Periostin is a disulfide bonded homodimer and forms a complex with fibronectin in human skin

ABSTRACT: The protein periostin is a matricellular protein that is expressed in connective tissue. It is composed of five globular domains arranged in an elongated structure with an extensive disordered C-terminal tail. Periostin contains eleven cysteine residues, of which one is unpaired, and the rest forms five intra-molecular disulfide bonds. Periostin plays an important role during wound healing and is also involved in driving the inflammatory state in atopic diseases. This study provides a comprehensive biochemical characterization of periostin in human skin and in dermal and pulmonary fibroblasts in vitro. Through the application of Western blotting, co-immunoprecipitation, and LC-MS/MS, we show for the first time that periostin is a disulfide bonded homodimer and engages in a novel disulfide bonded complex with fibronectin both in vivo and in vitro. This inherent characteristic of periostin holds the potential to redefine our approach to exploring and understanding its functional role in future research endeavors.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Skin, Fibroblast

SUBMITTER: Christian Rusbjerg-Weberskov  

LAB HEAD: Jan J.

PROVIDER: PXD045285 | Pride | 2025-01-22

REPOSITORIES: pride