Cloning and expression of a type IX-like collagen in tissues of the ascidian Ciona intestinalis. (Articolo in rivista)

Type
Label
  • Cloning and expression of a type IX-like collagen in tissues of the ascidian Ciona intestinalis. (Articolo in rivista) (literal)
Anno
  • 2002-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/S0167-4781(02)00403-7 (literal)
Alternative label
  • Vizzini A., Arizza V., Cervello M., Cammarata M., Gambino R., Parrinello N. (2002)
    Cloning and expression of a type IX-like collagen in tissues of the ascidian Ciona intestinalis.
    in Biochimica et biophysica acta, N. Gene structure and expression (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Vizzini A., Arizza V., Cervello M., Cammarata M., Gambino R., Parrinello N. (literal)
Pagina inizio
  • 38 (literal)
Pagina fine
  • 44 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 1577 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Animal Biology, University of Palermo, via Archirafi 18, 90123 Palermo, Italy Institute of Developmental Biology, C.N.R., via Ugo la Malfa 153, 90146 Palermo, Italy (literal)
Titolo
  • Cloning and expression of a type IX-like collagen in tissues of the ascidian Ciona intestinalis. (literal)
Abstract
  • Collagens are highly preserved proteins in invertebrates and vertebrates. To identify the collagens in urochordates, the total RNA extracted from the pharynx of the ascidian Ciona intestinalis was hybridized with a heterologous probe specific for the echinoderm Paracentrotus lividus fibrillar type I-like larval collagen. Using this probe, two main bands (i.e. 6 and 2.8 kb mRNA) were observed on Northern blot hybridization. The cDNA library prepared from poly(A)+RNA extracted from pharyngeal tissue was screened and a cDNA that specifies a type IX-like collagen was identified. This molecule presents a conceptual open reading frame for a protein containing 734 amino acids. In particular, we showed a 1 alpha chain type IX-like collagen characterized by three short triple-helical domains interspersed with four non-triple-helical sequences, with structural features of fibril-associated collagens with interrupted triple- helices (FACIT) collagens. Northern blot hybridizations indicate a 2.8 kb transcript size. Sequence comparison indicated homology (47.64%, 48.95%) between the type IX-like collagen of C. intestinalis and mouse and human type IX collagen. In situ hybridization of tunic and pharynx tissues shows the presence of transcripts in connective tissue cells. (literal)
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