TAILIEUCHUNG - Báo cáo khoa học: Characterization of a cathepsin L-associated protein in Artemia and its relationship to the FAS-I family of cell adhesion proteins

We reported previously that the major cysteine protease in embryos and larvaeof thebrine shrimp,Artemia franciscana, is a heterodimeric protein consisting of a catalytic subunit ( kDa) with a high degree of homology with cathep-sin L, and a noncatalytic subunit ( kDa) of unknown function. In the study reportedhere thenoncatalytic subunit, or cathepsin L-associated protein (CLAP), was separated from cathepsin L by chromatography on Mono S and found tocontainmultiple isoformswithpIs ranging to . Heterodimeric and monomeric cathepsin L showed similar activity between pH5 and , while the heterodimer was about twice as active as monomeric cathepsin L below pH 5 | Eur. J. Biochem. 271 4014-4025 2004 FEBS 2004 doi Characterization of a cathepsin L-associated protein in Artemia and its relationship to the FAS-I family of cell adhesion proteins Alden H. Warner1 Ervin Pullumbi1 Reinout Amons2 and Liqian Liu1 1 Department of Biological Sciences University of Windsor Windsor Ontario Canada department of Molecular Cell Biology Sylvius Laboratory Leiden the Netherlands We reported previously that the major cysteine protease in embryos and larvae of the brine shrimp Artemia franciscana is a heterodimeric protein consisting of a catalytic subunit kDa with a high degree of homology with cathepsin L and a noncatalytic subunit kDa of unknown function. In the study reported here the noncatalytic subunit or cathepsin L-associated protein CLAP was separated from cathepsin L by chromatography on Mono S and found to contain multiple isoforms with pIs ranging from to . Heterodimeric and monomeric cathepsin L showed similar activity between pH 5 and while the heterodimer was about twice as active as monomeric cathepsin L below pH 5. The heterodimer was more stable than the monomer between pH 6 and and at 30-50 C. Artemia CLAP and cathepsin L are present in nearly equimolar amounts at all stages in the life cycle and most abundant in encysted eggs and embyros. Moreover CLAP either free or as a complex with cathepsin L was resistant to hydrolysis by cathepsin L. Two clones coding for CLAP were isolated from an Artemia embryo cDNA library and sequenced. Both clones have nearly identical open reading frames but show differences at the 5 - and 3 -termini. Each cDNA clone has an extensive 3 -untranslated region containing 70-72 A T. The deduced amino acid sequence of CLAP cDNA revealed two domains which were very similar to domains in fasciclin I and other cell adhesion proteins. The nucleotide sequences of clones 1 and 2 have been entered into the NCBI database AY307377 and AY462276 . This .

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