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Identification of 12-lipoxygenase interaction with cellular proteins by yeast two-hybrid screening.

The platelet isoform of 12-lipoxygenase (12-LOX) is expressed in a variety of human tumors. 12-LOX metabolizes arachidonic acid to 12(S)-hydroxyeicosateraenoic acid (12(S)-HETE), which induces a number of cellular responses associated with tumor progression and metastasis. Little is known about 12-LOX regulation and no direct regulators of 12-LOX activity have been identified. To identify potential regulators of 12-LOX, we isolated cDNAs encoding 12-LOX interacting proteins using the yeast two-hybrid system. We screened a yeast two-hybrid interaction library from human epidermoid carcinoma A431 cells and identified four cellular proteins that interact specifically with 12-LOX. We identified type II keratin 5, lamin A, the cytoplasmic domain of integrin beta4 subunit and a phosphoprotein C8FW as 12-LOX interacting proteins. Here, we demonstrated that keratin 5, a 58 kD protein required for formation of 8 nm intermediate filaments, binds to 12-LOX in human tumor cells and may contribute to the regulated trafficking of 12-LOX. We also showed that lamin A binds 12-LOX in human tumor cells. These proteins provide the first candidate regulators of 12-LOX.

Pubmed ID: 10727209


  • Tang K
  • Finley RL
  • Nie D
  • Honn KV



Publication Data

March 28, 2000

Associated Grants

  • Agency: NCI NIH HHS, Id: CA-29997
  • Agency: NHGRI NIH HHS, Id: R29HG01536

Mesh Terms

  • Antigens, CD
  • Arachidonate 12-Lipoxygenase
  • Blood Platelets
  • Cloning, Molecular
  • Gene Library
  • Humans
  • Integrin beta4
  • Integrins
  • Isoenzymes
  • Keratins
  • Lamin Type A
  • Lamins
  • Neoplasm Proteins
  • Nuclear Proteins
  • Phosphoproteins
  • Saccharomyces cerevisiae
  • Tumor Cells, Cultured
  • Two-Hybrid System Techniques