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.

scholarly journals Selective induction of tyrosine hydroxylase by cell-cell contact in bovine adrenal chromaffin cells is mimicked by plasma membranes.

1986 ◽  
Vol 103 (5) ◽  
pp. 1991-1997 ◽  
Author(s):  
S Saadat ◽  
H Thoenen
Keyword(s):  
Tyrosine Hydroxylase ◽  
Adrenal Medulla ◽  
Chromaffin Cells ◽  
Plasma Membranes ◽  
High Density ◽  
Heat Denaturation ◽  
Cell Contact ◽  
Low Density ◽  
Adrenal Chromaffin Cells ◽  
Adrenal Chromaffin

As a first step towards the identification and purification of the molecule(s) that are involved in cell contact-mediated tyrosine hydroxylase (TH) induction in cultures of bovine adrenal chromaffin cells, we have prepared plasma membranes (PM) from bovine adrenal medulla and tested their ability to mimick cell contact-mediated TH induction in low density chromaffin cultures. PM indeed induced TH in a manner similar to that observed in high density cultures. The maximal TH induction reached by PM corresponded to 69% of that of high density cultures, and half-maximal TH induction was obtained with 12 micrograms of PM per ml of medium. The induction of TH by PM was blocked by alpha-amanitin as observed in high density cultures. Since acetylcholinesterase was neither induced in high density nor in PM-treated low density cultures, an induction of TH as a result of a general increase in protein synthesis was excluded. The cell contact molecule(s) appear to be intrinsic membrane proteins. They were not removed by high or low salt extraction, but solubilized by 50 mM octylglucoside. They were resistant to 0.1% trypsin and heat denaturation but inactivated by 0.01% chymotrypsin. PM isolated from the adrenal cortex, kidney, and liver also induced TH in low density chromaffin cell cultures, although to a smaller extent than PM of the adrenal medulla. In contrast, muscle and erythrocyte PM were inactive. This shows that the cell contact molecule(s) are not restricted to the adrenal medulla, but are also present in some other but not all tissues.

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

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.

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