(Download) "Stathmin Binds Heat-Shock-Protein 70." by Proceedings of the Indiana Academy of Science ~ Book PDF Kindle ePub Free
eBook details
- Title: Stathmin Binds Heat-Shock-Protein 70.
- Author : Proceedings of the Indiana Academy of Science
- Release Date : January 29, 2003
- Genre: Engineering,Books,Professional & Technical,
- Pages : * pages
- Size : 166 KB
Description
ABSTRACT. Stathmin is a cytosolic protein postulated to act as an intracellular relay in cell signaling. It interacts via coiled-coil motifs with several proteins, including BiP/Grp78 and Hsc70, two members of the heat-shock-70 (Hsp70) family of proteins. In the current study, a glutathione-S-transferase (GST)stathmin fusion protein was used to determine whether stathmin also binds to Hsp70, a third member of the Hsp70 family. Stathmin-binding proteins were examined in Nb2 cells, a rat lymphoma, and in PC12 cells, a rat pheochromocytoma. Prolactin (PRL)-stimulated Nb2 cells were used as the primary source of cytosol and membrane proteins because it has been demonstrated that PRL induces expression of Hsp70 in these cells. PC12 cells were used because they are of neuronal origin, and stathmin appears to play important roles in neural signaling. The results showed that stathmin binds multiple Nb2- and PC12-cell proteins. Immunostaining confirmed that stathmin binds to tubulin and showed for the first time that stathmin binds to Hsp70. Keywords: Stathmin, Nh2, PC12, Hsp70, glutathione-S-transferase