Synthesis and characterization of cDNA encoding a cartilage-specific short collagen.

Ninomiya, Yoshifumi; Olsen, Bjørn R.

doi:10.1073/pnas.81.10.3014

Cited by 125 publications

(38 citation statements)

References 34 publications

(36 reference statements)

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“…pMG377 was digested with EcoRI and HindIl for electrophoresis through 1.5% agarose gels, blotted onto nitrocellulose, and probed with nick-translated al(I) and a2(I) cDNA probes. The results showed that it did not hydridize to type H20 6 +c 7 -c 8 +c 9 Fig. 2; the result of the sequence analysis is shown in Fig.…”

Section: Resultsmentioning

confidence: 98%

“…Total RNA from 6-day-old chicken embryo cornea and from 15-or 17-day-old tendons, sterna, and calvarial bones was isolated by using the guanidine thiocyanate method (12) as adapted by Maniatis et al (13). Poly(A)+ RNA, obtained by oligo(dT)-cellulose chromatography (14), was fractionated by centrifugation through low-salt sucrose gradients (15 (9). After electrophoresis at 300 V through 10% polyacrylamide gels, the gels were exposed to x-ray film to determine which cDNAs exhibited the Sau96I "ladder" pattern typical of collagens.…”

Section: Methodsmentioning

confidence: 99%

“…cDNA probes corresponding to the al(IX) and a2(IX) chains (9,10) have been used to demonstrate that type IX collagen mRNAs are expressed in a tissue-specific manneri.e., they are expressed by chicken embryo chondrocytes but not by chicken embryo fibroblasts (9,11). However, tendon fibroblasts do contain mRNAs capable of synthesizing bacterial collagenase-sensitive polypeptides that are similar in size to type IX polypeptides (11).…”

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confidence: 99%

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Type XII collagen: distinct extracellular matrix component discovered by cDNA cloning.

Gordon¹,

Gerecke²,

Olsen³

1987

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

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127

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We have screened a cDNA library constructed from tendon fibroblast mRNA for the presence of collagenous coding sequences. Nucleotide sequence analysis of one isolated clone, pMG377, reveals that the clone encodes a polypeptide that is homologous to, yet distinctly different from, type IX short-chain collagen polypeptides. The structure of the conceptual translation product of the cDNA is also different from that of all other collagen types. Therefore, we The extracellular matrix components classified as collagens on the basis of their triple-helical domain constitute a heterogeneous group of proteins with a variety of molecular structures and interaction properties. Within this group, the fibrillar collagens I, II, III, and V form characteristic "quarter-staggered" fibrils in connective tissues (for a review, see ref. 1). However, types IV, VI, VII, VIII, IX, and X collagens do not form these kinds of fibrils and have molecular structures distinct from those of fibrillar collagens. We have isolated genes encoding the polypeptides of types IX and X collagens, and we have found that the genes for these two "short-chain" collagens also have an exon structure that is clearly distinct from that of fibrillar collagen genes (2, 3).Although the function of type IX collagen in extracellular matrices is not known, some intriguing structural characteristics of this collagen are known. First, the molecules do not contain one long triple-helical domain like fibrillar collagens but instead are composed of three triple-helical domains interspersed with noncollagenous domains (4). Second, type IX collagen contains a sulfated glycosaminoglycan side-chain covalently attached to the polypeptide subunit designated the a2(IX) chain. This gives type IX collagen a proteoglycan character (5-8).cDNA probes corresponding to the al(IX) and a2(IX) chains (9,10) have been used to demonstrate that type IX collagen mRNAs are expressed in a tissue-specific manneri.e., they are expressed by chicken embryo chondrocytes but not by chicken embryo fibroblasts (9, 11). However, tendon fibroblasts do contain mRNAs capable of synthesizing bacterial collagenase-sensitive polypeptides that are similar in size to type IX polypeptides (11). To explore the nature of these polypeptides in detail, we have screened a cDNA library constructed from tendon fibroblast mRNA for the presence of collagenous coding sequences. Here we report on the isolation and characterization of one such clone, pMG377. Nucleotide sequence analysis reveals that the clone encodes a collagenous polypeptide that is homologous to, yet distinctly different from, type IX collagen polypeptides synthesized by chondrocytes. The structure of the conceptual translation product of pMG377 is different from that of collagens I-X and type XI (la, 2a.) chains. Therefore, we have given the type IX-like collagen chain encoded by pMG377 the designation al(XII). Ribonuclease protection assays using cRNA derived from pMG377 as probe show that al(XII) mRNA is present in several tissues, such as...

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Section: Resultsmentioning

confidence: 98%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Type XII collagen: distinct extracellular matrix component discovered by cDNA cloning.

Gordon¹,

Gerecke²,

Olsen³

1987

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

Self Cite

127

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“…The amino-terminal NC4 region of the a1 chain of type IX collagen from cartilage is a large (266 amino acids) globular domain (Ninomiya and Olsen, 1984;Vasios et al, 1988); NC4 of the other two chains are short peptides. In some other tissues, the large NC4 domain is missing, having been replaced by a short peptide similar to those in the a2(IX) and a3(IX) chains (Hayashi et al, 1992;Brewton et al, 1991;Nishimura et al, 1989).…”

Section: Molecular Isoformsmentioning

confidence: 99%

Analysis of transcriptional isoforms of collagen types IX, II, and I in the developing avian cornea by competitive polymerase chain reaction

