scholarly journals Effects of cordycepin (3'-deoxyadenosine) on 8-Br cAMP-mediated induction of tyrosine hydroxylase (TH) in primary cultures of bovine adrenal chromaffin cells

1981 ◽  
Vol 31 ◽  
pp. 90
Author(s):  
Konosuke Kumakura
Keyword(s):  
Tyrosine Hydroxylase ◽  
Chromaffin Cells ◽  
Primary Cultures ◽  
Adrenal Chromaffin Cells ◽  
Adrenal Chromaffin

scholarly journals Laminin increases both levels and activity of tyrosine hydroxylase in calf adrenal chromaffin cells.

1986 ◽  
Vol 102 (1) ◽  
pp. 151-159 ◽  
Author(s):  
A Acheson ◽  
D Edgar ◽  
R Timpl ◽  
H Thoenen
Keyword(s):  
Tyrosine Hydroxylase ◽  
Chromaffin Cells ◽  
Primary Cultures ◽  
Enzyme Regulation ◽  
Acid Decarboxylase ◽  
Heparin Binding ◽  
Adrenal Chromaffin Cells ◽  
Methyl Transferase ◽  
Amino Acid Decarboxylase ◽  
Adrenal Chromaffin

We have investigated the effects of substrate-bound laminin on levels of enzymes of the catecholamine biosynthetic pathway in primary cultures of calf adrenal chromaffin cells. Laminin increases the levels of the enzymes tyrosine hydroxylase, dopamine-beta-hydroxylase, and phenylethanolamine-N-methyl-transferase. This effect is selective, in that levels of other enzymes (lactate dehydrogenase, aromatic amino acid decarboxylase, and acetylcholinesterase) are not increased. The effect of laminin can be blocked by antibodies directed against a fragment of the heparin-binding domain of the molecule, whereas antibodies directed against other fragments do not block the increase in tyrosine hydroxylase. Thus the laminin domain involved in enzyme regulation in chromaffin cells is apparently the same as that previously implicated in laminin's interactions with neurons to potentiate survival and stimulate neurite outgrowth (Edgar, D., R. Timpl, and H. Thoenen, 1984, EMBO (Eur. Mol. Biol. Organ.) J., 3:1463-1468). The increase in chromaffin cell tyrosine hydroxylase levels is preceded by an activation of the enzyme in which the Vmax (but not the Km) is altered. The effects of laminin appear to be developmentally regulated, since neither activation nor increased levels of tyrosine hydroxylase occur in adult adrenal chromaffin cells exposed to laminin.

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

Glucagon does not Affect Catecholamine Release in Primary Cultures of Bovine Adrenal Chromaffin Cells

2005 ◽  
Vol 37 (4) ◽  
pp. 205-208 ◽  
Author(s):  
Y. Sharabi ◽  
R. Zimlichman ◽  
S. Alesci ◽  
T. Huynh ◽  
R. Mansouri ◽  
...  
Keyword(s):  
Chromaffin Cells ◽  
Primary Cultures ◽  
Catecholamine Release ◽  
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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