http://www.cnr.it/ontology/cnr/individuo/prodotto/ID55758
Glycosylation enhances functional stability of the chemotactic cytokine CCL-2. (Articolo in rivista)
- Type
- Label
- Glycosylation enhances functional stability of the chemotactic cytokine CCL-2. (Articolo in rivista) (literal)
- Anno
- 2003-01-01T00:00:00+01:00 (literal)
- Alternative label
Ruggiero P., Flati S., Di Cioccio V., G. Maurizi G., Macchia G., Facchin A., Anacardio R., Maras B., Lucarelli M., Boraschi D. (2003)
Glycosylation enhances functional stability of the chemotactic cytokine CCL-2.
in European cytokine network (Montrouge)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Ruggiero P., Flati S., Di Cioccio V., G. Maurizi G., Macchia G., Facchin A., Anacardio R., Maras B., Lucarelli M., Boraschi D. (literal)
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- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Titolo
- Glycosylation enhances functional stability of the chemotactic cytokine CCL-2. (literal)
- Abstract
- The human chemokine CCL2 gene was expressed in the yeast P.pastoris and gave rise to a mixture of differently glycosylated recombinant proteins. In comparison to non-glycosylated E.coli-derived CCL2, glycosylated yeast CCL2L was 4-20 times less active in a chemotactic assay in vitro. However, CCL2L could maintain full activity upon prolonged incubation at 37°C, whereas the non-glycosylated chemokine readily lost activity. It could be hypothesized that glycosylation is a mechanism used by the organism to modulate CCL2 stability. The partial loss of specific activity due to glycosylation is balanced by the advantage of prolonging the effectiveness of chemokine. Thus, differential glycosylation allows one to obtain highly effective short-lived CCL2 or less-effective long-lived CCL2 and may thus represent a novel mechanism of adaptation to pathological vs. physiological conditions. (literal)
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