The shed ectodomain of type XIII collagen associates with the fibrillar fibronectin matrix and may interfere with its assembly in vitro.
Type XIII collagen is a transmembrane collagen, which is known to exist also as a soluble variant due to ectodomain shedding. Earlier studies with the recombinant ectodomain have shown it to interact in vitro with a number of extracellular matrix proteins, e.g. Fn (fibronectin). In view of its strong binding to Fn, we examined in the present study whether the released soluble ectodomain can bind to the fibrillar Fn matrix under cell-culture conditions and, if so, influence its assembly. In this study, we demonstrate that the type XIII collagen ectodomain of mammalian cells can associate with Fn fibres and may eventually hamper incorporation of the fibrillar Fn meshwork. The association between type XIII collagen and Fn was implicated to be mediated by the C-terminal end of type XIII collagen and the N-terminal end of Fn. The results presented here imply that the shedding of the type XIII collagen ectodomain results in a biologically active molecule capable of remodelling the structure of the pericellular matrix.
Väisänen
Marja-Riitta
MR
Collagen Research Unit, Biocenter Oulu and Department of Medical Biochemistry and Molecular Biology, University of Oulu, P.O. Box 5000, 90014 University of Oulu, Finland.
Väisänen
Timo
T
Tu
Hongmin
H
Pirilä
Päivi
P
Sormunen
Raija
R
Pihlajaniemi
Taina
T
D000818:Animals; D002417:Cattle; D002478:Cells, Cultured; D024181:Collagen Type XIII / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006224:Cricetinae; D005109:Extracellular Matrix / Q000378:metabolism; D005353:Fibronectins / Q000096:biosynthesis* / Q000737:chemistry / Q000378:metabolism*; D017353:Gene Deletion; D006801:Humans; D011347:Procollagen / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D015854:Up-Regulation
D024181:Collagen Type XIII; D005353:Fibronectins; D011347:Procollagen