A systematic review of chromogranin A (CgA) and its biomedical applications, unveiling its structure-related functions

Abstract

Chromogranin A (CgA), which is an intrinsically disordered protein that belongs to the granin family, was first discovered in the bovine adrenal medulla, and later identified in various organs. Under certain physiological conditions, CgA is cleaved into functionally diverse peptides, such as vasostatin-1, pancreastatin, and catestatin. In this review, we first describe the historical and systematic challenges for elucidating the molecular structures of CgA and its derived peptides and give a perspective of utilizing emerging techniques through integrative approaches. Subsequently, we review specific biological processes associated with CgA and its derived peptides in the neuroendocrine, immune, and digestive systems. Finally, we discuss biomedical applications of CgA as a biomarker, suggesting future directions toward translational and precision medicine.

Never Fold to Fold Continuously: A Conundrum in Ubiquitin–Proteasome System (UPS)-Mediated Protein Quality Control (PQC)

“…(V) Assemblers, which, as suggested by the name, interact with multiple binding partners, thereby bringing them together and thus encouraging and promoting the formation of higher-order protein complexes, such as members of the transcription preinitiation complex, ribosomes, and RIP1/RIP3 necrosomes [26][27][28]. Lastly, we have (VI) scavengers and sponges, which are classified as such as they are capable of storing and neutralizing small ligands and heavy metals (i.e., chromogranin A, caseins, and other calcium-binding proteins) [29][30][31].…”