scholarly journals Non-Chromaffin Cell Constituents of the Adrenal Medulla are Detrimental to the Survival of Grafted Adrenal Chromaffin Cells: Studies in Rats and Non-Human Primates

1992 ◽  
Vol 3 (4) ◽  
pp. 209-210 ◽  
Author(s):  
Sherry B. Schueler ◽  
John D. Ortega ◽  
Jacqueline Sagen ◽  
Jeffrey H. Kordower
Keyword(s):  
Adrenal Medulla ◽  
Chromaffin Cells ◽  
Chromaffin Cell ◽  
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 Activin A stimulates catecholamine secretion from rat adrenal chromaffin cells: a new physiological mechanism

2005 ◽  
Vol 186 (2) ◽  
pp. R1-R5 ◽  
Author(s):  
Damien J Keating ◽  
Chen Chen
Keyword(s):  
Adrenal Cortex ◽  
Adrenal Medulla ◽  
Chromaffin Cells ◽  
Transforming Growth Factor ◽  
Activin A ◽  
Catecholamine Secretion ◽  
Maximal Effect ◽  
Dependent Manner ◽  
Adrenal Chromaffin Cells ◽  
Adrenal Chromaffin

Activin A is a member of the transforming growth factor-β family and has known roles in the adrenal cortex, from which activin A is secreted. We aimed to find whether activin A induces secretion of catecholamines from chromaffin cells of the adrenal medulla, which neighbours the adrenal cortex in vivo. Using carbon fibre amperometry, we were able to measure catecholamine secretion in real-time from single chromaffin cells dissociated from the rat adrenal medulla. Activin A stimulated catecholamine secretion in a rapid and dose-dependent manner from chromaffin cells. This effect was fully reversible upon washout of activin A. The minimum dose at which activin A had a maximal effect was 2 nM, with an EC50 of 1.1 nM. The degree of secretion induced by activin A (2 nM) was smaller than that due to membrane depolarization caused by an increase in the external K+ concentration from 5 to 70 mM. No response to activin A was seen when Ca2+ channels were blocked by Cd2+ (200 μM). We conclude from these findings that activin A is capable of stimulating a robust level of catecholamine secretion from adrenal chromaffin cells in a concentration-dependent manner. This occurs via the opening of voltage-gated Ca2+ channels, causing Ca2+ entry, thereby triggering exocytosis. These findings illustrate a new physiological role of activin A and a new mechanism in the control of catecholamine secretion from the adrenal medulla.

Effects of transplantation on mouse adrenal chromaffin cells

1988 ◽  
Vol 116 (1) ◽  
pp. 149-NP ◽  
Author(s):  
M. Jousselin-Hosaja
Keyword(s):  
Adrenal Medulla ◽  
Chromaffin Cells ◽  
Adrenal Glands ◽  
Occipital Cortex ◽  
Adrenal Chromaffin Cells ◽  
Dense Cores ◽  
Morphometric Methods ◽  
Adrenal Chromaffin ◽  
The Brain

ABSTRACT The effects of long-term transplantation on the ultrastructure of adrenaline- and noradrenaline-storing cells from the adrenal medulla were determined using morphometric methods. Mouse adrenal medulla were freed from the adrenal cortex and grafted into the occipital cortex of the brain. Two types of chromaffin cells were identified by electron microscopy in grafts fixed with glutaraldehyde and osmium tetroxide. Noradrenaline-type cells were predominant and formed 70–80% of the surviving population of grafted chromaffin cells. A minority of the chromaffin cells contained medium-sized granules (140–210 nm in diameter) (medium granule cell; MGC) with finely granular moderately electron dense cores. Morphometric analysis of noradrenaline phenotype cells and MGC cells in transplants showed no significant differences compared with the noradrenaline-storing cells of normal adrenal glands. In contrast, noradrenaline-type cells and MGC cells in the grafts had areas of secretory vesicles which were significantly (P<0·01) larger and areas of rough endoplasmic reticulum which were significantly (P<0 ·01) smaller than those of the adrenaline-storing cells of normal adrenal glands. It was concluded that long-term transplantation caused no degenerative changes in the ultrastructure of mouse adrenal chromaffin cells. J. Endocr. (1988) 116, 149–153

