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

Abstract:

:Lactoferrin, a single chain cationic glycoprotein, present in the secondary 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 sites and the dissociation constant. By Western blotting analysis performed on K562 lysates we find a band of about 120 kDa responsible for specific binding of lactoferrin. We also show that lactoferrin, after binding at the cell surface, is internalized in a temperature dependent way and is immunologically detectable as a DNA-linked protein in nuclear extracts.

journal_name

J Cell Physiol

authors

Garré C,Bianchi-Scarrá G,Sirito M,Musso M,Ravazzolo R

doi

10.1002/jcp.1041530306

keywords:

subject

Has Abstract

pub_date

1992-12-01 00:00:00

pages

477-82

issue

3

eissn

0021-9541

issn

1097-4652

journal_volume

153

pub_type

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