Protein kinase C alpha, beta I, beta II, delta, epsilon, eta, and theta (PKC alpha/betaI/betaII/delta/epsilon/eta/theta)

Protein kinase C (PKC) is a family of serine/threonine kinases that act as key mediators in various signal transduction pathways [5]. This specific target profile encompasses the classical isoforms (alpha, beta I, and beta II) and the novel isoforms (delta, epsilon, eta, and theta), which are distinguished by their activation requirements for calcium and diacylglycerol [2, 3]. These kinases regulate fundamental cellular processes, including growth, differentiation, and the immune response; for instance, PKC theta is critical for T-cell receptor signaling and activation [2, 6]. Dysregulation of these PKC isoforms is implicated in a wide range of diseases, such as uveal melanoma, diabetic microvascular complications, and autoimmune disorders [4, 7, 8]. Drugs targeting this group, such as the pan-PKC inhibitor sotrastaurin, typically act by competing with ATP for the kinase's catalytic site [3, 8]. While broad inhibition offers therapeutic potential in complex diseases, it also presents challenges related to off-target effects and systemic toxicities like gastrointestinal distress and immunosuppression [7, 8].

Other names

PRKCAPRKCBPRKCDPRKCEPRKCHPRKCQClassical and novel PKC isoformsPan-PKC (excluding gamma and atypical)

Small molecule inhibition of the catalytic domain (ATP-binding site) of multiple Protein Kinase C isoforms, preventing the phosphorylation of downstream substrates like MARCKS and CARD11.