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Galectin-3 is a nuclear matrix protein which binds RNA
L Wang1, H Inohara, K J Pienta
1Tumor Progression and Metastasis, karmanos Cancer Institute, Detroit, MI 48201, USA.
Biochemical and Biophysical Research Communications
|December 5, 1995
Summary
Galectin-3, a protein, binds to RNA and single-stranded DNA within the cell nucleus. This interaction occurs independently of its known carbohydrate-binding function, suggesting a novel role in nuclear processes.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Galectin-3 is an endogenous carbohydrate-binding protein found in the cytoplasm and on the cell surface.
- It functions as a receptor for poly-N-acetyllactosamine sequences and is implicated in nuclear processes like pre-mRNA splicing.
- Limited information exists regarding galectin-3's specific nuclear localization and binding partners.
Purpose of the Study:
- To investigate the nuclear localization of galectin-3.
- To identify the ligands galectin-3 binds to within the nucleus.
- To determine the mechanism of galectin-3's interaction with nuclear components.
Main Methods:
- Association of galectin-3 with the nuclear matrix (RNA-protein skeleton).
- Binding assays to assess interactions with single-stranded DNA (ssDNA) and RNA.
- Determination of binding affinity and evaluation of lactose's inhibitory effect.
Main Results:
- Galectin-3 was found to be associated with the nuclear matrix.
- Direct binding of galectin-3 to both ssDNA and RNA was demonstrated, with a binding affinity of 2.3 microM.
- Lactose did not inhibit galectin-3 binding to ssDNA or RNA, and poly(A) ribonucleotide homopolymers showed the highest affinity.
Conclusions:
- Galectin-3 interacts with the nuclear matrix.
- Galectin-3 functions as an RNA-binding protein in the nucleus.
- This nuclear RNA-binding activity is independent of galectin-3's known carbohydrate-binding function.