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(American Journal of Pathology. 2000;157:2045-2053.)
© 2000 American Society for Investigative Pathology


Regular Articles

Immunohistochemical Analysis of Endothelial-Monocyte-Activating Polypeptide-II Expression in Vivo

J. Clifford Murray*, Georgina Barnett*, Maarten Tas*, Anne Jakobsen*, Joanne Brown*, Des Powe{dagger} and Colin Clelland{ddagger}

From the CRC Department of Clinical Oncology,*
University of Nottingham Laboratory of Molecular Oncology, and the Department of Histopathology,{ddagger}
City Hospital, Nottingham; and the Division of Pathology,{dagger}
School of Clinical Laboratory Sciences, University Hospital, Queens Medical Center, Nottingham, United Kingdom

Endothelial-monocyte activating polypeptide (EMAP)-II is a novel molecule with cytokine-like pro-inflammatory properties, inducing procoagulant activity on the surface of endothelial cells and monocyte/macrophages in vitro, as well as up-regulating E- and P-selectin expression. EMAP-II is chemotactic for monocytes/macrophages and neutrophils, and stimulates myeloperoxidase release from neutrophils. Injection of EMAP-II into the mouse footpad induces an acute inflammatory response, although some regression occurs in response to direct injection of EMAP-II into murine tumors. Very little is known about the expression of EMAP-II in normal tissues of mice or humans, or about its function in vivo. We developed polyclonal antibodies against EMAP-II using recombinant protein produced in Escherichia coli, and used these antibodies to carry out an immunohistochemical study of the occurrence and distribution of EMAP-II in human tissues. The distribution of EMAP-II protein is relatively restricted, occurring primarily in endocrine organs, in cells of neuroendocrine origin, but also in tissues with high turnover. EMAP-II is strongly expressed in secretory epithelial cells of the thyroid, pancreas, adrenal and salivary glands, among others, as well as in neurons and subsets of monocytes/macrophages. It is also found in the epithelium of the small and large intestines. We conclude that EMAP-II expression is usually, but not always, associated with tissues that display high turnover and high levels of protein synthesis.





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