ALLM (Calpain inhibitor II), a potent calpain and cathepsin protease inhibitor, not only prevents neuronal cell death but also enhances chronic neurological function following spinal cord injury (SCI)[1][2].
Protein kinase C (PKC ) is a calcium-independent, phospholipid- and diacylglycerol-dependent serine threonine kinase involved in diverse signaling pathways, including those involved in neuronal signaling, cytoskeletal function, and inflammation.[1] PKC inhibitor peptide is a synthetic peptide corresponding to an amino acid sequence found in the amino terminal C2 domain of most mammalian forms of PKC .[2] It selectively and reversibly inhibits the translocation of PKC to intracellular membranes, blocking activation.[2] PKC inhibitor peptide is commonly used in cells to evaluate the role of PKC in various cellular responses.[3],[4],[5]
3-Iodothyronamine is derived from the deiodination and decarboxylation of endogenous thyroxine. It activates the G protein-coupled receptor known as trace amine-associated receptor 1 at nanomolar concentrations whereupon it rapidly influences thyroid hormone actions including body temperature, heart rate, and cardiac output. It has also been reported to function in controlling lipid and glucose utilization, hormonal secretion, and neuronal function, and has been considered for use in chemically-induced hibernation for medical purposes.
Z640 an aPKC agonist. Z640 was further confirmed as a non‑selective aPKC agonist that can activate the kinase activity of both PKCι and PKCζ. In the cell‑based assay, Z640 was found to protect neuronal cell lines from amyloid‑β (Aβ) oligomer‑induced cell death by reducing reactive oxygen species production and restore mitochondrial function. In addition, Z640 could reduce Aβ40 generation in a dose‑dependent manner and shift amyloid precursor protein processing towards the non‑amyloid pathway