Abstract:
:The ultrastructural immunohistochemical localization of gamma aminobutyric acid (GABA) and its regulating enzymes, L-glutamate decarboxylase (GAD) and gamma aminobutyrate-alpha-ketoglutarate transaminase, was determined utilizing an immunogold post-embedding protocol in pancreatic exocrine tissue. Within the acinar cell, GABA and its biosynthetic enzyme, GAD, were localized in zymogen granules. Quantitative analysis of the GABA immunoreactivity in the acinar cell revealed 1.7 +/- 0.5 gold particles/micron2 over the cytoplasm, 36.6 +/- 14.1 gold particles/micron2 over the zymogen granules, and 2.9 +/- 2.1 gold particles/micron2 over the mitochondria. Quantitative analysis of the distribution of colloidal gold particles, representing glutamate decarboxylase immunoreactivity in the acinar cells, revealed 38.4 +/- 2.5 gold particles/micron2 over the zymogen granules, 4.7 +/- 1.1 gold particles/micron2 over the mitochondria and 6.3 +/- 0.5 gold particles/micron2 over the remainder of the cytoplasm. Substitution of normal sheep serum for the sheep anti-glutamate decarboxylase serum revealed a significant (p less than 0.001) decrease of the colloidal gold particle distribution over the zymogen granules and cytoplasmic compartments of the acini. Gamma aminobutyrate-alpha-ketoglutarate transaminase, the catabolic enzyme for GABA, was not detected in the mitochondria, zymogen granules, and cytoplasm of the acinar cell, suggesting that GABA is not catabolized within the acinar cell. Preabsorption and substitution controls resulted in an absence of labeling. These results suggest that GABA may act extracellularly and/or have a role within the zymogen granule in the exocrine pancreas.
journal_name
Cell Tissue Resjournal_title
Cell and tissue researchauthors
Garry DJ,Garry MG,Sorenson RLdoi
10.1007/BF00213841subject
Has Abstractpub_date
1988-04-01 00:00:00pages
191-7issue
1eissn
0302-766Xissn
1432-0878journal_volume
252pub_type
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journal_title:Cell and tissue research
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