Literature DB >> 3518416

The distribution of lysozyme, alpha-1-antitrypsin, and alpha-1-antichymotrypsin in normal hematopoietic cells and in myeloid leukemias: an immunoperoxidase study on cytocentrifuge preparations, smears, and paraffin sections.

L Krugliak, P R Meyer, C R Taylor.   

Abstract

Blood and bone marrow samples from 20 individuals with reactive conditions and 26 cases of acute and chronic myeloid leukemias were tested for the presence of lysozyme, alpha-1-antitrypsin (alpha-1-AT), and alpha-1-antichymotrypsin (alpha-1-ACT). We compared the reactivity of samples in smears, cytocentrifuge preparations, and paraffin sections. Lysozyme, alpha-1-antitrypsin, and alpha-1-antichymotrypsin were found only in polymorphonuclear leukocytes and monocytes and their precursors. Lymphocytes, E-rosetting cells, Con A-activated lymphocytes, natural killer (NK) cells, red blood cells, erythroblasts, and megakaryocytes were consistently negative. Leukemic myeloblasts showed definite reactivity for both alpha-1-antitrypsin and alpha-1-ACT, but not for lysozyme. By contrast, lysozyme was present in poorly differentiated leukemic monoblasts, while alpha-1-antitrypsin and alpha-1-antichymotrypsin showed only weak reactivity. More mature myeloid and moncytic cells showed positive staining for all three antigens tested with differences in staining distribution and intensity. In four cases of chronic myeloid leukemia (CML), circulating mature polymorphonuclear leukocytes were deficient in both lysozymne and alpha-1-antitrypsin. The use of lysozyme, alpha-1-antitrypsin, and alpha-1-antichymotrypsin identifies normal and leukemic cells of the myeloid-monocytic series at all stages of maturation and is applicable to a variety of sample preparations.

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Year:  1986        PMID: 3518416     DOI: 10.1002/ajh.2830210112

Source DB:  PubMed          Journal:  Am J Hematol        ISSN: 0361-8609            Impact factor:   10.047


  5 in total

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2.  Expression patterns of murine antichymotrypsin-like genes reflect evolutionary divergence at the Serpina3 locus.

Authors:  Anita J Horvath; Sharon L Forsyth; Paul B Coughlin
Journal:  J Mol Evol       Date:  2004-10       Impact factor: 2.395

3.  Differences in distribution and synthesis of the functional opponents alpha 1-proteinase inhibitor and neutrophil elastase in eukaryotic cells.

Authors:  E Davids; A Ogilvie
Journal:  Histochem Cell Biol       Date:  1995-09       Impact factor: 4.304

4.  An evaluation of the prognostic significance of alpha-1-antitrypsin expression in adenocarcinomas of the lung: an immunohistochemical analysis.

Authors:  M Higashiyama; O Doi; K Kodama; H Yokouchi; R Tateishi
Journal:  Br J Cancer       Date:  1992-02       Impact factor: 7.640

5.  Serum concentration of alpha-1 antitrypsin is significantly higher in colorectal cancer patients than in healthy controls.

Authors:  Sergio Pérez-Holanda; Ignacio Blanco; Manuel Menéndez; Luis Rodrigo
Journal:  BMC Cancer       Date:  2014-05-21       Impact factor: 4.430

  5 in total

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