scholarly journals Phenylalanine as substrate for tyrosine hydroxylase in bovine adrenal chromaffin cells

1990 ◽  
Vol 268 (2) ◽  
pp. 525-528 ◽  
Author(s):  
M H Fukami ◽  
J Haavik ◽  
T Flatmark
Keyword(s):  
Tyrosine Hydroxylase ◽  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Bovine Chromaffin Cells ◽  
Adrenal Chromaffin ◽  
Dopa Formation

Incubation of bovine chromaffin cells with L-[14C]phenylalanine resulted in label accumulation in catecholamines at about 30% of the rate seen with L-tyrosine as precursor. Studies with purified tyrosine hydroxylase (EC 1.14.16.2) showed that the enzyme catalysed the hydroxylation of L-phenylalanine first to L-p-tyrosine and then to 3,4-dihydroxyphenylalanine (DOPA). No evidence for a significant involvement of an L-m-tyrosine intermediate in DOPA formation was found.

Retinol activates tyrosine hydroxylase acutely by increasing the phosphorylation of serine40 and then serine31 in bovine adrenal chromaffin cells

2007 ◽  
Vol 103 (6) ◽  
pp. 2369-2379 ◽  
Author(s):  
Daniel P. Gelain ◽  
Jose C. F. Moreira ◽  
Lia R. M. Bevilaqua ◽  
Phillip W. Dickson ◽  
Peter R. Dunkley
Keyword(s):  
Tyrosine Hydroxylase ◽  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Adrenal Chromaffin

Regulation of catecholamine release and tyrosine hydroxylase in human adrenal chromaffin cells by interleukin-1β: role of neuropeptide Y and nitric oxide

2009 ◽  
Vol 109 (3) ◽  
pp. 911-922 ◽  
Author(s):  
Joana Rosmaninho-Salgado ◽  
Inês M. Araújo ◽  
Ana Rita Álvaro ◽  
Alexandrina F. Mendes ◽  
Lígia Ferreira ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Tyrosine Hydroxylase ◽  
Neuropeptide Y ◽  
Chromaffin Cells ◽  
Catecholamine Release ◽  
Interleukin 1Β ◽  
Adrenal Chromaffin Cells ◽  
Adrenal Chromaffin

NGF-like trophic support from peripheral nerve for grafted rhesus adrenal chromaffin cells

1990 ◽  
Vol 73 (3) ◽  
pp. 418-428 ◽  
Author(s):  
Jeffrey H. Kordower ◽  
Massimo S. Fiandaca ◽  
Mary F. D. Notter ◽  
John T. Hansen ◽  
Don M. Gash
Keyword(s):  
Tyrosine Hydroxylase ◽  
Adrenal Medulla ◽  
Sural Nerve ◽  
Chromogranin A ◽  
Chromaffin Cells ◽  
Chromaffin Cell ◽  
Adrenal Chromaffin Cells ◽  
Content Type ◽  
Adrenal Chromaffin ◽  
Fine Print

✓ Autopsy results on patients and corresponding studies in nonhuman primates have revealed that autografts of adrenal medulla into the striatum, used as a treatment for Parkinson's disease, do not survive well. Because adrenal chromaffin cell viability may be limited by the low levels of available nerve growth factor (NGF) in the striatum, the present study was conducted to determine if transected peripheral nerve segments could provide sufficient levels of NGF to enhance chromaffin cell survival in vitro and in vivo. Aged female rhesus monkeys, rendered hemiparkinsonian by the drug MPTP (n-methyl-4-phenyl-1,2,3,6 tetrahydropyridine), received autografts into the striatum using a stereotactic approach, of either sural nerve or adrenal medulla, or cografts of adrenal medulla and sural nerve (three animals in each group). Cell cultures were established from tissue not used in the grafts. Adrenal chromaffin cells either cocultured with sural nerve segments or exposed to exogenous NGF differentiated into a neuronal phenotype. Chromaffin cell survival, when cografted with sural nerve into the striatum, was enhanced four- to eightfold from between 8000 and 18,000 surviving cells in grafts of adrenal tissue only up to 67,000 surviving chromaffin cells in cografts. In grafts of adrenal tissue only, the implant site consisted of an inflammatory focus. Surviving chromaffin cells, which could be identified by both chromogranin A and tyrosine hydroxylase staining, retained their endocrine phenotype. Cografted chromaffin cells exhibited multipolar neuritic processes and numerous chromaffin granules, and were also immunoreactive for tyrosine hydroxylase and chromogranin A. Blood vessels within the graft were fenestrated, indicating that the blood-brain barrier was not intact. Additionally, cografted chromaffin cells were observed in a postsynaptic relationship with axon terminals from an undetermined but presumably a host origin.

scholarly journals Cell contact-mediated regulation of tyrosine hydroxylase synthesis in cultured bovine adrenal chromaffin cells.

1983 ◽  
Vol 97 (3) ◽  
pp. 925-928 ◽  
Author(s):  
A L Acheson ◽  
H Thoenen
Keyword(s):  
Tyrosine Hydroxylase ◽  
Cell Density ◽  
Messenger Rna ◽  
Chromaffin Cells ◽  
High Density ◽  
Cell Contact ◽  
Transcriptional Level ◽  
Adrenal Chromaffin Cells ◽  
General Process ◽  
Adrenal Chromaffin

The specific activity of tyrosine hydroxylase (TH) in bovine adrenal chromaffin cells can be controlled by changing cell density. Chromaffin cells initially plated at low density (2-3 X 10(4) cells/cm2), and subsequently replated at a 10-fold higher density showed a sixfold increase in specific TH activity within 48 h, resulting from enhanced synthesis (increased number of TH molecules as demonstrated by immunotitration and blockade by cycloheximide) rather than activation. The density-mediated TH induction was blocked by inhibitors of both messenger RNA synthesis (alpha-amanitin) and processing (9-beta-arabinofuranosyladenine), indicating a transcriptional level of regulation. Medium conditioned by high density replated cells could not mimic the effect of high density plating itself, thus direct cell contact, rather than a diffusible factor, is responsible for the density-mediated TH induction. Since neither acetylcholinesterase nor lactate dehydrogenase specific activities were increased by high cell density, it can be concluded that the contact-mediated induction of TH is rather specific, and not the result of a general process of enzyme induction.

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