Cloning of the chicken <i>α</i>3(IX) collagen chain completes the primary structure of type IX collagen

Brewton, Randolph G.; Ouspenskaia, Maia V.; Rest, Michel van der; Mayne, Richard

doi:10.1111/j.1432-1033.1992.tb16798.x

Cited by 25 publications

(7 citation statements)

References 44 publications

(25 reference statements)

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“…Two oligonucleotide primers (MP23 and MP24) were designed for the non-collagenous NC1 and NC2 domains of the α3 chain of the type IX collagen based on the available chick Col9a3 cDNA and bovine amino acid sequences [4,[17][18][19]. The same degenerate oligonucleotides were used for the amplification of both mouse and human α3(IX) collagen cDNA covering sequences coding for the collagenous (COL) domain COL1 and parts of the non-collagenous domains NC1 and NC2.…”

Section: Results Cdna Cloning Of Mouse and Human α3(ix) Collagen Mrnamentioning

confidence: 99%

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Developmental regulation of mRNA species for types II, IX and XI collagens during mouse embryogenesis

Perälä

Savontaus

Metsäranta

et al. 1997

Biochemical Journal

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Several techniques were used to study the co-ordination of mRNA levels for five constituent chains of cartilage collagen fibrils during mouse development. Short cDNA clones were first constructed for mouse and human alpha3(IX) and for mouse proalpha1(XI) collagen mRNA species. Northern analysis of developing mouse embryos revealed that the mRNA species for alpha1, alpha2 and alpha3 chains of type IX collagen peaked earlier than those for proalpha1(II) and proalpha1(XI) collagen chains. Quantification of these mRNA species by slot-blot hybridization confirmed this developmental regulation: the mRNA ratios for type II/type IX/type XI collagens changed from 5.7:1:0.6 (at embryonic day 12.5) to 10.6:1:0.9 (in newborn mice). However, the genes coding for the three chains of type IX collagen seemed to be under more co-ordinated regulation during mouse development. In addition to high mRNA levels in cartilages and the eye, low levels of type IX collagen transcripts were identified in brain and skin of newborn mouse using RNase protection and reverse transcriptase-PCR assays. Finally, hybridization in situ revealed identical tissue distributions of the three type IX collagen mRNA species during early chondrogenesis but somewhat more widespread expression of the alpha1(IX) and alpha3(IX) mRNA species during endochondral ossification at day 16.5 of embryonic development. These results suggest a relatively tight co-ordination of the alpha1(IX), alpha2(IX), and alpha3(IX) collagen mRNA species in chondrocytes, but a lack of co-ordination in several non-cartilaginous tissues.

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Section: Results Cdna Cloning Of Mouse and Human α3(ix) Collagen Mrnamentioning

confidence: 99%

“…chain. Two interruptions in the Gly-Xaa-Yaa repeat structure are also conserved between the three species [18,19].…”

Section: Results Cdna Cloning Of Mouse and Human α3(ix) Collagen Mrnamentioning

confidence: 99%

Developmental regulation of mRNA species for types II, IX and XI collagens during mouse embryogenesis

Perälä

Savontaus

Metsäranta

et al. 1997

Biochemical Journal

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“…The complete cDNA sequences for the ␣3(IX) chain are currently available for chick (22,23) and human (24). Here we report the complete genomic organization and sequences of the human COL9A3 gene.…”

