TY - JOUR
T1 - Periostin Is a Disulfide-Bonded Homodimer and Forms a Complex with Fibronectin in the Human Skin
AU - Rusbjerg-Weberskov, Christian E.
AU - Scavenius, Carsten
AU - Enghild, Jan J.
AU - Nielsen, Nadia Sukusu
PY - 2024/10
Y1 - 2024/10
N2 - 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 11 cysteine residues, of which one is unpaired and the rest form five intramolecular 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.
AB - 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 11 cysteine residues, of which one is unpaired and the rest form five intramolecular 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.
UR - http://www.scopus.com/inward/record.url?scp=85205896497&partnerID=8YFLogxK
U2 - 10.1021/acs.biochem.4c00240
DO - 10.1021/acs.biochem.4c00240
M3 - Journal article
C2 - 39352075
AN - SCOPUS:85205896497
SN - 0006-2960
VL - 63
SP - 2658
EP - 2669
JO - Biochemistry
JF - Biochemistry
IS - 20
ER -