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Breaking barriers: How modified citrus pectin inhibits galectin-8
Ming Shuai1,2, Yiqing Li1,2, Fanqi Guan1,2
1Department of Laboratory Medicine, Affiliated Hospital of Zunyi Medical University, Zunyi, Guizhou, 563003, China. zhangt760@hotmail.com.
Food & Function
|April 10, 2024
Summary
Modified citrus pectin (MCP) fractions, particularly MCP-30-3, can bind to galectin-8, suggesting a new role for pectin in modulating cancer metastasis and functional food development.
Area of Science:
- Biochemistry
- Glycobiology
- Cancer Research
Background:
- Modified citrus pectin (MCP) is known to inhibit galectin-3, a key factor in cancer metastasis.
- The potential of MCP to antagonize galectin-8 function has not been previously investigated.
Purpose of the Study:
- To investigate if MCP can bind to galectin-8.
- To characterize the structure-function relationship of MCP fractions interacting with galectin-8.
Main Methods:
- Isolation of MCP fractions using ethanol precipitation and ion-exchange chromatography.
- Assessment of galectin-8 binding activity and determination of minimum inhibitory concentration (MIC).
- Structural analysis of the active component MCP-30-3 and evaluation of enzymatic hydrolysis impact.
Main Results:
- MCP-30-3, a 168 kDa fraction, was isolated and characterized.
- MCP-30-3 demonstrated specific binding to galectin-8 with an MIC of 0.04 mg/mL.
- Hydrolysis of MCP-30-3 by β-galactosidase or pectinase significantly reduced its binding activity.
Conclusions:
- Modified citrus pectin (MCP) can bind to galectin-8, expanding its known biological activities.
- The specific structure of MCP-30-3 is crucial for its galectin-8 binding.
- These findings highlight the potential of MCP in functional foods and as an anti-metastatic agent.
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