Relationship between CHIP and myocardial ischemia/reperfusion injury / 中国病理生理杂志

ABSTRACT

Carboxyl terminus of the HSP70-interacting protein (CHIP) is a co-chaperone of HSPs as well as an E3 ubiquitin ligase, and it is the connexin between heat shock proteins and ubiquitin-proteasome system. Recent research discovered that CHIP also possesses an intrinsic chaperone activity that enables it to recognize and bind nonnative proteins independently. CHIP regulates the HSPs expression and activity, and facilitates the client proteins ubiquitination and subsequent proteasome-dependent degradation. CHIP also inhibits apoptosis through MAPKs signaling pathways, and affects eNOS specific activity by means of the effects on Akt. Moreover, CHIP plays an important role in mitochondrial oxidative stress protection. With these above points, this paper reviews the function of CHIP in myocardial ischemia/reperfusion injury.