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Stage-specific Expression of a Schistosoma mansoniPolypeptide Similar to the Vertebrate Regulatory Protein Stathmin
Ist Teil von
The Journal of biological chemistry, 1999-11, Vol.274 (48), p.33869-33874
Ort / Verlag
American Society for Biochemistry and Molecular Biology
Erscheinungsjahr
1999
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
The ubiquitous vertebrate protein stathmin is expressed and phosphorylated in response to a variety of external and internal
signals. Stathmin, in turn, controls cell growth and differentiation through its capacity to regulate microtubule assembly
dynamics. This is the first report on the molecular cloning and characterization of a stathmin-like protein (SmSLP) in an
invertebrate, the human blood fluke Schistosoma mansoni. SmSLP is first synthesized at high levels in the intermediate molluscan host and completely disappears 48 h after penetration
into the mammalian host. The protein is preferentially iodinated in intact immature parasites using the Bolton-Hunter reagent,
can be quantitatively extracted in high salt buffers, and remains soluble after boiling. Native SmSLP was partially sequenced,
and its complete structure was derived from the cloning and sequencing of its cDNA. The sequence is up to 26% identical to
vertebrate stathmin sequences and contains two potential phosphorylation sites. Native SmSLP is indeed phosphorylated because
phosphatase digestion shifts its mobility in electrofocusing gels. SmSLP associates with tubulin, as suggested by immune co-precipitation
results. In vitro experiments demonstrated that SmSLP inhibits tubulin assembly and causes the depolymerization of preassembled microtubules,
thus probably fulfilling regulatory roles in critical steps of schistosome development.