Sequence analysis of a full-length cDNA for the murine proα2(I) collagen chain: Comparison of the derived primary structure with human proα2(I) collagen

Phillips, Charlotte L.; Morgan, Alan L.; Lever, L W; Wenstrup, Richard J.

doi:10.1016/0888-7543(92)90065-z

Cited by 22 publications

(16 citation statements)

References 5 publications

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“…We assumed that rat tail tendon collagen is similar to mouse type I collagen, whose complete primary sequence is known (29,30). Based on the mouse sequence (␣1(I) chain: CA11_MOUSE, Swiss-Prot accession number P11087; and ␣2(I) chain: CA21_MOUSE, Swiss-Prot accession number Q01149), one expects an intact molecule to contain 14 tyrosines: 12 in telopeptides and 2 in the triple helical region of the ␣2(I) chain.…”

Section: Resultsmentioning

confidence: 99%

Does the Triple Helical Domain of Type I Collagen Encode Molecular Recognition and Fiber Assembly while Telopeptides Serve as Catalytic Domains?

Kuznetsova¹,

Leikin

1999

Journal of Biological Chemistry

108

104

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Over the last several decades, it has been established that proteolytic removal of short, non-helical terminal peptides (telopeptides) from type I collagen significantly alters the kinetics of in vitro fibrillogenesis. However, it has also been observed that the protein is still capable of forming fibers even after complete removal of telopeptides. This study focuses on the characterization of this fibrillogenesis competency of collagen. We have combined traditional kinetic and thermodynamic assays of fibrillogenesis efficacy with direct measurements of interaction between collagen molecules in fibers by osmotic stress and x-ray diffraction. We found that telopeptide cleavage by pepsin or by up to 20 h of Pronase treatment altered fiber assembly kinetics, but the same fraction of the protein still assembled into fibers. Small-angle x-ray diffraction showed that these fibers have normal, native-like D-stagger. Force measurements indicated that collagen-collagen interactions in fibers were not affected by either pepsin or Pronase treatment. In contrast, prolonged (>20 h) Pronase treatment resulted in cleavage of the triple helical domain as indicated by SDS-polyacrylamide gel electrophoresis. The triple-helix cleavage correlated with the observed decrease in the fraction of protein capable of forming fibers and with the measured loss of attraction between helices in fibers. These data suggest that telopeptides play a catalytic role, whereas the information necessary for proper molecular recognition and fiber assembly is encoded in the triple helical domain of collagen.Type I collagen is a major component of the extracellular matrix in all higher vertebrates, e.g. it is the main structural protein of skin, bone, and tendon (see, for example, Refs. 1 and 2). Each molecule is a heterotrimer composed of two ␣1(I) chains and one ␣2(I) chain. It contains a long triple helical domain (ϳ1000 residues from each chain) and short, non-helical terminal peptides (telopeptides).In vitro, under appropriate conditions, type I molecules spontaneously form fibers that are virtually indistinguishable from native fibers by electron microscopy (see, for example, Ref.3).X-ray diffraction patterns from such reconstituted fibers and from native fibers are similar as well (4 -7). It is commonly believed that type I collagen contains all structural information that is necessary for its self-assembly into fibers, except maybe for some tissue-specific factors (see, for example, Ref. 8). However, the location of the "coding" regions, the nature of this information, and how it is "translated" into intermolecular forces responsible for fibrillogenesis are still poorly understood.One of the debated issues is the role of telopeptides. Telopeptides form covalent cross-links with triple helical regions on opposing molecules (see, for example, Refs. 9 and 10). It is believed that this occurs after completion of fibrillogenesis and that the cross-links stabilize rather than create appropriate molecular arrangement. It was also suggested that telopept...

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Section: Resultsmentioning

confidence: 99%

Does the Triple Helical Domain of Type I Collagen Encode Molecular Recognition and Fiber Assembly while Telopeptides Serve as Catalytic Domains?

