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Decreased prion protein expression in human peripheral blood leucocytes from patients with paroxysmal nocturnal
J Dürig1, A Giese, U Schmücker
1Department of Haematology, University Hospital Essen, D-45122, Germany. duerig@t-online.de
Abstract:
The cellular isoform of the prion protein (PrPC) is a cell surface glycoprotein attached to the outer leaflet of the plasma membrane by a glycosylphosphatidyl-inositol (GPI) anchor. PrPC is involved in the pathogenesis of prion diseases and has recently been shown to play a role in haemopoietic cell activation and proliferation. We have used the PrPC-specific monoclonal antibody (mAb) 3F4 in a flow cytometry approach to analyse the constitutive expression of PrPC on human peripheral blood (PB) cell populations from patients with paroxysmal nocturnal haemoglobinuria (PNH), which are characterized by a deficiency of GPI-linked cell surface proteins. Comparable PrPC expression levels (P > 0.05), quantified as mean fluorescent intensity, were measured on lymphocytes isolated from normal donors (n = 10) and patients with PNH (n = 5), whereas PNH PB monocytes and granulocytes exhibited substantially lower PrPC surface immunoreactivity than their normal counterparts (P < 0.05). More detailed histogram analyses of the PNH PB leucocytes revealed that PrPC was absent in PNH granulocytes, but was normally expressed in lymphocytes from four out of five patients. However, in one patient a bimodal distribution of 3F4 mAb staining was observed, indicating the presence of a PrPC-deficient lymphocyte subpopulation. In conclusion, our results show that PNH haemopoietic cells are deficient in cell surface-bound PrPC.
Insights
This study reveals that patients with paroxysmal nocturnal haemoglobinuria (PNH) exhibit reduced cell surface prion protein (PrPC) expression on monocytes and granulocytes. Lymphocytes showed comparable PrPC levels, though some PNH patients had PrPC-deficient lymphocyte subpopulations.
Area of Science:
- Biochemistry
- Immunology
- Cell Biology
Background:
- The cellular prion protein (PrPC) is a GPI-anchored glycoprotein on the cell surface.
- PrPC plays roles in cell activation, proliferation, and prion disease pathogenesis.
- Paroxysmal nocturnal haemoglobinuria (PNH) is characterized by deficiencies in GPI-linked proteins.
Purpose of the Study:
- To investigate PrPC expression on peripheral blood cells from PNH patients.
- To compare PrPC levels in PNH cells versus normal controls.
- To identify potential alterations in PrPC expression patterns in PNH.
Main Methods:
- Utilized the PrPC-specific monoclonal antibody (mAb) 3F4.
- Employed flow cytometry to analyze PrPC surface expression.
- Quantified PrPC levels using mean fluorescent intensity and histogram analysis.
Main Results:
- PNH monocytes and granulocytes showed significantly lower PrPC surface immunoreactivity compared to normal controls.
- PrPC was absent on PNH granulocytes.
- Lymphocytes from most PNH patients displayed normal PrPC expression, but one patient had a PrPC-deficient lymphocyte subpopulation.
Conclusions:
- PNH haemopoietic cells demonstrate a deficiency in cell surface-bound PrPC.
- The findings highlight differential PrPC expression in PNH blood cell populations.
- Further research may elucidate the functional implications of PrPC deficiency in PNH.
