Collagen XXIV, a vertebrate fibrillar collagen with structural features of invertebrate collagens: selective expression in developing cornea and bone.
Tissue-specific assembly of fibers composed of the major collagen types I and II depends in part on the formation of heterotypic fibrils, using the quantitatively minor collagens V and XI. Here we report the identification of a new fibrillar-like collagen chain that is related to the fibrillar alpha1(V), alpha1(XI), and alpha2(XI) collagen polypeptides and which is coexpressed with type I collagen in the developing bone and eye. The new collagen was designated the alpha1(XXIV) chain and consists of a long triple helical domain flanked by typical propeptide-like sequences. The carboxyl propeptide is classic, with 8 conserved cysteine residues. The amino-terminal peptide contains a thrombospodin-N-terminal-like (TSP) motif and a highly charged segment interspersed with several tyrosine residues, like the fibril diameter-regulating collagen chains alpha1(V) and alpha1(XI). However, a short imperfection in the triple helix makes alpha1(XXIV) unique from other chains of the vertebrate fibrillar collagen family. The triple helical interruption and additional select features in both terminal peptides are common to the fibrillar chains of invertebrate organisms. Based on these data, we propose that collagen XXIV is an ancient molecule that may contribute to the regulation of type I collagen fibrillogenesis at specific anatomical locations during fetal development.
Koch
Manuel
M
Institute for Biochemistry II, University of Cologne, Joseph-Stelzmann Strasse 52, Cologne 50931, Germany.
Laub
Friedrich
F
Zhou
Peihong
P
Hahn
Rita A
RA
Tanaka
Shizuko
S
Burgeson
Robert E
RE
Gerecke
Donald R
DR
Ramirez
Francesco
F
Gordon
Marion K
MK
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001842:Bone and Bones / Q000196:embryology* / Q000378:metabolism; D003001:Cloning, Molecular; D003094:Collagen / Q000096:biosynthesis* / Q000737:chemistry*; D003315:Cornea / Q000196:embryology* / Q000378:metabolism; D018076:DNA, Complementary / Q000378:metabolism; D006801:Humans; D017403:In Situ Hybridization; D051379:Mice; D008957:Models, Genetic; D008969:Molecular Sequence Data; D016376:Oligonucleotides, Antisense / Q000378:metabolism; D010455:Peptides / Q000737:chemistry; D017434:Protein Structure, Tertiary; D012313:RNA / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid; D013997:Time Factors; D014018:Tissue Distribution
D018076:DNA, Complementary; D016376:Oligonucleotides, Antisense; D010455:Peptides; D012333:RNA, Messenger; C467802:collagen type XXIV; D012313:RNA; D003094:Collagen