Collagen Polymorphism: Characterization of Molecules with the Chain Composition [α1(III)]
            <sub>3</sub>
            in Human Tissues

Chung, Endy; Miller, Edward J.

doi:10.1126/science.183.4130.1200

Cited by 514 publications

(160 citation statements)

References 12 publications

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“…55,73 In contrast, fibrillar human collagens from native tissues have been reported to yield 42-54% hydroxylation, with variations dependent on tissue source, collagen type, and extraction method. 55,78,79 Although our levels of approximately 0.5% proline hydroxylation in S. cereVisiae strain InvSC1p4H are low relative to previously reported levels for this yeast, we observed 10-fold increases (to 4-6% hydroxylation) by altering the S. cereVisiae strain, hydroxylase gene copy numbers, and the plasmid system (see Supporting Information). Hydroxylation levels in the InvSC1p4H strain do not appear to be dependent on the source of the collagen gene, as these values are consistent regardless of whether the collagen gene is the native (COL3A1) or the modular collagen (MCol).…”

Section: Discussioncontrasting

confidence: 54%

Recombinant Human Collagen and Biomimetic Variants Using a De Novo Gene Optimized for Modular Assembly

et al. 2010

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A collagen-mimetic polymer that can be easily engineered with specific cell-responsive and mechanical properties would be of significant interest for fundamental cell-matrix studies and applications in regenerative medicine. However, oligonucleotide-based synthesis of full-length collagen has been encumbered by the characteristic glycine-X-Y sequence repetition, which promotes mismatched oligonucleotide hybridizations during de novo gene assembly. In this work, we report a novel, modular synthesis strategy that yields full-length human collagen III and specifically defined variants. We used a computational algorithm that applies codon degeneracy to design oligonucleotides that favor correct hybridizations while disrupting incorrect ones for gene synthesis. The resulting recombinant polymers were expressed in Saccharomyces cereVisiae engineered with prolyl-4-hydroxylase. Our modular approach enabled mixing-and-matching domains to fabricate different combinations of collagen variants that contained different secretion signals at the N-terminus and cysteine residues imbedded within the triple-helical domain at precisely defined locations. This work shows the flexibility of our strategy for designing and assembling specifically tailored biomimetic collagen polymers with re-engineered properties.

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Section: Discussioncontrasting

confidence: 54%

Recombinant Human Collagen and Biomimetic Variants Using a De Novo Gene Optimized for Modular Assembly

et al. 2010

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“…Identical studies were performed using the recently identified Type I11 collagen (chain composition [a 1(111)13), which has a tissue distribution similar to Type I collagen (17).…”

mentioning

confidence: 99%

Antibodies to native and denatured collagens in sera of patients with rheumatoid arthritis

Andriopoulos

Městecký

Miller

et al. 1976

Arthritis & Rheumatism

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190

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A passive hemagglutination akay was used to detect antibodies to native human collagens and to collagen chains in the sera of 110 rheumatoid patients and those of 75 normal controls. The incidence and titer of anticollagen antibodies in rheumatoid arthritis are high, but in controls they are low or in most instances absent. N o correlation was found between the stage of RA, or titers of rheumatoid factor, or ANA and the incidence and/or titers of antibody to any given type of collagen.Rheumatoid arthritis (RA) is a chronic disease with many features that suggest the implication of anti-

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“…This was true even for the collagens extracted without the use of pepsin, suggesting either that procollagen was not present in significant amounts in the culture medium or that it was subsequently converted to collagen during the extraction and/or purification procedures (20). The absence of Y-components would also indicate that Type III collagen was not synthesized in either control or BrdUrd-treated cultures, since the latter collagen is always isolated as y-or larger components (21).…”

Section: Resultsmentioning

confidence: 99%

Analysis of changes in collagen biosynthesis that occur when chick chondrocytes are grown in 5-bromo-2'-deoxyuridine.

