J. Darbes et al., DEMONSTRATION OF FELINE AND CANINE PLATELET GLYCOPROTEINS BY IMMUNOCHEMISTRY AND LECTIN HISTOCHEMISTRY, Histochemistry, 100(1), 1993, pp. 83-91
Canine and feline platelet cytocentrifuge preparations (CCPs), cryosta
t and paraffin-embedded bone marrow sections were used in this study.
We evaluated whether platelets, megakaryocytes and megakaryocyte precu
rsor cells could be labelled by monoclonal antibodies (Y2/51, CLB-thro
mb/1, HPL1) against human platelet membrane glycoprotein GP IIIa and t
he GP IIb/IIIa complex or by the following 10 biotinylated lectins: co
ncanavalin A (Con A), Lens culinaris agglutinin (LCA), Pisum sativum a
gglutinin (PsA), wheat germ agglutinin (WGA), peanut agglutinin (PNA),
Phaseolus vulgaris lectin (PHA-L), Ricinus communis agglutinin 120 (R
CA120), Ulex europaeus agglutinin - I(UEA-1), soybean agglutinin (SBA)
and Dolichos biflorus agglutinin (DBA). Monoclonal antibodies Y2/51 a
nd HPL1 cross reacted with platelets and megakaryocytic cells from bot
h species, whereas CLB-thromb/1 was unreactive with canine preparation
s. Only Y2/51 labelled megakaryocytic cells in paraffin-embedded sampl
es. LCA, PSA, WGA and PHA-L labelled feline and canine platelets and d
ifferent numbers of morphologically identifiable megakaryocytes and nu
merous other, mostly myeloid, cells. Immunoblots of dog and cat platel
et lysates using Y2/51 visualized a single protein of 95 kDa (unreduce
d), a mol .wt value within the range of those reported for GP IIIa. So
me of the platelet (but not necessarily megakaryocyte) glycoproteins r
eacting with LCA, PSA and WGA could be identified in lectin blots foll
owing one- or two (nonreduced/reduced)-dimensional sodium dodecyl sulp
hate-polyacrylamide gel electrophoresis (SDS-PAGE). Thus in dogs and c
ats, the immunohistochemical detection of GP IIIa (and eventually GP I
Ib/IIIa) rather than lectin binding patterns could be important for th
e diagnosis of megakaryoblastic leukaemias.