Identification of the physiological substrates of PDIp, a pancreas-specific protein-disulfide isomerase family member.

ABSTRACT: About 20 members of the protein-disulfide isomerase (PDI) family are present in the endoplasmic reticulum of mammalian cells. They are thought to catalyze thiol-disulfide exchange reactions within secretory or membrane proteins to assist in their folding or to regulate their functions. PDIp is a PDI family member highly expressed in the pancreas and known to bind estrogen in vivo and in vitro However, the physiological functions of PDIp remained unclear. In this study, we set out to identify its physiological substrates. By combining acid quenching and thiol alkylation, we stabilized and purified the complexes formed between endogenous PDIp and its target proteins from the mouse pancreas. MS analysis of these complexes helped identify the disulfide-linked PDIp targets in v

SUBMITTER: Fujimoto T 

PROVIDER: S-EPMC6290160 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature