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Human myeloid cell nuclear differentiation antigen binds specifically to nucleolin
1Department of Pathology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA.
Journal of Cellular Biochemistry
|December 1, 1995
Summary
The human myeloid cell nuclear differentiation antigen (MNDA) protein binds to nucleolin, a key nuclear protein. This interaction suggests MNDA
Area of Science:
- Molecular Biology
- Cell Biology
- Immunology
Background:
- The human myeloid cell nuclear differentiation antigen (MNDA) is a nuclear protein.
- MNDA is specifically expressed in myelomonocytic cells and regulated by interferon alpha.
- MNDA belongs to a family of interferon-regulated genes with unknown functions.
Purpose of the Study:
- To elucidate the function of MNDA by characterizing its protein binding activities.
- To identify proteins that specifically bind to MNDA.
Main Methods:
- Affinity purification
- Coimmunoprecipitation
- Protein blot assay
- Microsequence analysis
Main Results:
- MNDA specifically binds to the 100 kDa nucleolin protein.
- Nucleolin identification was confirmed using specific antibodies.
- MNDA possesses motifs potentially responsible for nucleolin binding.
Conclusions:
- MNDA's function is likely mediated through protein-protein interactions.
- MNDA may provide cell-specific regulation of ubiquitous proteins like nucleolin.
- Understanding MNDA binding is crucial for elucidating MNDA and related interferon-inducible gene functions.