Synteny between the loci for a novel FACIT-like collagen locus (D6S228E) and α1(IX) collagen (COL9A1) on 6q12–q14 in humans

Yoshioka, Hidekatsu; Zhang, Hui; Ramirez, Francesco; Matteï, Marie‐Geneviève; Moradi-Améli, Mahnaz; Rest, Michel van der; Gordon, Marion K.

doi:10.1016/0888-7543(92)90176-s

Cited by 50 publications

(27 citation statements)

References 6 publications

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“…Three distinct mouse embryonic cDNA libraries were screened under low stringency conditions using probes specific for the human ␣1(XIX) collagen (4, 7). Hybridizations carried out at 55°C overnight in a mixture containing 5 ϫ SSC (1 ϫ SSC; 0.15 M NaCl, 0.015 M sodium citrate, pH 6.8), 1% N-laurylsarcosine, 50 g/ml salmon sperm DNA, and 32 P-labeled probes after prehybridization which is the same solution without probes for 1 h. Isolation and purification of the positive clones were as described previously (7). Sequencing was carried out according to the dideoxy chain termination methods using an ABI 373S automatic sequencer.…”

Section: Methodsmentioning

confidence: 99%

“…Type XIX collagen was originally discovered through cDNA cloning of RNA transcripts from the human rhabdomyosarcoma cell line RD (CCL 136) (7). The predicted polypeptide was found to contain 1,142 amino acid residues with a 23-residue signal peptide followed by the five collagenous (COL) domains, interspersed and flanked with the six non-collagenous (NC) domains (3,4,8).…”

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“…Additionally, an unusual number of splicing events appeared to occur in the RD cell line. More interestingly, the ␣1(XIX) collagen gene (COL19A1) was located to human chromosome 6q12-q14, syntenic to the ␣1(IX) collagen (COL9A1) and ␣1(XII) collagen genes (COL12A1) (7,9). Type IX collagen is found in tissues containing type II collagen, such as hyaline cartilage and the vitreous body of the eye.…”

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Ubiquitous Expression of the α1(XIX) Collagen Gene (Col19a1) during Mouse Embryogenesis Becomes Restricted to a Few Tissues in the Adult Organism

Sumiyoshi

Inoguchi

Khaleduzzaman

et al. 1997

Journal of Biological Chemistry

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Type XIX collagen is a poorly characterized member of the fibril-associated collagens with an interrupted triple helices (FACIT) class of collagen molecules. As a first step toward elucidating its function, we have isolated full size cDNA clones from the mouse ␣1(XIX) collagen gene (Col19a1) and established its pattern of expression in the developing embryo and adult organism. Col19a1 transcripts can be detected as early as 11 days of gestation and in all embryonic tissues, except the liver, of an 18-day postcoitum mouse. In contrast, only a few adult tissues, brain, eye, and testis, seem to accumulate Col19a1 mRNA. Col19a1 transcripts are at least 10 times more abundant in adult than fetal brain and significantly less in adult than fetal muscle and skin. Consistent with the RNA data, polyclonal antibodies for ␣1(XIX) collagen reacted with a 150-kDa protein in the neutral salt extraction of adult mouse brain tissues. We therefore propose that type XIX collagen plays a distinct role from the other FACIT molecules, particularly in the assembly of embryonic matrices and in the maintenance of specific adult tissues.

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Section: Methodsmentioning

confidence: 99%

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Ubiquitous Expression of the α1(XIX) Collagen Gene (Col19a1) during Mouse Embryogenesis Becomes Restricted to a Few Tissues in the Adult Organism

Sumiyoshi

Inoguchi

Khaleduzzaman

et al. 1997

Journal of Biological Chemistry

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“…This dendrogram shows that all NC4 domains fall into two major groups, the NC4 motifs of the FACIT collagens IX, XI1 and X N being more closely related to each other than to the interstitial collagens V and XI. Very recently, two novel members of the FACIT family have been described (Pan et al, 1992;Yoshioka et al, 1992). It appears that these molecules also contain a domain related to the NC4 motif.…”

