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Evidence for a lactose-mediated association between two nuclear carbohydrate-binding proteins
A P Sève1, M Felin, M A Doyennette-Moyne
1Laboratoire de Glycobiologie et de Reconnaissance Cellulaire, INSERM U180, UFR Biomédicale des Saints-Pères, Paris, France.
Glycobiology
|February 1, 1993
Summary
Nuclear proteins CBP35 and CBP70 were identified in HL60 cells. These proteins interact via lactose, suggesting a role in mRNA processing and nuclear function.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- HL60 cell nuclei bind neoglycoproteins with glucosyl and galactosyl residues.
- Nuclear proteins were extracted from HL60 cell nuclei.
Purpose of the Study:
- To identify nuclear proteins in HL60 cells that bind to glucose, galactose, or lactose.
- To investigate the interaction between identified nuclear proteins.
Main Methods:
- Affinity chromatography using immobilized glucose, galactose, and lactose.
- SDS-PAGE for polypeptide separation.
- Immunoblotting with specific antibodies against CBP67, CBP35, and L14.
Main Results:
- HL60 cell nuclei contain CBP35 and a 70 kDa glucose-binding lectin (CBP70).
- CBP35 associates with CBP70 through lactose-dependent interactions.
- Evidence suggests CBP35 and CBP70 interact via protein-protein binding.
Conclusions:
- CBP35 and CBP70 are nuclear proteins in HL60 cells.
- Lactose mediates an interaction between CBP35 and CBP70.
- This interaction may be involved in mRNA processing, as CBP35 is implicated in in vitro mRNA splicing and lactose inhibits pre-RNA processing.