Scholarlink

Abstract <p>α-<i>N</i>-Acetylgalactosaminidase (α-NaGalase) is produced by all cancer tumors and accumulates in the plasma of patients, which leads to the suppression of macrophage activity in patients with advanced cancer. Avarol (sesquiterpene hydroquinone) from <i>Dysidea</i> sp. and Damiron A (alkaloid) from <i>Zyzzya fuliginosa</i> were shown for the first time to be nonessential K-type activators of α-NaGalase isolated from the biomass of human colorectal cancer cells HT-29 and DLD-1, respectively. Bioinformatic analysis of the structures of healthy lysosomal α-NaGalase and similar enzymes, the genes of which were found in the genomes of human colorectal cancer cell lines of various lines with known point mutations, showed that amino acid substitutions are located in the loop structure on the outer surface of the enzyme. The active center region does not contain mutations. According to molecular docking results, the activators bind near the catalytic site of the enzyme and affect the microenvironment of the catalytic residue Asp 217, probably increasing its reactivity.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Activating Effect of Avarol and Damiron A from Sea Sponges on α-N-Acetylgalactosaminidase from Human Colorectal Cancer Cell Cultures

  • 期刊论文

  • 发表日期：

    2026年3月1日

查看全文
  • I. Yu. Bakunina,
  • N. K. Utkina,
  • G. N. Likhatskaya,
  • S. P. Ermakova

摘要

Abstract

α-N-Acetylgalactosaminidase (α-NaGalase) is produced by all cancer tumors and accumulates in the plasma of patients, which leads to the suppression of macrophage activity in patients with advanced cancer. Avarol (sesquiterpene hydroquinone) from Dysidea sp. and Damiron A (alkaloid) from Zyzzya fuliginosa were shown for the first time to be nonessential K-type activators of α-NaGalase isolated from the biomass of human colorectal cancer cells HT-29 and DLD-1, respectively. Bioinformatic analysis of the structures of healthy lysosomal α-NaGalase and similar enzymes, the genes of which were found in the genomes of human colorectal cancer cell lines of various lines with known point mutations, showed that amino acid substitutions are located in the loop structure on the outer surface of the enzyme. The active center region does not contain mutations. According to molecular docking results, the activators bind near the catalytic site of the enzyme and affect the microenvironment of the catalytic residue Asp 217, probably increasing its reactivity.