Kuznetsova¹,

Leikin

1999

Journal of Biological Chemistry

108

104

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“…Genomic DNA from blood and tumor specimens was used as the template in the PCR reaction. We used previously published primer sequences and PCR conditions as follows: 5'TCTTCATCCCTACGTATCACTAG-GCC3' and S'CACCCCATTCTCCGTCTGTC-CCCTTGC3' with incubation at 94°C for 5 min followed by 40 cycles of denaturation at 94°C for 1 min, primer annealing at 56°C for 1 min, and elongation at 72°C for 1 min (Phillips et al, 1992). A final elongation step at 72°C for 10 min completed the PCR.…”

Section: Methodsmentioning

confidence: 99%

Deletion of chromosome arm 17p dna sequences in pediatric high‐grade and juvenile pilocytic astrocytomas

Willert

Daneshvar

Sheffield

et al. 1995

Genes Chromosomes & Cancer

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In adults, loss of heterozygosity for DNA on 17p has been shown in high-grade anaplastic astrocytomas (AAs) and glioblastomas multiforme (GMs), and mutation of the TP53 tumor suppressor gene has been reported in all grades of astrocytomas. Little is known, however, about 17p deletion and TP53 mutation in juvenile pilocytic astrocytomas (JPAs), the most common low-grade tumors seen in children. To elucidate the genetic characteristics of pediatric high-grade astrocytomas and JPAs, we performed restriction fragment length polymorphism analysis with probes derived from 17p and TP53 mutational studies in 28 tumor specimens. Telomeric chromosome arm 17p markers 144-D6 and ABR were lost in 6 (75%) of 8 informative tumors classified as high-grade (7 AAs, 1 GM) and in 2 (10%) of 20 informative JPAs. Loss of 17p probes centromeric to the TP53 gene were also detected in 3 AAs and 5 JPAs. Four of the 6 (66%) JPAs with losses of 17p DNA sequences recurred rapidly despite aggressive therapy, whereas only 5 of the other 14 (36%) recurred. Mutation of the TP53 gene was detected by polymerase chain reaction and denaturing gradient gel electrophoresis in only 1 JPA and 1 AA. These tumors were also examined for MDM2 gene amplification as an alternate inactivation mechanism for TP53 gene function: no instances of alteration were identified. These results suggest that a gene or genes in addition to TP53 on 17p may be involved in the etiology or progression of high-grade astrocytomas and aggressive JPAs in children.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…RT of total RNA (2 lg) was performed in a final volume of 100 ll containing 19 TaqMan RT buffer, 5.5 mM MgCl 2 , 500 lM/L each deoxy-unspecified nucleoside 5 0 -triphsophate, 2.5 lM random hexamers, 0.4 U/ml RNase inhibitor, and 1.25 U/ml multiscribe RT. PCR primers for TGF-b1 [21], col1a2 [22], and b-actin [14] contained the following sequences: TGF-b1 sense (5 0 -AAAATCAAGTGTGGAGCAAC-3 0 ), and antisense (5 0 -CAAGAGACTTCCAGCCAGTTGC-3 0 ); col1a2 sense (5 0 -GGAACAGCGATTACTACTGG-3 0 ), and antisense (5 0 -TCTCCTAACCAGACATGCTT-3 0 ); b-actin sense (5 0 -TGGAATCCTGTGGCATCCATGAAAC-3 0 ), and antisense (5 0 -TAAAACGCAGCTCAGTAACAGTC CG-3 0 ).…”

Section: Determination Of Serum Alt Levelsmentioning

confidence: 99%

Dietary olive oil prevents carbon tetrachloride-induced hepatic fibrosis in mice

et al. 2009

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Sequence analysis of a full-length cDNA for the murine proα2(I) collagen chain: Comparison of the derived primary structure with human proα2(I) collagen

Cited by 22 publications

References 5 publications

Does the Triple Helical Domain of Type I Collagen Encode Molecular Recognition and Fiber Assembly while Telopeptides Serve as Catalytic Domains?

Does the Triple Helical Domain of Type I Collagen Encode Molecular Recognition and Fiber Assembly while Telopeptides Serve as Catalytic Domains?

Deletion of chromosome arm 17p dna sequences in pediatric high‐grade and juvenile pilocytic astrocytomas

Dietary olive oil prevents carbon tetrachloride-induced hepatic fibrosis in mice

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