Immunoreaction at 43 kDa with anti-ubiquitin antibody in breast neoplasms.

Journal Article

Protein ubiquitination has been implicated in ATP-dependent protein turnover and normal cell proliferation. To investigate whether the ubiquitin-mediated system is functionally involved in the cancerous state, we examined changes in protein ubiquitination in 52 surgically resected primary breast tumors. Immunohistochemically, ubiquitin (Ub) was identified in the cytoplasm of cancer cells, which were stained more strongly than adjacent normal ductal epithelium. Corresponding immunoblot analysis of normal and neoplastic regions of human breast showed that the immunoreaction for Ub at about 43 kDa was increased in all of the tumors (100%), regardless of the clinical stage or histologic grade. This protein, which gave a single spot on two-dimensional gel electrophoresis, had partial amino acid sequences which were identical to those of actin family members. Our results suggest that ubiquitination of this 43-kDa protein may be involved in the carcinogenesis or biological characteristics of human breast neoplasms.

Full Text

Duke Authors

Cited Authors

  • Iwaya, K; Nishibori, H; Osada, T; Matsuno, Y; Tsuda, H; Sato, S; Kono, H; Fukutomi, T; Suzuki, M; Torikata, C; Iwamatsu, A; Hirohashi, S

Published Date

  • March 1997

Published In

Volume / Issue

  • 88 / 3

Start / End Page

  • 273 - 280

PubMed ID

  • 9140112

Pubmed Central ID

  • 9140112

International Standard Serial Number (ISSN)

  • 0910-5050

Digital Object Identifier (DOI)

  • 10.1111/j.1349-7006.1997.tb00378.x


  • eng

Conference Location

  • Japan