Norepinephrine transporter (NET) is expressed in cardiac sympathetic ganglia of adult rat

Li, He; Sun, Kai; Hu, Xiao; Zhang, Gou Yuan; Fei, Jian

doi:10.1038/sj.cr.7290102

Cited by 22 publications

(22 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Peroxynitrite was synthesized as described previously (23). Annexin II antibodies were generated using purified bovine annexin II and affinity-purified (30).…”

Section: Methodsmentioning

confidence: 99%

Fusion of Lamellar Body with Plasma Membrane Is Driven by the Dual Action of Annexin II Tetramer and Arachidonic Acid

Chattopadhyay

Sun

Wang

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

Annexin II has been implicated in membrane fusion during the exocytosis of lamellar bodies from alveolar epithelial type II cells. Most previous studies were based on the fusion assays by using model membranes. In the present study, we investigated annexin II-mediated membrane fusion by using isolated lamellar bodies and plasma membrane as determined by the relief of octadecyl rhodamine B (R18) self-quenching. Immunodepletion of annexin II from type II cell cytosol reduced its fusion activity. Purified annexin II tetramer (AIIt) induced the fusion of lamellar bodies with the plasma membrane in a dose-dependent manner. This fusion is Ca 2؉ -dependent and is highly specific to AIIt because other annexins (I and II monomer, III, IV, V, and VI) were unable to induce the fusion. Modification of the different functional residues of AIIt by N-ethylmaleimide, nitric oxide, or peroxynitrite abolished AIIt-mediated fusion. Arachidonic acid enhanced AIIt-mediated fusion and reduced its Ca 2؉ requirement to an intracellularly achievable level. This effect is due to membranebound arachidonic acid, not free arachidonic acid. Other fatty acids including linolenic acid, palmitoleic acid, myristoleic acid, stearic acid, palmitic acid, and myristic acid had little effect. AIIt-mediated fusion was suppressed by the removal of arachidonic acid from lamellar body and plasma membrane using bovine serum albumin. The addition of arachidonic acid back to the arachidonic acid-depleted membranes restored its fusion activity. Our results suggest that the fusion between lamellar bodies with the plasma membrane is driven by the synergistic action of AIIt and arachidonic acid.Lung surfactant is a surface active material synthesized and secreted by cuboidal alveolar type II cells (1-3). It is composed of phospholipids, mainly dipalmitoylphosphatidylcholine, and surfactant proteins A-D. It minimizes the surface tension at the air-liquid interface by inserting phospholipids between water molecules. As a result, surfactant disrupts the cohesive hydrogen bonds and prevents them from exerting high molecular forces at the alveolar surface. Deficiency of dipalmitoylphosphatidylcholine in the alveolar surface has been associated with infant respiratory distress syndrome.The secretion of surfactant by type II cells involves the translocation, docking, and fusion of lamellar bodies to the plasma membrane. For the lamellar body content to reach its extracellular destination, a continuity of the vesicular lumen and extracellular fluid must be established. This continuity is maintained through the formation of a narrow pore similar to membrane channels (4 -6). The formation of this pore is a complex event involving physical and chemical factors and is regulated by intracellular Ca 2ϩ and proteins (7). Studies on mast cells and chromaffin cells revealed that the opening of fusion pore and extrusion of granule content is influenced by an osmotic force depending upon the osmolarity of the surrounding solution (8).Annexin II plays multidimensional roles in dif...

show abstract

“…Peroxynitrite was synthesized as described previously (23). Annexin II antibodies were generated using purified bovine annexin II and affinity-purified (30).…”

Section: Methodsmentioning

confidence: 99%

Fusion of Lamellar Body with Plasma Membrane Is Driven by the Dual Action of Annexin II Tetramer and Arachidonic Acid

Chattopadhyay

Sun

Wang

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Knockdown of annexin A2 reduces the Ca 2ϩ -evoked exocytosis of WeibelPalade bodies in endothelial cells (10). In alveolar type II cells, accumulating evidence supports a role for annexin A2 in controlling the fusion of lamellar bodies with the plasma membrane and promoting surfactant secretion (11)(12)(13)(14). Nevertheless, relatively little is known about the molecular mechanisms of annexin A2 action in this process, especially in relation to its targets and biological pathways.…”