Development of chromaffin cells depends on MASH1 function

Development ◽  
2002 ◽  
Vol 129 (20) ◽  
pp. 4729-4738 ◽  
Author(s):  
Katrin Huber ◽  
Barbara Brühl ◽  
François Guillemot ◽  
Eric N. Olson ◽  
Uwe Ernsberger ◽  
...  
Keyword(s):  
Adrenal Medulla ◽  
Chromaffin Cells ◽  
Adrenal Glands ◽  
Sympathetic Neurons ◽  
Cell Lineage ◽  
Neuroendocrine Differentiation ◽  
Sympathetic Ganglia ◽  
Adrenal Chromaffin Cells ◽  
Wild Type ◽  
Adrenal Chromaffin

The sympathoadrenal (SA) cell lineage is a derivative of the neural crest (NC), which gives rise to sympathetic neurons and neuroendocrine chromaffin cells. Signals that are important for specification of these two types of cells are largely unknown. MASH1 plays an important role for neuronal as well as catecholaminergic differentiation. Mash1 knockout mice display severe deficits in sympathetic ganglia, yet their adrenal medulla has been reported to be largely normal suggesting that MASH1 is essential for neuronal but not for neuroendocrine differentiation. We show now that MASH1 function is necessary for the development of the vast majority of chromaffin cells. Most adrenal medullary cells in Mash1–/– mice identified by Phox2b immunoreactivity, lack the catecholaminergic marker tyrosine hydroxylase. Mash1 mutant and wild-type mice have almost identical numbers of Phox2b-positive cells in their adrenal glands at embryonic day (E) 13.5; however, only one-third of the Phox2b-positive adrenal cell population seen in Mash1+/+ mice is maintained in Mash1–/– mice at birth. Similar to Phox2b, cells expressing Phox2a and Hand2 (dHand) clearly outnumber TH-positive cells. Most cells in the adrenal medulla of Mash1–/– mice do not contain chromaffin granules, display a very immature, neuroblast-like phenotype, and, unlike wild-type adrenal chromaffin cells, show prolonged expression of neurofilament and Ret comparable with that observed in wild-type sympathetic ganglia. However, few chromaffin cells in Mash1–/– mice become PNMT positive and downregulate neurofilament and Ret expression. Together, these findings suggest that the development of chomaffin cells does depend on MASH1 function not only for catecholaminergic differentiation but also for general chromaffin cell differentiation.

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.

Functional mitochondria are required for O2 but not CO2 sensing in immortalized adrenomedullary chromaffin cells

2008 ◽  
Vol 294 (4) ◽  
pp. C945-C956 ◽  
Author(s):  
J. Buttigieg ◽  
S. T. Brown ◽  
M. Lowe ◽  
M. Zhang ◽  
C. A. Nurse
Keyword(s):  
Complex I ◽  
Chromaffin Cells ◽  
Chromaffin Cell ◽  
Carbonic Anhydrase Ii ◽  
Adrenal Chromaffin Cells ◽  
Wild Type ◽  
Mitochondrial Complex ◽  
Adrenal Chromaffin Cell ◽  
Adrenal Chromaffin ◽  
First Time