Mayne¹,

Vail²,

Miller³

1975

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

136

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Chick embryo chondrocytes, in primary culture, initially synthesize only Type II collagen (chain composition, [al(II)J3), as judged by two criteria: (i) carboxymethylcellulose chromatography of the denatured collagen, and (ii) carboxymethyl-cellulose chromatography of the cyanogen bromide peptides derived from the isolated chains. After a period of growth in 5-bromo-2'-deoxyuridine, however, synthesis of two different types of collagen could be detected after differential salt precipitation of the newly synthesized native collagens from neutral salt solutions at 2.2 M NaCl and subsequently at 0.01 M Na2HPO4. By the criteria indicated above, the collagen precipitating at 2.2 M NaCI was identified as Type I collagen (chain composition, [al(I)Jsa2), whereas the collagen subsequently precipitated at 0.01 M Na2HPO4 was found to be comprised entirely of al(I) chains, indicating a chain composition, [al(I)13. We propose to designate the latter type of molecule as the Type I trimer.By careful selection of a culture medium, embryonic chick chondrocytes will maintain the cartilage phenotype in vitro for as many as 35 doublings (1). If, however, the cells are grown in media containing embryo extract (2, 3) or 5-bromo-2-deoxyuridine (BrdUrd) (4-7), or if a clone of chondrocytes is allowed to grow until there is loss of division capacity (8), the cells will flatten and lose their ability to accumulate metachromatic matrix. Such cells have been variously described as dedifferentiated, "altered," or fibroblast-like (8-10). When it was realized that the large amount of unsulfated glycosaminoglycan synthesized by chondrocyte cultures grown in embryo extract could be identified as hyaluronic acid (11, 12), it was proposed that any instability on the part of the chondrocyte phenotype might also be evident in the synthesis of collagen chains other than the al(II). chain. This collagen chain is a normal and specific gene product synthesized exclusively by cartilaginous structures (13,14). Previous chromatographic analyses of the collagen chains synthesized by control chondrocyte cultures and cultures grown in the presence of either embryo extract or BrdUrd strongly suggested that the cells normally elaborate al(II) chains (Type II collagen), but that in the presence of embryo extract or BrdUrd al(I) and a2 chains (Type I collagen) were synthesized as well (3,9).The present communication examines in greater detail both the collagen chains and the native collagens synthesized by chondrocytes grown in the presence of BrdUrd. The data indicate that there is a definite switch in collagen biosynthesis involving the cessation of Type II collagen synthesis, the initiation of Type I collagen synthesis, and the assembly of molecules comprised of only a1(I) chains.MATERIALS AND METHODS Materials. F-10 medium containing 2X amino acids and 2X pyruvate (F-10 2X), trypsin (2.5%), bovine serum albuAbbreviations: CM-cellulose, carboxymethyl-cellulose; CNBr, cyanogen bromide; BrdUrd, 5-bromo-2'-deoxyuridine. All cultures were fed daily for a...

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Collagen Polymorphism: Characterization of Molecules with the Chain Composition [α1(III)] ₃ in Human Tissues

Cited by 514 publications

References 12 publications

Recombinant Human Collagen and Biomimetic Variants Using a De Novo Gene Optimized for Modular Assembly

Recombinant Human Collagen and Biomimetic Variants Using a De Novo Gene Optimized for Modular Assembly

Antibodies to native and denatured collagens in sera of patients with rheumatoid arthritis

Analysis of changes in collagen biosynthesis that occur when chick chondrocytes are grown in 5-bromo-2'-deoxyuridine.

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Collagen Polymorphism: Characterization of Molecules with the Chain Composition [α1(III)] 3 in Human Tissues

Cited by 514 publications

References 12 publications

Recombinant Human Collagen and Biomimetic Variants Using a De Novo Gene Optimized for Modular Assembly

Recombinant Human Collagen and Biomimetic Variants Using a De Novo Gene Optimized for Modular Assembly

Antibodies to native and denatured collagens in sera of patients with rheumatoid arthritis

Analysis of changes in collagen biosynthesis that occur when chick chondrocytes are grown in 5-bromo-2'-deoxyuridine.

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Collagen Polymorphism: Characterization of Molecules with the Chain Composition [α1(III)] ₃ in Human Tissues