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Expression of peptidylglycine alpha-amidating monooxygenase: an in situ hybridization and immunocytochemical study.
Abstract
Peptide alpha-amidation, an essential posttranslational modification that confers bioactivity to many neuroendocrine peptides, is catalyzed by peptidylglycine alpha-amidating monooxygenase (PAM; EC 1.14.17.3). To complement our previous studies on the distribution of PAM in neuroendocrine organs, we have examined expression of the PAM gene in several endocrine tissues by in situ hybridization and immunocytochemistry. In all instances, the autoradiographic densities for PAM mRNA correlated with staining patterns for PAM immunoreactivity. Very high levels of PAM mRNA were found in all heart atrial cardiomyocytes, while much lower levels were present in ventricular cells. In the sublingual gland, PAM was expressed diffusely in both acinar and tubule cells. In contrast, expression of PAM was confined to granular convoluted tubule cells in the submaxillary gland. PAM was expressed at high levels in a subset of adrenal medullary chromaffin cells, and low levels of PAM mRNA and immunoreactivity were also detected in the adrenal cortex. PAM was found predominantly in the calcitonin-producing parafollicular C-cells in the thyroid gland and in the glucagon-containing A-cells in the endocrine pancreas. Collecting and distal tubule cells of the kidney expressed both PAM mRNA and immunoreactivity. The basal cells in testicular seminiferous tubules containing PAM may represent developing germ and Sertoli cells. The cellular localization of PAM within the thyroid gland, adrenal gland, testis, and pancreas correlated with known peptidergic systems, and some of the observed cellular heterogeneity in PAM mRNA expression and immunoreactivity may reflect differences in the levels of amidated peptide production. The expression of PAM in cells not known to produce high levels of alpha-amidated peptides may indicate the production of yet unidentified alpha-amidated bioactive peptides or alternative functions of the PAM protein.
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The α-amidation reaction catalyzed by PAM is crucial for the production of a number of hormones/neurotransmitters (e.g., calcitonin, oxytocin, vasopressin, GLP-1, substance P, neuropeptide Y).
“The reaction is crucial for the production of a number of hormones/neurotransmitters (e.g., calcitonin, oxytocin, vasopressin, GLP-1, substance P, neuropeptide Y)”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [151]
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Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination
Doseděl, M., Jirkovský, E., Macáková, K., Krčmová, L., Javorská, L., Pourová, J., Mercolini, L., Remião, F., Nováková, L., Mladěnka, P., et al. (2021) · Nutrients · doi:10.3390/nu13020615 · Cited by 553
Metadata
- Authors
- Braas, K. M., Harakall, S. A., Ouafik, L., Eipper, B. A., & May, V
- Affiliations
- University of Vermont (US)
- Venue
- Endocrinology
- Publisher
- The Endocrine Society
- Published
- 1992-05
- Volume
- 130
- Issue
- 5
- Pages
- 2778-2788
- ISSN
- 0013-7227 (ISSN-L)
- 1945-7170
- OpenAlex
- W2085694338
- Cited by
- 40
- References
- 0
- Citations by year
- 2024: 1 · 2021: 1 · 2020: 2 · 2019: 1 · 2017: 1 · 2015: 1 · 2014: 1 · 2012: 2
- FWCI
- 1.09
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- National Institute on Drug Abuse (DA 00098, DA.00266)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Neuroendocrine regulation and behavior
- Health Sciences › Medicine › Surgery › Cardiovascular, Neuropeptides, and Oxidative Stress Research
- Keywords
- peptidylglycine alpha-amidating monooxygenase, PAM, post-translational modification, neuroendocrine cells, cardiomyocytes, sublingual gland, submandibular gland, adrenal medulla, chromaffin cells, glucagon cells, kidney tubule cells, germ cells, Sertoli cells, endocrine pancreas, endocrine tissues
- MeSH terms
- Adrenal Medulla, Animals, Mixed Function Oxygenases, Immune Sera, Immunohistochemistry, Kidney, Male, Multienzyme Complexes, Myocardium, Nucleic Acid Hybridization, Pancreas, Rats, Inbred Strains, RNA, Messenger, Salivary Glands, Testis, Thyroid Gland, Transcription, Genetic, Rats
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