteur.ac.ir/browse.php?a_code=A-10-1-458&slc_lang=en&sid=en
فایل مقاله فایلی برای مقاله ذخیره نشده است
کد مقاله (doi)
زبان مقاله منتشر شده fa
موضوعات مقاله منتشر شده
نوع مقاله منتشر شده مقاله کامل
برگشت به: صفحه اول پایگاه   |   نسخه مرتبط   |   نشریه مرتبط   |   فهرست نشریات