Catecholamine (CAT) release from adrenomedullary chromaffin cells (AMC) in response to stressors such as low O2 (hypoxia) and elevated CO2/H+ is critical during adaptation of the newborn to extrauterine life. Using a surrogate model based on a v -myc immortalized adrenal chromaffin cell line (i.e., MAH cells), combined with genetic perturbation of mitochondrial function, we tested the hypothesis that functional mitochondria are required for O2 sensing. Wild-type MAH cells responded to both hypoxia and increased CO2 (hypercapnia) with K+ current inhibition and membrane depolarization. Additionally, these stimuli caused a rise in cytosolic Ca2+ and CAT secretion, determined by fura-2 spectrofluorimetry and carbon fiber amperometry, respectively. In contrast, mitochondria-deficient (ρ0) MAH cells were hypoxia insensitive, although responses to hypercapnia and expression of several markers, including carbonic anhydrase II, remained intact. Rotenone (1 μM), a mitochondrial complex I blocker known to mimic and occlude the effects of hypoxia in primary AMC, was effective in wild-type but not ρ0 MAH cells. These data demonstrate that functional mitochondria are involved in hypoxia-sensing by adrenal chromaffin cells. We also show for the first time that, like their neonatal chromaffin cell counterparts, MAH cells are CO2 sensors; however, this property is independent of functional mitochondria.

Dynorphin and enkephalins in adrenal paraneurones. Opiates in the adrenal medulla

1984 ◽  
Vol 62 (5) ◽  
pp. 484-492 ◽  
Author(s):  
Simon Lemaire ◽  
Robert Day ◽  
Michel Dumont ◽  
Lucie Chouinard ◽  
Raymond Calvert
Keyword(s):  
Adrenal Medulla ◽  
Cell Population ◽  
Chromaffin Cells ◽  
Cell Extract ◽  
Tissue Extract ◽  
Molecular Forms ◽  
Adrenal Chromaffin Cells ◽  
Bovine Adrenal Medulla ◽  
Order Of Magnitude ◽  
Adrenal Chromaffin

Immunoreactive dynorphin (ir-Dyn), immunoreactive leucine-enkephalin (ir-Leu-Enk) and various other neuropeptides were measured in acid extracts of bovine adrenal medulla and isolated adrenal chromaffin cells. Their respective levels ranged as follows: Leu-Enk > Dyn > bombesin > vasoactive intestinal peptide (VIP) > neurotensin > substance P. Comparisons of the total catecholamine levels with the levels of Leu-Enk in both extracts gave ratios in the same order of magnitude (2600, tissue extract and 5000, cell extract). However, the catecholamine/Dyn ratio in the tissue extract (138 000) was much higher than that found in the cell extract (20 180), suggesting a possible selective degradation of Dyn in tissue extract as compared with cell extract or an induction of Dyn biosynthesis in cells which have been isolated from their natural microenvironment. Immunofluorescence staining of isolated chromaffin cell sections revealed the presence of ir-Dyn in 5 to 10% of the total cell population. To localize ir-Dyn in regard to Leu-Enk and catecholamines, adrenal chromaffin cells were separated into three populations (I, II, and III) on a stepwise bovine serum albumin (BSA) gradient. Relative high levels of ir-Dyn were measured in cell layer I (4 pmol/106 cells), a cell population enriched in noradrenaline. However, ir-Leu-Enk was more concentrated in cell layers II and III (5.3 and 8.3 pmol/106 cells), two populations enriched in adrenaline. Isolation and high pressure liquid chromatography (HPLC) analysis of adrenomedullary Dyn indicated the presence of at least five molecular forms corresponding to Dyn-(1-11), Dyn-(1-12), Dyn-(1-13), Ala-containing-Dyn-(1-13) and a nonidentified molecule eluting closely to Dyn-(1-13). These data indicate that adrenal ir-Dyn and ir-Leu-Enk have distinct cellular distributions. In addition, the identification of Dyn fragments in bovine adrenal medulla indicates that these short peptides may be considered as natural active forms of Dyn.

scholarly journals Oxygen sensitivity in the sheep adrenal medulla: role of SK channels

2001 ◽  
Vol 281 (5) ◽  
pp. C1434-C1441 ◽  
Author(s):  
Damien J. Keating ◽  
Grigori Y. Rychkov ◽  
Michael L. Roberts
Keyword(s):  
Adrenal Medulla ◽  
Chromaffin Cells ◽  
Catecholamine Secretion ◽  
Resting Potential ◽  
Sk Channels ◽  
Adrenal Chromaffin Cells ◽  
Simultaneous Application ◽  
Adrenal Chromaffin ◽  
Small Conductance

