TY - JOUR
T1 - Collagen XXVII is developmentally regulated and forms thin fibrillar structures distinct from those of classical vertebrate fibrillar collagens
AU - Plumb, Darren A.
AU - Dhir, Vivek
AU - Mironov, Aleksandr
AU - Ferrara, Laila
AU - Poulsom, Richard
AU - Kadler, Karl E.
AU - Thornton, David J.
AU - Briggs, Michael D.
AU - Boot-Handford, Raymond P.
PY - 2007/4/27
Y1 - 2007/4/27
N2 - We have generated an antiserum to the variable domain of mouse collagen XXVII, a recently discovered novel member of the fibrillar collagen family. Collagen XXVII protein was first detectable in the mouse at embryonic day 12.5 (E12.5). By E14.5, the protein localized to cartilage, developing dermis, cornea, the inner limiting membrane of the retina, and major arteries of the heart. However, at E18.5, collagen XXVII protein was no longer apparent in most tissues and appeared restricted mainly to cartilage where expression continued into adulthood. Type XXVII collagen immunolocalized to 10-nm-thick nonstriated fibrils that were distinct from fibrils formed by the classical fibrillar collagens. The transient nature of its expression and unusual fibrillar structure suggest that collagen XXVII plays a developmental role distinct from those of the classical fibrillar collagens. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
AB - We have generated an antiserum to the variable domain of mouse collagen XXVII, a recently discovered novel member of the fibrillar collagen family. Collagen XXVII protein was first detectable in the mouse at embryonic day 12.5 (E12.5). By E14.5, the protein localized to cartilage, developing dermis, cornea, the inner limiting membrane of the retina, and major arteries of the heart. However, at E18.5, collagen XXVII protein was no longer apparent in most tissues and appeared restricted mainly to cartilage where expression continued into adulthood. Type XXVII collagen immunolocalized to 10-nm-thick nonstriated fibrils that were distinct from fibrils formed by the classical fibrillar collagens. The transient nature of its expression and unusual fibrillar structure suggest that collagen XXVII plays a developmental role distinct from those of the classical fibrillar collagens. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
U2 - 10.1074/jbc.C700021200
DO - 10.1074/jbc.C700021200
M3 - Article
C2 - 17331945
SN - 1083-351X
VL - 282
SP - 12791
EP - 12795
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 17
ER -