Section: Amino-acid Sequencementioning

confidence: 99%

Complete primary structure of chicken collagen XIV

Wälchli

Trueb

Kessler

et al. 1993

European Journal of Biochemistry

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We have isolated and characterized several overlapping cDNA clones for chicken collagen XIV which span a total of 6.5 kbp. These clones contain an open reading frame of 5571 bp encoding the entire collagen XIV polypeptide. The predicted polypeptide has an estimated molecular mass of 205 kDa in its glycosylated form. It is composed of 1857 amino acids which are arranged in 16 individual subdomains, including a signal peptide of 28 residues. The large amino-terminal globular domain of collagen XIV (NC3) comprises 11 of these 16 subdomains. Two of them are related to the A modules of von Willebrand factor, eight show some relationship to the type 111-repeats of fibronectin and one is similar to the NC4 domain of collagen IX. The carboxy-terminal triple-helical domain is composed of two collagenous segments (COL1 and COL2), which make up less than 14% of the entire molecular mass, and of two short non-collagenous domains (NC1 and NC2). A detailed analysis of our cDNA clones indicates that collagen XIV exists in two alternatively spliced forms which differ by 31 amino acids in their NC1 domain. The variant form of the polypeptide contains 1888 amino acids with a total molecular mass of 208 kDa. Our results demonstrate that collagen XIV displays a complex multidomain structure resembling that proposed for collagen XII.The mechanical stability of the tissues in the body is mainly provided by the tensile strength of distinct collagen fibrils embedded in their extracellular matrix. These fibrils are composed of the interstitial collagen molecules I, 11,

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“…Collagen XIX was identified from independently isolated clones from a human rhabdomyosarcoma cell line (9,10). The type XIX chain is composed of a 268-residue, noncollagenous amino terminus, an 832-residue discontinuous collagenous region, and a 19-residue carboxyl-terminal peptide (10 -12).…”

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Trimerization and Triple Helix Stabilization of the Collagen XIX NC2 Domain

Boudko

Engel

Bächinger

2008

Journal of Biological Chemistry

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The fibril-associated collagens with interrupted triple helices (FACIT 2 collagens) include type IX, XII, XIV, XVI, XIX, XX, XXI, and XXII. Collagen IX is a heterotrimer composed of three different ␣-chains, and all others are homotrimers whose ␣-chains are characterized by short collagenous (COL) domains interrupted by several noncollagenous (NC) domains (1, 2). Unlike the fibril-forming collagens, the FACITs have significantly shorter carboxyl-terminal NC domains (NC1 domains): 37 residues for collagen XIV, 20 -25 residues for collagen IX, and even fewer than 20 residues for collagen types XII and XIX (based on human sequences). In contrast, the carboxyl-terminal NC domains of fibrillar collagens (C-propeptides) are of a different type and contain about 260 residues. The FACITs share a remarkable sequence homology at their COL1/ NC1 junctions, each having two strictly conserved cysteine residues separated by four residues in their NC1 domain. Several studies suggest that the COL1 domain and the NC1 domain are involved in the mechanism of chain selection in the assembly of collagens . Contrary to these studies, very recent studies on collagen IX show that three ␣-chains can associate in the absence of the COL1 and NC1 domains to form a triple helix, although the COL2-NC2 region alone is not sufficient for trimerization (7). This suggests that folding and chain selection of collagen IX is a cooperative process involving multiple COL and NC domains (7). It has also been hypothesized that the NC2 domain of all FACIT collagens is able to form an ␣-helical coiled-coil, thus bearing an ability to trimerize those collagens (8), but no experimental evidence has been reported so far.Collagen XIX was identified from independently isolated clones from a human rhabdomyosarcoma cell line (9, 10). The type XIX chain is composed of a 268-residue, noncollagenous amino terminus, an 832-residue discontinuous collagenous region, and a 19-residue carboxyl-terminal peptide (10 -12). It is by far the least abundant collagen so far purified, with a composition of ϳ10 Ϫ6 % of the dry weight of umbilical cord (13). Several features in the type XIX sequence place this collagen in the largest subclass of the nonfibrillar group, the FACIT collagens. These include a ϳ250-residue thrombospondin module at the amino terminus, the position of two 2-amino acid interruptions in the collagenous subdomain closest to the carboxyl terminus, and a Cys-Xaa 4 -Cys motif situated at the junction of the collagenous region and carboxyl peptide (COL1/NC1 junction) (11, 12).Characterization of mice harboring null or structural mutations in the collagen XIX (Col19a1) gene has revealed the critical contribution of this matrix protein to muscle physiology and differentiation (14). The phenotype includes smooth muscle motor dysfunction and a hypertensive sphincter. Mice without collagen XIX also display impaired smooth-to-skeletal muscle cell conversion in the abdominal segment of the esophagus (14). Electron microscope images of protein purified from human umb...

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Synteny between the loci for a novel FACIT-like collagen locus (D6S228E) and α1(IX) collagen (COL9A1) on 6q12–q14 in humans

Cited by 50 publications

References 6 publications

Ubiquitous Expression of the α1(XIX) Collagen Gene (Col19a1) during Mouse Embryogenesis Becomes Restricted to a Few Tissues in the Adult Organism

Ubiquitous Expression of the α1(XIX) Collagen Gene (Col19a1) during Mouse Embryogenesis Becomes Restricted to a Few Tissues in the Adult Organism

Complete primary structure of chicken collagen XIV

Trimerization and Triple Helix Stabilization of the Collagen XIX NC2 Domain

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