Lectin histochemistry of human bone marrow: investigation of trephine biopsy specimens in normal and reactive states and neoplastic disorders. 1991

U Schumacher, and H P Horny, and U Welsch, and E Kaiserling
University of Southampton, UK.

The lectin binding pattern of bone marrow cells in normal and reactive states and in various neoplastic disorders was investigated using trephine biopsy specimens taken from the iliac crest. The tissue samples were routinely processed (fixed in formalin and embedded in paraffin wax) and subjected to mild decalcification with EDTA. The following results were obtained. (1) More than half of the 23 fluoresceinated lectins used reacted with normal blood cells and/or their neoplastic derivatives. Inhibition tests with the appropriate sugars confirmed the specificity of binding for the majority, but not all, of the lectins. (2) WGA, Con A, PSA, STA and RCA60 and RCA120 produced a particularly intense reaction with normal, reactive and neoplastic myeloid cells. Erythroblasts exhibited weak staining in a few cases by a few lectins (WGA producing the strongest staining), while megakaryocytes nearly always remained unstained. Neoplastic lymphoid cells in various lymphoproliferative disorders and plasmacytoma cells generally reacted with the same lectins as the myeloid cells. (3) Since neoplastic myeloid cells in various myelodysplastic and myeloproliferative disorders exhibited a lectin binding pattern similar to that of myeloid cells in normal and reactive bone marrow, it is unlikely that lectin histochemistry of the bone marrow will prove of great value in the diagnosis of myelodysplastic-myeloproliferative disorders.

UI MeSH Term Description Entries
D009196 Myeloproliferative Disorders Conditions which cause proliferation of hemopoietically active tissue or of tissue which has embryonic hemopoietic potential. They all involve dysregulation of multipotent MYELOID PROGENITOR CELLS, most often caused by a mutation in the JAK2 PROTEIN TYROSINE KINASE. Disorder, Myeloproliferative,Disorders, Myeloproliferative,Myeloproliferative Disorder
D010954 Plasmacytoma Any discrete, presumably solitary, mass of neoplastic PLASMA CELLS either in BONE MARROW or various extramedullary sites. Plasma Cell Tumor,Plasmocytoma,Plasma Cell Tumors,Plasmacytomas,Plasmocytomas,Tumor, Plasma Cell,Tumors, Plasma Cell
D001773 Blood Cells The cells found in the body fluid circulating throughout the CARDIOVASCULAR SYSTEM. Blood Corpuscles,Blood Cell,Blood Corpuscle,Cell, Blood,Cells, Blood,Corpuscle, Blood,Corpuscles, Blood
D001853 Bone Marrow The soft tissue filling the cavities of bones. Bone marrow exists in two types, yellow and red. Yellow marrow is found in the large cavities of large bones and consists mostly of fat cells and a few primitive blood cells. Red marrow is a hematopoietic tissue and is the site of production of erythrocytes and granular leukocytes. Bone marrow is made up of a framework of connective tissue containing branching fibers with the frame being filled with marrow cells. Marrow,Red Marrow,Yellow Marrow,Marrow, Bone,Marrow, Red,Marrow, Yellow
D001854 Bone Marrow Cells Cells contained in the bone marrow including fat cells (see ADIPOCYTES); STROMAL CELLS; MEGAKARYOCYTES; and the immediate precursors of most blood cells. Bone Marrow Cell,Cell, Bone Marrow,Cells, Bone Marrow,Marrow Cell, Bone,Marrow Cells, Bone
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D012886 Skull The SKELETON of the HEAD including the FACIAL BONES and the bones enclosing the BRAIN. Calvaria,Cranium,Calvarium,Skulls
D037102 Lectins Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition. Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal

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