Mistletoe lectin binds to multidrug resistance-associated protein MRP5.

Abstract:

BACKGROUND:Mistletoe lectins (MLs) are the active components of aqueous mistletoe extracts widely used in complementary cancer therapy, however, it is not clear if they bind to carbohydrate residues only or whether they interact with proteins as well. Protein-protein interactions do not seem unlikely as MLs act at very low molar concentrations usually observed with peptide-peptide interactions only and not seen with lectin-sugar interactions. MATERIALS AND METHODS:In order to detect protein-protein interactions a random peptide library was screened for the ability to bind to MLs. RESULTS:MLs bound to peptides showing homologies to multidrug resistance-associated protein 5 (MRP5). However, the MLs only slightly modified the MRP5 efflux pump, while periodate treatment to inhibit cell membrane binding via glycan completely abolished the ML-I binding sites in MRP5 overexpressing cells. CONCLUSION:The protein sequence is not important for ML-I binding, indicating that the biological activity of MLs can most likely be attributed to the sugar chains.

journal_name

Anticancer Res

journal_title

Anticancer research

authors

Nehmann N,Schade UM,Pfüller U,Schachner M,Schumacher U

subject

Has Abstract

pub_date

2009-12-01 00:00:00

pages

4941-8

issue

12

eissn

0250-7005

issn

1791-7530

pii

29/12/4941

journal_volume

29

pub_type

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