Covalent structure of collagen: amino acid sequence of .alpha.1(III)-CB9 from type III collagen of human liver

Seyer, Jerome M.; Kang, Andrew H.

doi:10.1021/bi00512a040

Cited by 57 publications

(22 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The lack of any 3-hydroxylation of the A1 site motif at Pro 992 in ␣1(III) (Fig. 6), despite a candidate proline, is consistent with an earlier reported absence of 3Hyp from human and bovine type III collagen based on amino acid composition and Edman sequencing analyses (25).…”

supporting

confidence: 90%

“…Most of the data on 3Hyp in collagen in the literature were gathered from amino acid analyses as the different chain types were discovered and their cyanogen bromide-derived peptides were characterized (21)(22)(23)(24)(25)(26)(27). The present results are consistent with these original quantitative measurements, which showed, for example, one residue of 3Hyp per ␣1(I) and ␣2(I) chain of type I collagen (22,23).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Location of 3-Hydroxyproline Residues in Collagen Types I, II, III, and V/XI Implies a Role in Fibril Supramolecular Assembly

Weis

Hudson

Kim

et al. 2010

Journal of Biological Chemistry

146

189

View full text Add to dashboard Cite

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 ␣1(I), ␣1(II), and ␣2(V). Two partially modified sites (A2 and A3) were found at Pro 944 in ␣1(II) and ␣2(V) and Pro 707 in ␣2(I) and ␣2(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 ␣2(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 ␣1(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.Collagens are the most abundant and ubiquitous proteins in multi-cellular animals. It is well established that 4-hydroxyproline (4Hyp) 2 residues stabilize the collagen triple helix through water-bridged intramolecular hydrogen bonding (1). However, the function of the much less abundant 3-hydroxyproline (3Hyp), although discovered 50 years ago, is unknown (2). Only 1-2 residues of 3Hyp occur per chain in collagen types I and II and 3-6 residues occur per chain in collagen types V and XI. The content is highest in type IV collagens of basement membranes in which 10% of the total hydroxyproline can be 3Hyp (3).Specific prolyl 3-hydroxylases (P3Hs) are responsible for 3Hyp synthesis. Three different genes encoding P3H1, P3H2, and P3H3 are present in the human genome, which show tissue specificity in their expression (4, 5). Substrate proline residues occur in a prerequisite sequence -Pro-4Hyp-Gly. The ␣1(I) chain has only one established 3Hyp site at Pro 986 in a motif conserved across vertebrate species (human GLPGPIGPPGPR) a close variant of which also occurs in type II collagen (human GIPGPIGPPGPR).Renewed interest in 3Hyp was recently sparked by the discovery that a recessive form of osteogenesis imperfecta (OI) is caused by mutations in CRTAP. This gene encodes a protein (cartilage-associated protein) that is bound to P3H1 and cyclophilin B in the endoplasmic reticulum and is requi...

show abstract

supporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Location of 3-Hydroxyproline Residues in Collagen Types I, II, III, and V/XI Implies a Role in Fibril Supramolecular Assembly

Weis

Hudson

Kim

et al. 2010

Journal of Biological Chemistry

146

189

View full text Add to dashboard Cite

show abstract

“…Previous amino acid analysis of ␣1(V) chains from human placenta (69) or human skin (15) estimated 3-Hyp content at four or ten 3-Hyp residues, respectively, per 1000 amino acids, levels higher than those detected by similar analyses of the major fibrillar collagen chains (71)(72)(73)(74). The nine Hyp residues mapped here to the X-positions of Gly-Hyp-Hyp repeats in the COL1 domain of human recombinant pro-␣1(V) chains falls within this range (15,69).…”

Section: Comparison Of the Col1 Ptms Of Bovine Placental ␣1(v) And Humentioning

confidence: 95%

Comprehensive Mass Spectrometric Mapping of the Hydroxylated Amino Acid residues of the α1(V) Collagen Chain

