Bo Zhang, Yujie Zhang, Ziwei Liao, Ting Jiang, Jingjing Zhao, Yanyan Tuo, Xiaojian She, Shun Shen, Jun Chen, Qizhi Zhang, Xinguo Jiang, Yu Hu, Zhiqing Pang: UPA-sensitive ACPP-conjugated nanoparticles for multi-targeting therapy of brain glioma. Biomaterials Volume 36, January 2015, Pages 98-109.
Prostatic acid phosphatase (PAP, or ACPP), also known as prostatic specific acid phosphatase (PSAP), is an enzyme produced by the prostate. As a non-specific phosphomonoesterase, Prostatic acid phosphatase is synthesized and secreted into seminal plasma under androgenic control. The enzyme is a dimer of molecular weight around 100 kDa. Prostatic Acid Phosphatase (ACPP) catalyzes the hydrolysis of a variety of phosphate monoesters, including phosphorylated proteins. The activity optimum of ACPP is in the pH range of 4-6, and the activity is inhibited by L(+)-tartrate. ACPP expression levels are highest in the prostate, with much lower expression in most other tissues. ACPP is a type I integral membrane protein of the plasma membrane and lysosomes, and a secreted form also exists. The concentration of ACPP is elevated in the circulation of prostate cancer patients, making the enzyme a marker for the progression of prostate cancer. Cellular ACPP has been shown to be a protein tyrosine phosphatase. Protein substrates include the epidermal growth factor receptor and HER-2. Cellular ACPP is considered to function as a tumor suppressor.
1μg (R: reducing condition, N: non-reducing condition).
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