Lactoferrin binding sites and nuclear localization in K562(S) cells

✍ Scribed by Cecilia Garré; Giovanna Bianchi-Scarrà; Mario Sirito; Marco Musso; Roberto Ravazzolo

• Book ID: 102882693
• Publisher: John Wiley and Sons
• Year: 1992
• Tongue: English
• Weight: 604 KB
• Volume: 153
• Category: Article
• ISSN: 0021-9541
• DOI: 10.1002/jcp.1041530306

✦ Synopsis

Lactoferrin, a single chain cationic glycoprotcin, present in the sccondary granules of neutrophils, acts as a negative feedback regulator of myelopoiesis. Specific receptors for lactoferrin were detected on the surface of different hematopoietic cell types. The influence of lactoferrin on cell growth in culture has been reported.

Interactions of lactoferrin with DNA were also demonstrated.

In the present paper we confirm the presence of lactoferrin specific binding sites on K562 cells and we estimate the number of binding site3 and the dissociation constant. By Western blotting analysis performed on K562 lysates wc find a band of about 120 kUa responsible for specific binding of lactoferrin. We also show that lactoferrin, after binding at the cell surface, is internalized in a temDerature detectable as a DNA-linked piotein in dependent way and is immunologicallv nuclear extracts.