Fitch

Gordon

Gibney

et al. 1995

Developmental Dynamics

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The genes for the al(IX), al(II), and a2(I) collagen chains can give rise to different isoforms of mRNA, generated by alternative promotor usage [for al(1X) and &?(I)] or alternative splicing [for cyl(II)]. In this study, we employed competitive reverse transcriptase PCR to quantitate the amounts of transcriptional isoforms for these genes in the embryonic avian cornea from its inception (about 3 1/2 days of development) to 11 days. In order to compare values at different time points, the results were normalized to those obtained for the "housekeeping" enzyme, glycerol-3-phosphate dehydrogenase (G3PDH). These values were compared to those obtained from other tissues (anterior optic cup and cartilage) that synthesize different combinations of the collagen isoforms. We found that, in the cornea, transcripts from the upstream promotor of al(1X) collagen (termed "long IX") were predominant at stage 18-20 (about 3 1/2 days), but then fell rapidly, and remained at a low level. By 5 days (just before stromal swelling) the major mRNA isoform of al(1X) was from the downstream promotor (termed "short IX"). The relative amount of transcript for the short form of type IX collagen rose to a peak at about 6 days of development, and then declined. Throughout this period, the predominant transcriptional isoform of the collagen type I1 gene was IIA (i.e., containing the alternatively spliced exon 2). This indicates that the molecules of type I1 collagen that are assembled into heterotypic fibrils with type I collagen possess, at least transiently, an amino-terminal globular domain similar to that found in collagen types I, 111, and V. For type I, the "bone/tendon" mRNA isoform of the cy2(I) collagen gene was predominant; transcripts from the downstream promotor were at basal levels. In other tissues expressing collagen types IX and 11, long IX was expressed predominantly with the IIA form in the anterior optic cup at stage 22/23; in 14 112 day cartilage, long IX was expressed predominantly along with the IIB form of al(1I). The downstream transcript of the a2(I) gene (Icart) was found at high levels only in cartilage.

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“…However, the minor 10,000-base RNA detected in chondrocytes has not been observed in any other cell type or with any other collagen probe (including those for the types II and III collagen genes) (16). Furthermore, no RNA of this size has been observed with a probe for type IX collagen, one of the minor cartilage collagens (34). Thus if the 10,000-base RNA represents cross-hybridization to another collagen RNA, it must be one of those for which probes are not yet available.…”

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confidence: 95%

Control of types I and II collagen and fibronectin gene expression in chondrocytes delineated by viral transformation.

Allebach¹,

Boettiger²,

Pacifici³

et al. 1985

Mol. Cell. Biol.

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We have analyzed the effects of transformation by Rous sarcoma virus on expression of types I and II collagen and fibronectin genes in vertebral chondrocytes and compared them with expression of these genes in skin fibroblasts. Transformed chondrocytes display a dramatically decreased amount of type II collagen RNA, which can account fully for the decreased synthetic rate of this protein. Paradoxically, these cells also display greatly increased amounts of type I collagen RNAs, which are translated efficientlv in vitro, but not in the intact cells. We show here that the type I collagen RNAs in transformed chondrocytes are nearly indistinguishable from those found in skin fibroblasts, and that they clearly differ from the type I collagen RNAs found in normal chondrocytes. Transformed chondrocytes also display an increased amount of fibronectin RNA, which can account fully for the increased synthetic rate of this protein. Thus, the effects of transformation by Rous sarcoma virus on type I collagen and fibronectin RNAs in chondrocytes are the opposite of those observed in fibroblasts, which display decreased amounts of these three RNAs. These data indicate that the effects of transformation on the genes encoding type I collagen and fibronectin must be modulated by host cell-specific factors. They also imply that the types I and II collagen genes may be regulated by different mechanisms, the type I genes being controlled at both transcriptional and posttranscriptional levels, and the type II gene being controlled primarily at the transcriptional level.Transformation of differentiated cells by tumor viruses has provided a useful tool for analyzing the mechanisms of cellular gene expression. This has been particularly true for the genes encoding extracellular matrix proteins, whose expression is decreased by transformation with certain viruses. For example, transformation of chicken embryo fibroblasts by Rous sarcoma virus (RSV) results in reduced synthesis of type I collagen (10,20,25,(45)(46)(47) and, in some cases, fibronectin (36,39). Similarly, transformation of chicken vertebral chondrocytes by RSV results in decreased synthesis of type II collagen and the major cartilage proteoglycan (2,18,37,38). The reduced rates of synthesis of type I collagen and fibronectin in transformed fibroblasts reflect decreased amounts of the corresponding RNAs (1, 3. 15,19,43,45,46,51) These data demonstrate that transformation by RSV has opposite effects on the expression of type I collagen and fibronectin genes in chondrocytes and fibroblasts and imply that the action of src is modulated by host cell factors that differ between these cell types. They also imply that the types I and II collagen genes may be regulated by different mechanisms. The genes encoding type I collagen, a protein which is synthesized by many cell types, appear to be regulated at both transcriptional and posttranscriptional levels. In contrast, the type II collagen gene, which is expressed only by a very limited number of terminally differentiated cell type...

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Synthesis and characterization of cDNA encoding a cartilage-specific short collagen.

Cited by 125 publications

References 34 publications

Type XII collagen: distinct extracellular matrix component discovered by cDNA cloning.

Type XII collagen: distinct extracellular matrix component discovered by cDNA cloning.

Analysis of transcriptional isoforms of collagen types IX, II, and I in the developing avian cornea by competitive polymerase chain reaction

Control of types I and II collagen and fibronectin gene expression in chondrocytes delineated by viral transformation.

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