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Location of 3-hydroxyproline residues in collagen types I, II, III, and V/XI implies a role in fibril supramolecular assembly.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2010 Jan 22; Vol. 285 (4), pp. 2580-90. Date of Electronic Publication: 2009 Nov 23. - Publication Year :
- 2010
-
Abstract
- Collagen triple helices are stabilized by 4-hydroxyproline residues. No function is known for the much less common 3-hydroxyproline (3Hyp), although genetic defects inhibiting its formation cause recessive osteogenesis imperfecta. To help understand the pathogenesis, we used mass spectrometry to identify the sites and local sequence motifs of 3Hyp residues in fibril-forming collagens from normal human and bovine tissues. The results confirm a single, essentially fully occupied 3Hyp site (A1) at Pro(986) in A-clade chains alpha1(I), alpha1(II), and alpha2(V). Two partially modified sites (A2 and A3) were found at Pro(944) in alpha1(II) and alpha2(V) and Pro(707) in alpha2(I) and alpha2(V), which differed from A1 in sequence motif. Significantly, the distance between sites 2 and 3, 237 residues, is close to the collagen D-period (234 residues). A search for additional D-periodic 3Hyp sites revealed a fourth site (A4) at Pro(470) in alpha2(V), 237 residues N-terminal to site 3. In contrast, human and bovine type III collagen contained no 3Hyp at any site, despite a candidate proline residue and recognizable A1 sequence motif. A conserved histidine in mammalian alpha1(III) at A1 may have prevented 3-hydroxylation because this site in chicken type III was fully hydroxylated, and tyrosine replaced histidine. All three B-clade type V/XI collagen chains revealed the same three sites of 3Hyp but at different loci and sequence contexts from those in A-clade collagen chains. Two of these B-clade sites were spaced apart by 231 residues. From these and other observations we propose a fundamental role for 3Hyp residues in the ordered self-assembly of collagen supramolecular structures.
- Subjects :
- Adult
Amino Acid Sequence
Animals
Bone and Bones chemistry
Bone and Bones metabolism
Cartilage chemistry
Cartilage metabolism
Cattle
Chickens
Collagen genetics
Collagen Type I chemistry
Collagen Type I genetics
Collagen Type I metabolism
Collagen Type II chemistry
Collagen Type II genetics
Collagen Type II metabolism
Collagen Type III chemistry
Collagen Type III genetics
Collagen Type III metabolism
Collagen Type V chemistry
Collagen Type V genetics
Collagen Type V metabolism
Collagen Type XI chemistry
Collagen Type XI genetics
Collagen Type XI metabolism
Extracellular Matrix Proteins chemistry
Extracellular Matrix Proteins genetics
Extracellular Matrix Proteins metabolism
Humans
Hydroxyproline genetics
Molecular Sequence Data
Protein Processing, Post-Translational
Tandem Mass Spectrometry
Young Adult
Collagen chemistry
Collagen metabolism
Hydroxyproline chemistry
Hydroxyproline metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 285
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 19940144
- Full Text :
- https://doi.org/10.1074/jbc.M109.068726