Biochemical characterization of CA IX, one of the most active Carbonic Anhydrase isozymes. (Articolo in rivista)

Type
Label
  • Biochemical characterization of CA IX, one of the most active Carbonic Anhydrase isozymes. (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1074/jbc.M800938200 (literal)
Alternative label
  • Hilvo M; Baranauskiene L; Salzano AM; Scaloni A; Matulis D; Innocenti A;Scozzafava A; Monti SM; Di Fiore A; De Simone G; Lindfors M; Jänis J; Valjakka J; Pastoreková S; Pastorek J; Kulomaa MS; Nordlund HR; Supuran CT; Parkkila S. (2008)
    Biochemical characterization of CA IX, one of the most active Carbonic Anhydrase isozymes.
    in The Journal of biological chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Hilvo M; Baranauskiene L; Salzano AM; Scaloni A; Matulis D; Innocenti A;Scozzafava A; Monti SM; Di Fiore A; De Simone G; Lindfors M; Jänis J; Valjakka J; Pastoreková S; Pastorek J; Kulomaa MS; Nordlund HR; Supuran CT; Parkkila S. (literal)
Pagina inizio
  • 27799 (literal)
Pagina fine
  • 27809 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 283 (literal)
Rivista
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  • Pubblicazione su rivista internazionale (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Medical Technology and School of Medicine, University of Tampere and Tampere University Hospital, FI-33014 Tampere, Finland, the Laboratory of Biothermodynamics and Drug Design, Institute of Biotechnology, LT-02241 Vilnius, Lithuania, the Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, 80147 Naples, Italy, the ?Bioinorganic Chemistry Laboratory, University of Florence, 50019 Sesto Fiorentino (Florence), Italy, the Institute of Biostructures and Bioimages, National Research Council, 80134 Naples, Italy, the Department of Chemistry, University of Joensuu, FI-80101 Joensuu, Finland, the Centre of Molecular Medicine, Institute of Virology, Slovak Academy of Sciences, 84505 Bratislava, Slovak Republic (literal)
Titolo
  • Biochemical characterization of CA IX, one of the most active Carbonic Anhydrase isozymes. (literal)
Abstract
  • Carbonic anhydrase IX (CA IX) is an exceptional member of the CA protein family; in addition to its classical role in pH regulation, it has also been proposed to participate in cell proliferation, cell adhesion, and tumorigenic processes. To characterize the biochemical properties of this membrane protein, two soluble recombinant forms were produced using the baculovirus-insect cell expression system. The recombinant proteins consisted of either the CA IX catalytic domain only (CA form) or the extracellular domain, which included both the proteoglycan and catalytic domains (PG + CA form). The produced proteins lacked the small transmembrane and intracytoplasmic regions of CA IX. Stopped-flow spectrophotometry experiments on both proteins demonstrated that in the excess of certain metal ions the PG + CA form exhibited the highest catalytic activity ever measured for any CA isozyme. Investigations on the oligomerization and stability of the enzymes revealed that both recombinant proteins form dimers that are stabilized by intermolecular disulfide bond(s). Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures. Parallel experiments on a recombinant protein obtained by a mammalian cell expression system demonstrated the occurrence of an additional O-linked glycosylation site (Thr(78)) and characterized the nature of the oligosaccharide structures. This study provides novel information on the biochemical properties of CA IX and may help characterize the various cellular and pathophysiological processes in which this unique enzyme is involved. (literal)
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