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(American Journal of Pathology. 2001;159:449-455.)
© 2001 American Society for Investigative Pathology

Short Communications

Expression of Lysosome-Associated Membrane Proteins in Human Colorectal Neoplasms and Inflammatory Diseases

Koh Furuta^*, Masato Ikeda, Yoshifuku Nakayama, Kenjiro Nakamura, Masao Tanaka, Naotaka Hamasaki^¶, Masaru Himeno^||, Stanley R. Hamilton^** and J. Thomas August

From the Department of Clinical Chemistry and Laboratory Medicine,^*
National Cancer Center Hospital, Tokyo, Japan; the Department of Occupational Health Economics,
University of Occupational and Environmental Health, Kitakyushu, Japan; the Department of Pathology 1,
School of Medicine, Fukuoka University, Fukuoka, Japan; the Departments of Surgery 1
and Clinical Chemistry and Laboratory Medicine,^¶
Graduate School of Medical Sciences, and the Division of Pharmaceutical Cell Biology,^||
Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan; the Department of Pathology,^**
Division of Gastrointestinal-Liver Pathology, and the Department of Pharmacology and Molecular Sciences,
The Johns Hopkins University School of Medicine, Baltimore, Maryland

The lysosome-associated membrane proteins (LAMPs)-1 and -2 are major constituents of the lysosomal membrane. These molecules are known to be among the most glycosylated proteins of several types of cells and cancer cells, and their expression in cancer cells is marked by a distinct difference in the structures of the oligosaccharides as compared to nonmalignant cells. We analyzed by immunohistochemistry the intensity and distribution of LAMP-1 and LAMP-2 in 9 human colorectal cancer cases and in 16 control cases, including inflammatory diseases (diverticulitis, ulcerative colitis, and Crohn’s disease). LAMP proteins were expressed more intensely in the epithelium of colorectal neoplasms than in normal mucosa (P < 0.05), and no significant differences were found between adenoma and cancer cells (P > 0.05) in the same tissue section. Further, in sites of inactive inflammatory diseases and nonneoplastic areas in cancer specimens, no significant increases in epithelial LAMP proteins were observed, even in the proliferative zone of the lower crypt epithelium. Northern blot analysis showed increased expression of LAMP-1 and LAMP-2A in two of three colorectal cancers examined and increased LAMP-2B in all three cancers. Our findings suggest that LAMPs are related to neoplastic progression, but there is no direct association between the expression of LAMP molecules and cell proliferation.

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