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Galectin-3 expression in human papillary thyroid carcinoma
Phannee Sawangareetrakul1, Chantragan Srisomsap, Daranee Chokchaichamnankit
1Laboratory of Biochemistry, Chulabhorn Research Institute, Bangkok 10210, Thailand.
Cancer Genomics & Proteomics
|May 8, 2008
Summary
Galectin-3, a protein elevated in papillary thyroid carcinoma, was purified and identified. Structural variations in galectin-3 were observed, suggesting potential post-translational modifications or proteolysis.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Galectin-3 expression is significantly increased in papillary thyroid carcinoma (PTC).
- Understanding galectin-3's structure is crucial for its role in PTC.
Purpose of the Study:
- To partially purify and characterize galectin-3 from PTC.
- To investigate potential structural variations of galectin-3 in PTC.
Main Methods:
- Affinity chromatography using lactose-agarose for galectin-3 purification.
- SDS-PAGE and Western blotting with N-terminal and C-terminal galectin-3 antibodies.
- Liquid chromatography/mass spectrometry/mass spectrometry (LC/MS/MS) for protein identification.
- N-terminal amino acid sequencing.
Main Results:
- Seven protein bands identified as galectin-3 (16-31 kDa) using LC/MS/MS.
- Differential reactivity with C-terminal antibody observed among galectin-3 bands.
- N-terminal sequencing revealed blocked N-termini in three bands and distinct starting positions (Gly35, Gly65, Ala100) in others.
- A 20 kDa band showed strong reactivity with the C-terminal antibody.
Conclusions:
- PTC-derived galectin-3 exhibits structural heterogeneity.
- Observed variations may result from N-terminal blocking, proteolysis, or post-translational modifications.
- Further research is needed to elucidate the precise nature of these galectin-3 structural differences.
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