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Cell surface interaction of annexin A2 and galectin-3 modulates epidermal growth factor receptor signaling in Her-2 negative breast cancer cells

Overview of attention for article published in Molecular and Cellular Biochemistry, October 2015
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Title
Cell surface interaction of annexin A2 and galectin-3 modulates epidermal growth factor receptor signaling in Her-2 negative breast cancer cells
Published in
Molecular and Cellular Biochemistry, October 2015
DOI 10.1007/s11010-015-2584-y
Pubmed ID
Authors

Praveenkumar Shetty, Anil Bargale, Basavraj R. Patil, Rajashekar Mohan, U. S. Dinesh, Jamboor K. Vishwanatha, Pramod B. Gai, Vidya S. Patil, T. S. Amsavardani

Abstract

Overexpression and activation of tyrosine kinase receptors like EGFR and Src regulate the progression and metastasis of Her-2 negative breast cancer. Recently we have reported the role of cell membrane interaction of phospholipid-binding protein annexin A2 (AnxA2) and EGFR in regulating cellular signaling in the activation of angiogenesis, matrix degradation, invasion, and cancer metastasis. Beta-galactoside-specific animal lectin galectin-3 is an apoptosis inhibitor, and cell surface-associated extracellular galectin-3 also has a role in cell migration, cancer progression, and metastasis. Similar expression pattern and membrane co-localization of these two proteins made us to hypothesize in the current study that galectin-3 and AnxA2 interaction is critical for Her-2 negative breast cancer progression. By various experimental analyses, we confirm that glycosylated AnxA2 at the membrane surface interacts with galectin-3. N-linked glycosylation inhibitor tunicamycin treatment convincingly blocked AnxA2 membrane translocation and its association with galectin-3. To analyze whether this interaction has any functional relevance, we tried to dissociate this interaction with purified plant lectin from chickpea (Cicer arietinum agglutinin). This highly specific 30 kDa plant lectin could dissociate AnxA2 from endogenous lectin galectin-3 interaction at the cell surface. This dissociation could down-regulate Bcl-2 family proteins, cell proliferation, and migration simultaneously triggering cell apoptosis. Targeting this interaction of membrane surface glycoprotein and its animal lectin in Her-2 negative breast cancer may be of therapeutic value.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 16 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 16 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 5 31%
Professor > Associate Professor 3 19%
Researcher 2 13%
Librarian 1 6%
Professor 1 6%
Other 3 19%
Unknown 1 6%
Readers by discipline Count As %
Medicine and Dentistry 4 25%
Biochemistry, Genetics and Molecular Biology 3 19%
Agricultural and Biological Sciences 3 19%
Pharmacology, Toxicology and Pharmaceutical Science 1 6%
Immunology and Microbiology 1 6%
Other 3 19%
Unknown 1 6%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 07 October 2015.
All research outputs
#20,293,238
of 22,829,683 outputs
Outputs from Molecular and Cellular Biochemistry
#1,802
of 2,304 outputs
Outputs of similar age
#232,814
of 277,499 outputs
Outputs of similar age from Molecular and Cellular Biochemistry
#18
of 30 outputs
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