Mistletoe lectin binds to multidrug resistance-associated protein MRP5

Nina Nehmann, Ulrika M. Schade, U. W.E. Pfuller, Melitta Camartin, U. D.O. Schumacher

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)4941-4948
Number of pages8
JournalAnticancer Research
Volume29
Issue number12
StatePublished - Dec 1 2009
Externally publishedYes

Fingerprint

Mistletoe
Multidrug Resistance-Associated Proteins
Lectins
Proteins
Peptides
Peptide Library
Complementary Therapies
Polysaccharides
Binding Sites
Carbohydrates
Cell Membrane

All Science Journal Classification (ASJC) codes

  • Oncology
  • Cancer Research

Cite this

Nehmann, N., Schade, U. M., Pfuller, U. W. E., Camartin, M., & Schumacher, U. D. O. (2009). Mistletoe lectin binds to multidrug resistance-associated protein MRP5. Anticancer Research, 29(12), 4941-4948.
Nehmann, Nina ; Schade, Ulrika M. ; Pfuller, U. W.E. ; Camartin, Melitta ; Schumacher, U. D.O. / Mistletoe lectin binds to multidrug resistance-associated protein MRP5. In: Anticancer Research. 2009 ; Vol. 29, No. 12. pp. 4941-4948.
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Nehmann, N, Schade, UM, Pfuller, UWE, Camartin, M & Schumacher, UDO 2009, 'Mistletoe lectin binds to multidrug resistance-associated protein MRP5', Anticancer Research, vol. 29, no. 12, pp. 4941-4948.

Mistletoe lectin binds to multidrug resistance-associated protein MRP5. / Nehmann, Nina; Schade, Ulrika M.; Pfuller, U. W.E.; Camartin, Melitta; Schumacher, U. D.O.

In: Anticancer Research, Vol. 29, No. 12, 01.12.2009, p. 4941-4948.

Research output: Contribution to journalArticle

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AU - Nehmann, Nina

AU - Schade, Ulrika M.

AU - Pfuller, U. W.E.

AU - Camartin, Melitta

AU - Schumacher, U. D.O.

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N2 - 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.

AB - 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.

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Nehmann N, Schade UM, Pfuller UWE, Camartin M, Schumacher UDO. Mistletoe lectin binds to multidrug resistance-associated protein MRP5. Anticancer Research. 2009 Dec 1;29(12):4941-4948.