MYELOPEROXIDASE GENE-EXPRESSION IN NORMAL GRANULOPOIESIS AND ACUTE LEUKEMIAS

被引：23

作者：

AUSTIN, GE

CHAN, WC

ZHAO, WG

RACINE, M

机构：

[1] Atlanta Veterans Affairs Medical Center, Decatur, GA

[2] Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA

[3] Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE

来源：

LEUKEMIA & LYMPHOMA | 1994年 / 15卷 / 3-4期

关键词：

MYELOPEROXIDASE; GENE EXPRESSION; RNA; LEUKEMIAS;

D O I：

10.3109/10428199409049717

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Myeloperoxidase (MPO) is an abundant heme protein found in granulocytes and monocytes, which plays an important role in host defense against infection. MPO enzyme activity as determined by light microscopic cytochemistry has long been an important marker used in the diagnosis of acute leukemias and other hematopoietic disorders. Recently, MPO expression has been studied at the electron microscopic level, and monoclonal antibodies (mAbs) against MPO protein have been developed. Furthermore, techniques and probes for analysing MPO expression at the RNA level are now available. This has made possible more extensive studies of MPO expression in a wide range of neoplastic and preneoplastic blood disorders. This review will discuss the fundamental biology of MPO as well as recent developments in our understanding of MPO expression in leukemic cells and cell lines of various lineages.

引用

页码：209 / 226

页数：18

共 172 条

[31]

Harrison J.E., Shultz J., Studies on the chlorinating activity of myeloperoxidase, J. Biol. Chem., 251, pp. 1371-1374, (1976)

[32]

Tsan M.F., Denison R.C., Oxidation of n-formyl methionyl chemotactic peptide by human neutrophils, J. Immunol., 126, pp. 1387-1389, (1981)

[33]

Clark A.A., Extracellular effect of the myeloperoxidase-hydrogen peroxidase-halide system, Adv. Infect. Res., 5, pp. 107-123, (1983)

[34]

Rosen H., Bearman S.I., Gabig T.G., Myeloperoxidase-mediated inhibition of the neutrophil respiratory burst, Clin. Res., 31, (1983)

[35]

Olsen R.L., Little C., Studies on the subunits of human myeloperoxidase, Biochem. J., 222, pp. 701-709, (1984)

[36]

Harrison J.E., Pabalan S., Schultz J., The sub-unit structure of crystalline canine myeloperoxidase, Biochim. Biophys. Acta, 493, pp. 247-259, (1977)

[37]

Andrews P.C., Krinsky N.I., The reductive cleavage of myeloperoxidase in half, producing enzymatically active hemi-myeloperoxidase, J. Biol. Chem., 256, pp. 4211-4218, (1981)

[38]

Andersen M.R., Atkin C.L., Eyre H.J., Intact form of myeloperoxidase from normal human neutrophils, Arch. Biochem. Biophys., 214, pp. 273-283, (1982)

[39]

Wu N.C., Schultz J., The prosthetic group of myeloperoxidase, FEBS Lett., 60, pp. 141-144, (1975)

[40]

Harrison J.E., Schultz J., Myeloperoxidase: Confirmation and nature of heme-binding inequivalence: Resolution of a carbonyl substituted heme, Biochim. Biophys. Acta, 536, pp. 341-349, (1978)

← 1 2 3 4 5 6 7 8 9 10 →