DEMONSTRATION OF FELINE AND CANINE PLATELET GLYCOPROTEINS BY IMMUNOCHEMISTRY AND LECTIN HISTOCHEMISTRY

Citation
J. Darbes et al., DEMONSTRATION OF FELINE AND CANINE PLATELET GLYCOPROTEINS BY IMMUNOCHEMISTRY AND LECTIN HISTOCHEMISTRY, Histochemistry, 100(1), 1993, pp. 83-91
Citations number
56
Categorie Soggetti
Cytology & Histology
Journal title
ISSN journal
03015564
Volume
100
Issue
1
Year of publication
1993
Pages
83 - 91
Database
ISI
SICI code
0301-5564(1993)100:1<83:DOFACP>2.0.ZU;2-7
Abstract
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.