Catecholamine biosynthesis and secretion: physiological and pharmacological effects of secretin

Autor: Daniel T. O'Connor, Suvobroto Nandi, Sushil K. Mahata, Bhawanjit K. Brar, Kuizing Zhang, Manjula Mahata, Sajalendu Ghosh, Laurent Taupenot, Jiaur R. Gayen, Nitish R. Mahapatra
Rok vydání: 2011
Předmět:
Transcriptional Activation
medicine.medical_specialty
Histology
Transcription
Genetic
Tyrosine 3-Monooxygenase
Vasoactive intestinal peptide
Secretin receptor family
Secretin family
Inositol 1
4
5-Trisphosphate
CREB
PC12 Cells
Gene Expression Regulation
Enzymologic
Pathology and Forensic Medicine
Secretin
Catecholamines
Internal medicine
medicine
Cyclic AMP
Animals
Humans
Phosphorylation
Protein kinase A
Cyclic AMP Response Element-Binding Protein
Promoter Regions
Genetic
Egtazic Acid
calcium ion
catecholamine
cyclic AMP dependent protein kinase
cyclic AMP responsive element binding protein
hypophysis adenylate cyclase activating polypeptide
inositol 1
4
5 trisphosphate
mitogen activated protein kinase 1
mitogen activated protein kinase 3
phospholipase C
phospholipase C beta
receptor
secretin
secretin receptor
tyrosine 3 monooxygenase
unclassified drug
vasoactive intestinal polypeptide receptor 1
animal cell
calcium cell level
catecholamine release
catecholamine synthesis
cell strain
chelation therapy
controlled study
enzyme activity
gene
genetic transcription
nonhuman
priority journal
promoter region
protein binding
protein phosphorylation
rat
signal transduction
TH gene
Calcium
Calcium Channels
Cell Membrane
Cyclic AMP-Dependent Protein Kinases
Mitogen-Activated Protein Kinases
Protein Binding
Rats
Signal Transduction
Type C Phospholipases
Phospholipase C
biology
Chemistry
Cell Biology
Endocrinology
biology.protein
Secretin receptor
hormones
hormone substitutes
and hormone antagonists
Zdroj: Cell and tissue research. 345(1)
ISSN: 1432-0878
Popis: Pituitary adenylyl cyclase activating polypeptide (PACAP) and vasoactive intestinal polypeptide (VIP) augment the biosynthesis of tyrosine hydroxylase (TH). We tested whether secretin belonging to the glucagon/PACAP/VIP superfamily would increase transcription of the tyrosine hydroxylase (Th) gene and modulate catecholamine secretion. Secretin activated transcription of the endogenous Th gene and its transfected promoter (EC50 ?4.6 nM) in pheochromocytoma (PC12) cells. This was abolished by pre-treatment with a secretin receptor (SCTR) antagonist and by inhibition of protein kinase A (PKA), mitogen-activated protein kinase, or CREB (cAMP response element-binding protein). In agreement, secretin increased PKA activity and induced phosphorylation of CREB and binding to Th CRE, suggesting secretin signaling to transcription via a PKA-CREB pathway. Secretin stimulated catecholamine secretion (EC50 ?3.5 ?M) from PC12 cells, but this was inhibited by pre-treatment with VIP-preferring receptor (VPAC1)/PACAP-preferring receptor (PAC1) antagonists. Secretin-evoked secretion occurred without extracellular Ca2+ and was abolished by intracellular Ca2+ chelation. Secretin augmented phospholipase C (PLC) activity and increased inositol-1,4,5-triphosphate (IP3) levels in PC12 cells; PLC-? inhibition blocked secretin-induced catecholamine secretion, indicating the participation of intracellular Ca2+ from a phospholipase pathway in secretion. Like PACAP, secretin evoked long-lasting catecholamine secretion, even after only a transient exposure. Thus, transcription is triggered by nanomolar concentrations of the peptide through SCTR, with signaling along the cAMP-PKA and extracellular-signal-regulated kinase 1/2 pathways and through CREB. By contrast, secretion is triggered only by micromolar concentrations of peptide through PAC1/VPAC receptors and by utilizing a PLC/intracellular Ca 2+ pathway. � 2011 Springer-Verlag.
Databáze: OpenAIRE
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