Immunoreactivity for β/A4 protein, but not for its precursor, in human chromaffin cells
The present study was designed to establish a) whether chromaffin cells of the human adrenal medulla express immunoreactivity for β-amyloid precursor protein (βAPP) and/or β-amyloid protein (β/A4); and b) whether cells expressing one or both of the above-mentioned proteins display immunoreactivity f...
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Published in: | Brain research bulletin Vol. 37; no. 5; pp. 449 - 455 |
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Main Authors: | , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
New York, NY
Elsevier Inc
1995
Elsevier Science |
Subjects: | |
Online Access: | Get full text |
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Summary: | The present study was designed to establish a) whether chromaffin cells of the human adrenal medulla express immunoreactivity for β-amyloid precursor protein (βAPP) and/or β-amyloid protein (β/A4); and b) whether cells expressing one or both of the above-mentioned proteins display immunoreactivity for the low- (gp75) and/or the high-affinity (gp140-
trkA) nerve growth factor receptor. To identify chromaffin cells and their supporting cells, chromogranin A, neurofilament proteins, and S-100 protein were studied in parallel. βAPP and β/A4 immunoreactivity (IR) was observed primarily labeling two different cell populations, without colocalization: βAPP IR was found in the adrenal cortical cells, which were mainly localized in the reticulate layer and in the blood vessel walls, whereas β/A4 IR was observed in the chromeffin cells.
Furthermore, supporting cells were also immunoreactive for β/A4, and sympathetic gangionic cells were immunoreactive for both βAPP and β/A4. Interestingly, clusters of cells expressing β/A4 IR also displayed gp75 IR and/or gp140-
trkA IR. Finally, all chromaffin cells (identified by chromogranin A IR) were immunolsbeled for the 200 kDa neurofilament subunit, but not for a phosphorylated epitope of this protein. These results demonstrate the occurrence of β/A4 IR, but not of βAPP, in the chromaffin cells of the human adrenal gland. The complementary distribution of amyloid-related proteins, and the possible involvement of neurotrophins in β/A4 metabolism are discussed. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0361-9230 1873-2747 |
DOI: | 10.1016/0361-9230(95)00022-7 |