Section: From the Department Of Physiological Sciences Oklahoma Statmentioning

confidence: 99%

Annexin A2 Interactions with Rab14 in Alveolar Type II Cells

Gou

Mishra

Weng

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

Annexin A2, a calcium-dependent phospholipid-binding protein, is abundantly expressed in alveolar type II cells where it plays a role in lung surfactant secretion. Nevertheless, little is known about the details of its cellular pathways. To identify annexin A2-regulated or associated proteins, we silenced endogenous annexin A2 expression in rat alveolar type II cells by RNA interference and assessed the change of the cellular transcriptome by DNA microarray analysis. The loss of annexin A2 resulted in the change of 61 genes. Thirteen of the selected genes (11 down-regulated and 2 up-regulated genes) were validated by real time quantitative PCR. When the loss of rat annexin A2 was rescued by overexpressing EGFP-tagged human annexin A2, six of seven selected targets returned to their normal expression level, indicating that these genes are indeed annexin A2-associated targets. One of the targets, Rab14, co-immunoprecipitated with annexin A2. Rab14 also co-localized in part with annexin A2 and lamellar bodies in alveolar type II cells. The silencing of Rab14 resulted in a decrease in surfactant secretion, suggesting that Rab14 may play a role in surfactant secretion.The alveolar epithelium is composed of morphologically and functionally distinct type I and II cells. Type I cells provide the bulk of the surface area for gas exchange, whereas type II cells secrete lung surfactant to maintain mechanical stability of the alveoli (1-3). Lung surfactant is stored and secreted by exocytosis of lamellar bodies, which are specialized organelles found in type II cells. Exocytosis of the lamellar bodies is triggered by several intracellular signaling pathways. A key component of signaling involves the elevation of cytosolic Ca 2ϩ concentration in type II cells (4, 5). Because lung surfactant secretion is regulated by Ca 2ϩ signals, it is important to identify Ca 2ϩ -regulated proteins for exocytosis.Annexins are a family of Ca 2ϩ -dependent phospholipidbinding proteins. More than 50 different annexin isoforms have been identified (6, 7). Each annexin consists of a short variable N-terminal segment and a conserved C-terminal core domain. They have unique Ca 2ϩ -binding sites, which enable them to bind with negatively charged lipids. Annexins participate in many membrane-related events, such as the organization of membrane domains, the linkages of membrane-cytoskeleton, exocytosis and endocytosis, and the regulation of ion fluxes (7). Annexin A2 is abundant in alveolar type II cells. Several studies have indicated that annexin A2 is involved in Ca 2ϩ -regulated exocytosis (8 -10). In permeabilized chromaffin cells, the timedependent loss of secretory capacity can be blocked by the addition of annexin A2 to the culture medium (9). Knockdown of annexin A2 reduces the Ca 2ϩ -evoked exocytosis of WeibelPalade bodies in endothelial cells (10). In alveolar type II cells, accumulating evidence supports a role for annexin A2 in controlling the fusion of lamellar bodies with the plasma membrane and promoting surfactant secretion (11-14)...

show abstract

“…After acclimatization period, rats were sacrificed by decapitation, and the middle and inferior (stellate) sympathetic ganglia (middle cervical-stellate ganglion (MC-SG) complex) of both sides were isolated. The sympathetic ganglionic innervation of rat heart originates primarily MC-SG complex (Pardini et al, 1989;, and expression of cardiac NET mRNA is in the ganglia (Li et al, 2001).…”

Section: Methodsmentioning

confidence: 99%

“…DNase I was used to eliminate contamination of genomic DNA in RNA preparation, and 1 µg of total RNA of the ganglia was used for reverse transcription (RT) into cDNA with Moloney murine leukemia virus reverse transcriptase (M-MLV) (Gibco BRL) according to standard methods (Li et al, 2001).…”

Section: Methodsmentioning

confidence: 99%

Expressions of cardiac sympathetic norepinephrine transporter and β1-adrenergic receptor decreased in aged rats

et al. 2009

J. Zhejiang Univ. Sci. B

Self Cite

View full text Add to dashboard Cite

Evidence suggests that the deterioration of communication between the sympathetic nervous system and cardiovascular system always accompanies the aging of human and animals. Cardiac sympathetic norepinephrine (NE) transporter (NET) on presynaptic membrane is a predominant component to eliminate released NE in the synaptic cleft and maintains the sensitivity of the β-adrenergic receptor (β-AR). In the present study, we investigated NET and β 1 -AR mRNA levels and sympathetic nerve density in cardiac sympathetic ganglion and left ventricular myocardium in 2-and 16-month-old rats with Northern blot analysis and immunohistochemistry. The expression levels of NET mRNA, NET protein and β 1 -AR mRNA in the ganglia or myocardia of 16-month-old rats were markedly reduced by 67%, 26%, and 43%, respectively, in comparison with those in 2-month-old rats. Our results also show that aging induces a strong decrease of the catecholaminergic nerve fiber density.

show abstract

Norepinephrine transporter (NET) is expressed in cardiac sympathetic ganglia of adult rat

Cited by 22 publications

References 18 publications

Fusion of Lamellar Body with Plasma Membrane Is Driven by the Dual Action of Annexin II Tetramer and Arachidonic Acid

Fusion of Lamellar Body with Plasma Membrane Is Driven by the Dual Action of Annexin II Tetramer and Arachidonic Acid

Annexin A2 Interactions with Rab14 in Alveolar Type II Cells

Expressions of cardiac sympathetic norepinephrine transporter and β1-adrenergic receptor decreased in aged rats

Contact Info

Product

Resources

About