The hypoxia-evoked secretion of catecholamines from the noninnervated fetal adrenal gland is essential for surviving intrauterine hypoxemia. The ion channels responsible for the initial depolarization that leads to catecholamine secretion have not been identified. Patch-clamp studies of adrenal chromaffin cells isolated from fetal and adult sheep revealed the presence of a Ca2+-dependent K+ current that was reduced by hypoxia. Apamin, a blocker of small-conductance K+ (SK) channels, reduced the Ca2+-dependent K+current, and the sensitivity of the channels to apamin indicated that the channels involved were of the SK2 subtype. In the presence of apamin, the hypoxia-evoked change in K+ currents was largely eliminated. Both hypoxia and apamin blocked a K+current responsible for maintaining the resting potential of the cell, and the depolarization resulting from both led to an influx of Ca2+. Simultaneous application of hypoxia and apamin did not potentiate the increase in cytosolic Ca2+ concentration beyond that seen with either agent alone. Similar results were seen with curare, another blocker of SK channels. These results indicate that closure of SK2 channels would be the initiating event in the hypoxia-evoked catecholamine secretion in the adrenal medulla.

Effects of substance P on the long-term regulation of tyrosine hydroxylase activity and catecholamine levels in cultured adrenal chromaffin cells

1986 ◽  
Vol 64 (12) ◽  
pp. 1548-1555 ◽  
Author(s):  
P. Boksa
Keyword(s):  
Tyrosine Hydroxylase ◽  
Substance P ◽  
Chromaffin Cells ◽  
Chromaffin Cell ◽  
Splanchnic Nerve ◽  
Adrenal Chromaffin Cells ◽  
Hydroxylase Activity ◽  
Tyrosine Hydroxylase Activity ◽  
Adrenal Chromaffin

Acetylcholine, released from splanchnic nerve terminals innervating adrenal chromaffin cells, is known to increase synthesis of adrenal tyrosine hydroxylase, the rate-limiting enzyme in catecholamine synthesis. The neuropeptide substance P is also present in the splanchnic nerve innervating the adrenal medulla, and this study examined whether substance P has any long-term effects on tyrosine hydroxylase activity and catecholamine levels in cultures of adult bovine adrenal chromaffin cells. When cultures were incubated for 3 days with substance P and carbachol, a cholinergic agonist, substance P (10−6 M, and greater) completely inhibited the increase in tyrosine hydroxylase activity normally induced by carbachol. Long-term stimulation with carbachol also depleted endogenous catecholamines from the cells and substance P prevented this carbachol-induced depletion of catecholamine content. Substance P by itself, in the absence of carbachol, had only a slight effect on tyrosine hydroxylase activity. 8-Bromoadenosine 3′:5′-cyclic monophosphate, an analogue of adenosine 3′:5′-cyclic monophosphate, also increases tyrosine hydroxylase activity in chromaffin cells; however, substance P had no effect on the increase in tyrosine hydroxylase activity induced by this analogue. These results indicate that substance P's effects are relatively specific for the carbachol-induced increased in tyrosine hydroxylase activity and that the primary site of action of substance P is not a site common to the mechanism of tyrosine hydroxylase induction by carbachol and 8-bromoadenosine 3′:5′-cyclic monophosphate. During long-term incubation of chromaffin cell cultures, substance P inhibited the carbachol-induced increase in tyrosine hydroxylase activity only if peptidase inhibitors, bacitracin and captopril, were included in the medium, suggesting that chromaffin cell peptidases may be capable of terminating substance P's actions in these cells. The peptidase inhibitors bacitracin and captopril alone increased tyrosine hydroxylase activity and depleted catecholamines from the cells. The results suggest that substance P, released either from the splanchnic nerve or from the chromaffin cells themselves, may play a role in the long-term regulation of tyrosine hydroxylase activity and catecholamine levels in the mature adrenal chromaffin cell.

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