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Prion protein expression in human leukocyte differentiation
1Department of Microbiology and Immunology, Montreal Neurological Institute and Hospital, McGill University, Montreal, Québec, Canada.
Blood
|March 21, 1998
Summary
Prion protein (PrPC) is found on human bone marrow stem cells and peripheral blood cells. Its expression decreases during granulocyte differentiation, suggesting these cells may support prion replication.
Area of Science:
- Immunology
- Neuroscience
- Cell Biology
Background:
- The cellular prion protein (PrPC) is a cell surface glycoprotein implicated in prion disease pathogenesis.
- PrPC is attached to the plasma membrane via a glycosylphosphatidylinositol anchor.
- Understanding PrPC expression is crucial for prion disease research.
Purpose of the Study:
- To characterize PrPC expression patterns during human leukocyte maturation.
- To investigate the role of PrPC in different hematopoietic lineages.
- To establish a model for studying PrP gene regulation.
Main Methods:
- Flow cytometry using monoclonal antibodies against PrPC, CD15, and CD34.
- Analysis of PrPC expression on bone marrow stem cells and differentiating leukocytes.
- In vitro differentiation of HL-60 cells using retinoic acid.
Main Results:
- PrPC is expressed on CD34+ bone marrow stem cells.
- Lymphocytes and monocytes retain PrPC expression during differentiation.
- PrPC expression is downregulated during granulocyte differentiation, confirmed in HL-60 cells.
- Retinoic acid treatment reduces PrPC mRNA and protein levels in HL-60 cells.
Conclusions:
- Selected bone marrow and peripheral mononuclear cells may support prion agent replication due to PrPC availability.
- Retinoic acid-induced PrPC downregulation in HL-60 cells offers a model for studying PrP gene regulation and function.
- Cell-specific PrPC glycoforms may influence cellular susceptibility to prion infection.