Characterization of basal lysosomes in exocrine acinar cellsC Oliver
Exocrine acinar cells possess a unique system of basally located lysosomes. Cytochemically, these lysosomes do not contain acid phosphatase, but react positively for trimetaphosphatase (C Oliver: J Histochem Cytochem 28:78, 1980). The present study extends the morphological and cytochemical characterization of these lysosomes in pancreatic, parotid, and exorbital lacrimal acinar cells from Sprague- Dawley rats and National Institutes of Health Swiss mice. The basal lysosomes are highly pleomoric in nature, and frequently appear as a system of anastomosing tubules of varying width. The lysosomes have a close morphological relationship with both the rough endoplasmic reticulum and mitochondria. In addition to trimetaphosphatase activity, the lysosomes are reactive for aryl sulfatase B, thiolacetic acid esterase, and cholinesterase. Since the cholinesterase activity could not be inhibited by specific inhibitors, this activity is most likely due to the presence of nonspecific esterases. The results of this study confirm the lysosomal nature of the basal lysosomes and underscore the necessity of using multiple enzyme activities to identify and characterize lysosomes.
Volume 31,
Issue 10,
pp. 1209-1216,
10/01/1983
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M. Bendayan and V. Gisiger Demonstration of Acetylcholinesterase Molecular Forms in a Continuous Tubular Lysosomal System of Rat Pancreatic Acinar Cells J. Histochem. Cytochem., January 1, 2001; 49(1): 29 - 40. [Abstract] [Full Text] |
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M. Bendayan and E. A. Rasio Evidence of a Tubular System for Transendothelial Transport in Arterial Capillaries of the Rete Mirabile J. Histochem. Cytochem., October 1, 1997; 45(10): 1365 - 1378. [Abstract] [Full Text] [PDF] |
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