Interaction of BCR-ABL with the retinoblastoma protein in Philadelphia chromosome-positive cell lines.

Abstract

The tyrosine kinase activity of BCR-ABL fusion proteins plays an important role in the pathogenesis of leukemia that is for the Philadelphia chromosome (Ph1). Because nuclear c-ABL is regulated during the cell cycle through a specific interaction with the retinoblastoma protein (pRB), the possible interaction of BCR-ABL with pRB in Ph1-positive cell lines was investigated. P145 c-ABL as well as P190 and P210 BCR-ABL proteins interacted with pRB. Furthermore, c-ABL and BCR-ABL associated with both phosphorylated and nonphosphorylated forms of pRB. These findings suggest that BCR-ABL interferes with pRB function and thereby regulates cell growth.

• Authors: T Miyamura, J Nishimura, Y Yufu, H Nawata
• Journal: International journal of hematology (Int J Hematol) Vol. 65 Issue 2 Pg. 115-21 (Feb 1997) ISSN: 0925-5710 [Print] Japan
• PMID: 9071815 (Publication Type: Journal Article)

Chemical References

• Retinoblastoma Protein
• Fusion Proteins, bcr-abl

Topics

• Animals
• Fusion Proteins, bcr-abl (metabolism)
• Humans
• Leukemia, Myelogenous, Chronic, BCR-ABL Positive (metabolism)
• Mice
• Phosphorylation
• Protein Binding
• Retinoblastoma Protein (metabolism)
• Signal Transduction
• Tumor Cells, Cultured