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confidence: 99%

Complete Sequence of the 23-Kilobase Human COL9A3Gene

Paassilta

Pihlajamaa

Annunen

et al. 1999

Journal of Biological Chemistry

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We report the complete sequence of the human COL9A3 gene that encodes the ␣3 chain of heterotrimeric type IX collagen, a member of the fibril-associated collagens with interrupted triple helices family of collagenous proteins. Nucleotide sequencing defined over 23,000 base pairs (bp) of the gene and about 3000 bp of the 5-flanking sequences. The gene contains 32 exons. The domain and exon organization of the gene is almost identical to a related gene, the human COL9A2 gene. However, exon 2 of the COL9A3 gene codes for one -Gly-X-Y-triplet less than exon 2 of the COL9A2 gene. The difference is compensated by an insertion of 9 bp coding for an additional triplet in exon 4 of the COL9A3 gene. As a result, the number of -Gly-X-Y-repeats in the third collagenous domain remains the same in both genes and ensures the formation of an in-register triple helix. In the course of screening this gene for mutations, heterozygosity for separate 9-bp deletions within the COL1 domain were identified in two kindreds. In both instances, the deletions did not co-segregate with any disease phenotype, suggesting that they were neutral variants. In contrast, similar deletions in triple helical domain of type I collagen are lethal. To study whether ␣3(IX) chains with the deletion will participate in the formation of correctly folded heterotrimeric type IX collagen, we expressed mutant ␣3 chains together with normal ␣1 and ␣2 chains in insect cells. We show here that despite the deletion, mutant ␣3 chains were secreted as heterotrimeric, triple helical molecules consisting of three ␣ chains in a 1:1:1 ratio. The results suggest that the next noncollagenous domain (NC2) is capable of correcting the alignment of the ␣ chains, and this ensures the formation of an in-register triple helix.Type IX collagen is a structural component of hyaline cartilage and vitreous of the eye. It is a heterotrimeric molecule composed of three genetically distinct polypeptide chains: ␣1, ␣2, and ␣3 (1). The protein is characterized by interruptions in the triple helix, and it consists of three collagenous domains (COL1, COL2, and COL3, numbered from the C terminus) that are joined by four small noncollagenous domains (NC1 to NC4) (2, 3). In addition to interrupted triple helices, type IX collagen is a fibril-associated collagen and thus belongs to the FACIT subgroup of collagens (4).Type IX collagen is attached to the surface of type II collagen fibrils by lysine-derived covalent cross-links between the COL2 domain and telopeptides of type II collagen (5-8). Because the flexible NC3 domain enables the COL3 and NC4 domains to project out of the fibril surface, it has been suggested that the COL3 and NC4 domains may play a role in mediating interactions between collagens and noncollagenous components of hyaline cartilage (6, 9, 10). The NC3 domain of the ␣2(IX) chain also has an attachment site for a glycosaminoglycan side chain (11). Results from a recent study indicate that the NC1 domain of the three ␣ chains contains all of the necessary information for cha...

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“…The type IX collagen molecule is a heterotrimer consisting of genetically distinct a l , a2, and a3 chains [Brewton et al, 1992;Ninomiya and Olsen, 1984;Ninomiya et al, 19851. The gene encoding al(IX), COL9A1, has been localized on the long arm of chromosome 6 [Kimura et al, 19891, and the gene for a2(IX), COL9A2, has been mapped to chromosome 1 [Peraelae et al, 19931.…”

Section: Discussionmentioning

confidence: 99%

Abnormality of type IX collagen in a patient with diastrophic dysplasia

Diab

Shapiro

et al. 1994

Am. J. Med. Genet.

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There is growing evidence that a spectrum of chondrodysplasias are caused by mutations in the gene coding for type II collagen. The basic molecular defect in diastrophic dysplasia has not been defined, but it appears not to be in collagen type II. Cartilage contains other tissue-specific collagens, types IX, X, and XI, but no mutations have yet been found in their genes in clinical disease. Type IX collagen is hypothesized to play a role in the regulation of type II collagen fibril organization and structure in cartilage extracellular matrix. In this study, we have examined iliac crest growth cartilage from a patient with diastrophic dysplasia. Although collagen fibrils were markedly increased in diameter on transmission electron microscopy, type II collagen appeared to be normal biochemically. Type XI collagen was also normal. However, type IX collagen appeared abnormal on sodium dodecyl sulfate polyacrylamide gel electrophoresis with a pronounced excess of the COL1 domain of the molecule in pepsin extracts. The findings point to an abnormality in structure or metabolism of type IX collagen in diastrophic dysplasia.

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Cloning of the chicken α3(IX) collagen chain completes the primary structure of type IX collagen

Cited by 25 publications

References 44 publications

Developmental regulation of mRNA species for types II, IX and XI collagens during mouse embryogenesis

Developmental regulation of mRNA species for types II, IX and XI collagens during mouse embryogenesis

Complete Sequence of the 23-Kilobase Human COL9A3Gene

Abnormality of type IX collagen in a patient with diastrophic dysplasia

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