Suresh S. Ramalingam, MD, from the Winship Cancer Institute of Emory University, discusses the role of heat shock proteins in normal cells and their potential role in treating cancer.
Suresh S. Ramalingam, MD, a professor of medical oncology at the Winship Cancer Institute of Emory University in Atlanta, Georgia, discusses the role of heat shock proteins in normal cells and their potential role in treating cancer.
Heat shock proteins are often labeled chaperones because newly formed proteins require their assistance to become structurally active and perform their biologic function, Ramalingam notes. However, blocking this process by the inhibition of heat shock protein (Hsp) 90 with an agent like ganetespib renders these new proteins inactive.
In lung cancer, proteins such as EGFR and ALK, which stimulate tumor growth, depend on Hsp90 for activation. Altogether, Ramalingam notes, there are over 200 known proteins associated with Hsp90, many of which are important to the development of lung cancer. The promise with ganetespib is that by inhibiting Hsp90, multiple oncoproteins that fuel lung cancer would be inhibited at the same time.