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Carbohydrate sulfotransferases in lymphocyte homing
1Department of Respiratory Diseases, Roche Bioscience, Palo Alto, CA 94304-1397, USA.
Glycobiology
|September 16, 2000
Summary
Sulfation modifications, including Gal-6-SO4 and GlcNAc-6-SO4, are crucial for biological recognition, particularly in lymphocyte homing. Newly identified carbohydrate sulfotransferases play a key role in these essential processes.
Area of Science:
- Biochemistry
- Immunology
- Molecular Biology
Background:
- Sulfation is a vital post-translational modification involved in biological recognition events.
- Early research linked sulfation modifications on endothelial ligands to lymphocyte homing via L-selectin interactions.
Purpose of the Study:
- To investigate the specific sulfation modifications involved in L-selectin-mediated lymphocyte homing.
- To identify the molecular players responsible for generating these critical sulfation patterns.
Main Methods:
- Identification of a novel family of carbohydrate sulfotransferases.
- Reconstitution experiments to assess the function of these enzymes.
Main Results:
- Specific sulfation modifications, Galactose-6-sulfate (Gal-6-SO4) and N-acetylglucosamine-6-sulfate (GlcNAc-6-SO4), were confirmed on biological ligands.
- The identified sulfotransferase family was shown to be capable of generating these modifications.
Conclusions:
- The newly identified carbohydrate sulfotransferases are molecularly implicated in the generation of key sulfation modifications.
- These enzymes are critical for the process of lymphocyte homing.