Yang

Park

Davis

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: ␣1(V) is an extensively modified collagen chain important in disease. Results: Comprehensive mapping of ␣1(V) post-translational modifications reveals unexpectedly large numbers of X-position hydroxyprolines in Gly-X-Y amino acid triplets. Conclusion:The unexpected abundance of X-position hydroxyprolines suggests a mechanism for differential modification of collagen properties. Significance: Positions, numbers, and occupancy of modified sites can provide insights into ␣1(V) biological properties.

show abstract

“…Plasmid DNAs were cleaved with Pst I or HindIII/Pst I, and the fragments were directly ligated into M13 mpl8 mpl9 vectors. Protein sequences for the human al(III) collagen chain, obtained by Edman degradation, have been reported (29). Isolation of the human a2(V) collagen chain from amnion/chorionic mem- $To whom reprint requests should be addressed.…”

Section: Methodsmentioning

confidence: 99%

Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2.

Emanuel¹,

Cannizzaro²,

Seyer³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The multigene procollagen family encodes probably >20 genetically distinct but structurally related polypeptide chains. Recent characterization of human procollagen clones has allowed determination of functional domains within the proteins, genomic organization, and chromosomal location. Previously, we assigned the coordinately expressed type I genes (al and a2) to chromosomes 17 and 7, respectively, and now other investigators have mapped the type II gene to chromosome 12 [Strom, C. M., Eddy, R. L. & Shows, T. B. (1984) Somatic CeU Genet. 10, 651-655]. Recently, we isolated cDNA clones encoding the fourth interstitial procollagen, type III, and the a2 chain of the type V cytoskeletal components. To determine whether these genes were clustered with al(I), a2(I), or al(II) or were further dispersed in the genome, in situ hybridization of the a1(Ill) and a2(V) probes to metaphase chromosomes was carried out. Here we report a fourth autosome with procollagen gene loci but the first cytological evidence for linkage. By using normal and translocated cell lines, our results show that both the ail(llI) and a2(V) procollagen genes map to the q24.3--q31 region of chromosome 2.The procollagens constitute a group of proteins responsible for the structural integrity of connective tissue (see refs. 1-4 for reviews). The polypeptide chains are generally composed of a large collagenous domain with the repeating Gly-X-Y sequence flanked by smaller amino-and carboxyl-extension peptides. More than five major and five minor types of collagen have been identified, which consist of one, two, or three different chains folded into a triple-helical molecule (1-9). While several types have a unique tissue distribution (II in cartilage and IV in basement membrane), others (I, III, and V) are usually coexpressed but at different levels depending on the cell type (1-4). We have been studying the structure and regulation of these latter three collagens normally found together in the proportion I > III > V. Whereas type I is the major collagen species in skin, bone, tendon, placenta, lung, and liver, type III appears to predominate in blood vessels and internal organs (1-4, 10, 11). Little is currently known about the minor component, type V, except for its distribution in pericellular regions (12).Isolation of DNA clones encoding different procollagen chains has allowed determination of the amino acid sequence, genomic organization, and chromosomal assignment (see refs. 4 and 13 for reviews). For example, the sizes of the al(I) and a2(I) genes (13-15) are inversely proportional to the 2:1 ratio of the mRNAs in cultured fibroblasts, reflecting the subunit composition of type I collagen (16). Interestingly, these two carefully regulated coding units, both interrupted by -50 introns, are located on the long arm of chromosomes 17 and 7, respectively, as determined from somatic cell and in situ hybridization (17)(18)(19)(20). Since the collagens seem to have arisen by duplication of a 54-base-pair (bp) primordial unit (21), it had been ...

show abstract

Covalent structure of collagen: amino acid sequence of .alpha.1(III)-CB9 from type III collagen of human liver

Cited by 57 publications

References 20 publications

Location of 3-Hydroxyproline Residues in Collagen Types I, II, III, and V/XI Implies a Role in Fibril Supramolecular Assembly

Location of 3-Hydroxyproline Residues in Collagen Types I, II, III, and V/XI Implies a Role in Fibril Supramolecular Assembly

Comprehensive Mass Spectrometric Mapping of the Hydroxylated Amino Acid residues of the α1(V) Collagen Chain

Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2.

Contact Info

Product

Resources

About