Immunocytochemical localization of sphingolipid activator protein-1, the sulfatide/GM1 ganglioside activator,to lysosomes in human liver and colon |
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| Authors: | T. Tamaru S. Fujibayashi W. R. Brown D. A. Wenger |
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| Affiliation: | (1) Department of Medicine of the Veterans Administration Hospital, 4200 East Ninth Avenue, 80262 Denver, Colorado, USA;(2) University of Colorado School of Medicine, 4200 East Ninth Avenue, 80262 Denver, Colorado, USA;(3) Department of Pediatrics of the University of Colorado School of Medicine, 4200 East Ninth Avenue, 80262 Denver, Colorado, USA;(4) Present address: 1-2-7, Ujina Higashi, Minami-ku, 734 Hiroshima City, Hiroshima, Japan;(5) Present address: Yakumo National Sanatorium, 128, Miyazono-cho, Yakumo-cho, Yamakoshi-gun, 049-31 Hokkaido, Japan;(6) Division of Medical Genetics, Jefferson Medical College, 19107 Philadelphia, Pennsylvania, USA |
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| Abstract: | Summary Sphingolipid activator proteins (SAP) stimulate the enzymatic hydrolysis of sphingolipids. The results of biochemical studies have suggested that SAP are located within lysosomes. In this study we sought immunocytochemical verification of the lysosomal location of SAP-1, a SAP that stimulates the hydrolysis of sulfatide and GM1 ganglioside. We stained adjacent sections of normal adult liver and colon for either SAP-1, by peroxidase-labeled antibodies, or acid phosphatase, by enzyme histochemistry. At the light microscopic level, SAP-1 and acid phosphatase were present in similar cells of the colonic lamina propria and hepatic sinusoids, and in similar supranuclear sites of colonic epithelial cells. By electron microscopy, SAP-1 was present in vesicular structures morphologically similar to those containing acid phosphatase. Thus, SAP-1 is present in lysosomes of several different kinds of cells in the normal human liver and colon. |
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