Specific cytosol binding proteins for 25(OH)D3 and 1.25(OH)2D3 in human breast cancers.

نویسندگان

  • M Nakata
  • S Tsuboi
  • M Takenaka
  • Y Konishi
  • R Kawashima
  • M Tomita
  • T Nakagawa
  • N Iwamura
  • T Fujita
چکیده

Binding proteins for 1.25 (OH) 2D3 were investigated in thirty breast cancers. Human breast cancer was shown to contain specific, high affinity cytosol binding proteins for 1.25 (OH) 2D3 and 25 (OH) D3. The binding protein for 1.25 (OH) 2D3 sedimented at 3.7 S and the binding protein for 25 (OH) D3 at about 6.0 S on sucrose density gradient analysis containing 0.3 M KCl and 1 mM dithiothreitol in buffer. Kd for 1.25 (OH) 2D3 were from 0.1 x 10(-11) M to 7.1 x 10(-11) M measured by Scatchard plots. Competition binding studies indicated that the relative specificity of the binding protein for 1.25 (OH) 2D3 much greater than 25 (OH) D3 greater than 1 alpha (OH) D3, 24,25 (OH)2D3 greater than D3 much greater than Estradiol-17 beta. 1.25 (OH) 2D3 receptor-positive was detected in twenty-eight out of thirty breast cancers.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Inhibition of Human Cancer Cell Growth by 1,25-Dihydroxyvitamin D3 Metabolites1

Specific high-affinity 1,25-dihydroxyvitamin D3 [1,25-{OH)2D3] receptors, which can undergo hormone-dependent activation and nuclear localization, have been demonstrated in a wide variety of established human cancer cell lines and surgically obtained human cancer tissues. 1,25-(OH)2D3 has been reported by some workers to stimulate cancer cell replication at low "physiological" concentrations an...

متن کامل

Inhibition of human cancer cell growth by 1,25-dihydroxyvitamin D3 metabolites.

Specific high-affinity 1,25-dihydroxyvitamin D3 [1,25-(OH)2D3] receptors, which can undergo hormone-dependent activation and nuclear localization, have been demonstrated in a wide variety of established human cancer cell lines and surgically obtained human cancer tissues. 1,25-(OH)2D3 has been reported by some workers to stimulate cancer cell replication at low "physiological" concentrations an...

متن کامل

Cytoplasmic and nuclear binding components for 1alpha25-dihydroxyvitamin D3 in chick parathyroid glands.

Specific binding of 1 alpha,25-dihydroxyvitamin D3 [1alpha,25-(OH)2D3] to macromolecular components in the cytoplasm and nucleus is demonstrated in parathyroid glands of vitamin-D-deficient chicks. The interaction of 1alpha,25-(OH)2D3 with the cytoplasmic binding component is of high affinity (Kd = 3.2 X 10(-10) M) and high specificity [1alpha,25-(OH)2D3 greater than 25-hydroxyvitamin D3 greate...

متن کامل

1,25-dihydroxyvitamin D3 receptors and hormonal responses in cloned human skeletal muscle cells.

Although skeletal muscle is a major calcium-regulated organ, there remains uncertainty about whether muscle is a target organ for the action of 1,25-dihydroxyvitamin D3 [1,25-(OH)2D3]. In this study we examine pure populations of clonally derived human muscle cells for the presence of 1,25-(OH)2D3 receptors and direct responses to the hormone. All of the clones tested exhibited specific [3H]1,2...

متن کامل

Extrarenal vitamin D hydroxylase expression and activity in normal and malignant cells: modification of expression by epigenetic mechanisms and dietary substances.

Epidemiological studies have demonstrated an inverse correlation between risk of several cancers, sun exposure, and serum levels of 25-hydroxyvitamin D3 (25-OH-D3). 1,2 While 25-OH-D3 is present in human serum at nanomolar concentrations, levels of the active vitamin D metabolite 1,25(OH)2D3 are in the picomolar range, i.e. a thousand-fold lower. These low 1,25(OH)2D3 levels are strictly regula...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Endocrinologia japonica

دوره 28 6  شماره 

صفحات  -

تاریخ انتشار 1981