Human cDNA clones transcribed from an unusually high-molecular-weight RNA encode a new collagen chain

Myers, Jeanne C.; Sun, Mae Jane; D'Ippolito, Joseph A.; Jabs, Ethylin Wang; Dion, Arnold S.

doi:10.1016/0378-1119(93)90126-n

Cited by 34 publications

(34 citation statements)

References 15 publications

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“…Cloning, Expression, and Purification of NC2, (GPP) 10 NC2, and NC2(GPP) 10 -To facilitate expression and folding of short peptides containing the NC2 domain of human collagen XIX, they were cloned as part of fusion molecules with a His-tagged minifibritin that has a thrombin cleavage site (HT-mf-thr). Minifibritin is an obligatory trimer with both its amino and carboxyl termini exposed to solvent.…”

Section: Synthesis and Purification Of Reduced Nc1-containingmentioning

confidence: 99%

“…The NC2 domain was PCR-amplified using two oligonucleotides: 5Ј-TGCAGATCTCCGGCTGATGCA-GTTTCATTTGAA-3Ј (forward primer fNC2; the BglII site is underlined) and 5Ј-GTCAGTCGACTTAGCCATAAGCTTG-GGCAGCCAACATT-3Ј (reverse primer rNC2; the SalI site is underlined). Two other constructs for (GPP 10 )NC2 and NC2(GPP) 10 were PCR-amplified in two steps. The DNA fragment coding (GPP 10 )NC2 was prepared as follows.…”

Section: Synthesis and Purification Of Reduced Nc1-containingmentioning

confidence: 99%

“…The DNA fragment coding (GPP 10 )NC2 was prepared as follows. A synthetic oligonucleotide coding for (GPP) 10 (5Ј-GGTCCGCCTGGCC-CACCGGGCCCGCCCGGTCCGCCGGGCCCGCCGGGT-CCCCCAGGTCCGCCCGGCCCGCCGGGCCCTCCGGGT-CCACCG-3Ј) was used as a template to amplify the (GPP) 10 part, including a complementary end for the NC2 domain, using two oligonucleotides, 5Ј-TCAGGATCCGGTCCGCCT-GGCCCACCGGGC-3Ј (forward primer fGPP; the BamHI cloning site is underlined) and 5Ј-TTCAAATGAAACTGC-ATCAGCCGGAATCCCGGGTGGACCCGGAGGGCCC-GGC-3Ј (reversed primer; one half of it is complementary to the end of (GPP) 10 , and the other half is complementary to the beginning of the NC2 domain). The product of this PCR was purified and used together with the plasmid containing the NC2 domain sequence as a complex annealed template to PCRamplify the (GPP 10 )NC2 fragment using two oligonucleotides: fGPP and rNC2.…”

Section: Synthesis and Purification Of Reduced Nc1-containingmentioning

confidence: 99%

“…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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Section: Synthesis and Purification Of Reduced Nc1-containingmentioning

confidence: 99%

Section: Synthesis and Purification Of Reduced Nc1-containingmentioning

confidence: 99%

Section: Synthesis and Purification Of Reduced Nc1-containingmentioning

confidence: 99%

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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 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). The coding region of the ␣1(XIX) mRNA is small compared with the length of the entire transcript (10.4 kb), due to the presence of more than 5-kb long 3Ј-untranslated region.…”

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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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Embryonic expression of type XIX collagen is transient and confined to muscle cells

et al. 2001

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Plants have been used to produce many diverse and valuable recombinant proteins, including subunit vaccines, antibodies and antibody fragments, hormones, blood products, cytokines, and enzymes. Different plant species and platforms have been explored as production hosts, each with unique properties in terms of the gene transfer method, production time, environmental containment, scalability, downstream processing strategy, protein folding and accumulation, and overall costs. Seed‐based systems have many advantages because they exploit the natural storage properties of seeds, which facilitate batch processing and distribution. Seeds possess specialized storage organelles that may be used to accumulate recombinant proteins, offering stability both in planta and after harvest in the final preparation/formulation. The post‐harvest stabilizing effect of seeds allows recombinant subunit vaccines and antibodies to be delivered via the mucosal route because they are better able to withstand this harsh microenvironment when protected by the plant matrix. Native storage organelles such as starch granules and protein bodies offer this protective effect, but protein storage organelles can also be induced ectopically in vegetative tissues. In this paper, we discuss the technical capabilities of storage organelle‐based expression platforms and their potential applications.

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Human cDNA clones transcribed from an unusually high-molecular-weight RNA encode a new collagen chain

Cited by 34 publications

References 15 publications

Trimerization and Triple Helix Stabilization of the Collagen XIX NC2 Domain

Trimerization and Triple Helix Stabilization of the Collagen XIX NC2 Domain

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

Embryonic expression of type XIX collagen is transient and confined to muscle cells

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