Role of connexins and pannexins in cardiovascular physiology

Meens, Merlijn J.; Kwak, Brenda R.

doi:10.1007/s00018-015-1959-2

Cited by 39 publications

(34 citation statements)

References 162 publications

(170 reference statements)

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“…In endothelial cells, gap junctions are primarily formed of the connexin proteins CX37 (GJA4), CX40 (GJA5) and CX43 (GJA1) (Meens et al. ). Because the diabetic condition reduces their expression in vascular walls (Bobbie et al.…”

Section: Discussionmentioning

confidence: 99%

“…Arginine diffusion through these pores may compensate for changes in endothelial arginine concentration elicited by, for example, decreased arginine degradation in endothelial cells. In endothelial cells, gap junctions are primarily formed of the connexin proteins CX37 (GJA4), CX40 (GJA5) and CX43 (GJA1) (Meens et al 2015). Because the diabetic condition reduces their expression in vascular walls (Bobbie et al 2010;Hou et al 2008), reduced gap-junction activity could explain limited repletion of arginine in this condition (Chennupati et al 2014).…”

Section: Discussionmentioning

confidence: 99%

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Deletion of endothelial arginase 1 does not improve vasomotor function in diabetic mice

et al. 2018

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Endothelial arginase 1 was ablated to assess whether this prevents hyperglycemia‐induced endothelial dysfunction by improving arginine availability for nitric oxide production. Endothelial Arg1‐deficient mice (Arg1‐KOT ie2) were generated by crossing Arg1 fl/fl (controls) with Tie2Cre tg/− mice and analyzed by immunohistochemistry, measurements of hemodynamics, and wire myography. Ablation was confirmed by immunohistochemistry. Mean arterial blood pressure was similar in conscious male control and Arg1‐KOT ie2 mice. Depletion of circulating arginine by intravenous infusion of arginase 1 or inhibition of nitric oxide synthase activity with L‐NG‐nitro‐arginine methyl ester increased mean arterial pressure similarly in control (9 ± 2 and 34 ± 2 mmHg, respectively) and Arg1‐KOT ie2 mice (11 ± 3 and 38 ± 4 mmHg, respectively). Vasomotor responses were studied in isolated saphenous arteries of 12‐ and 34‐week‐old Arg1‐KOT ie2 and control animals by wire myography. Diabetes was induced in 10‐week‐old control and Arg1‐KOT ie2 mice with streptozotocin, and vasomotor responses were studied 10 weeks later. Optimal arterial diameter, contractile responses to phenylephrine, and relaxing responses to acetylcholine and sodium nitroprusside were similar in normoglycemic control and Arg1‐KOT ie2 mice. The relaxing response to acetylcholine was dependent on the availability of extracellular l‐arginine. In the diabetic mice, arterial relaxation responses to endothelium‐dependent hyperpolarization and to exogenous nitric oxide were impaired. The data show that endothelial ablation of arginase 1 in mice does not markedly modify smooth muscle and endothelial functions of a resistance artery under normo‐ and hyperglycemic conditions.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Deletion of endothelial arginase 1 does not improve vasomotor function in diabetic mice

et al. 2018

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“…Cx43 deubiquitylation may rescue the protein from lysosomal degradation, allowing its recycling back to the plasma membrane. also participates in slower physiological processes, such as cell growth and development (Belousov et al, 2017;Berthoud and Ngezahayo, 2017;Jagger and Forge, 2015;Lilly et al, 2016;Meens et al, 2015;Merrifield and Laird, 2016;Wei et al, 2004). For instance, Cx43-mediated intercellular communication has been described in immune-mediated processes, where gap junctions participate in the immunological synapse and promote the transfer of viral-and tumour-derived peptides and miRNA, allowing further stimulation and modulation of immune responses (Aucher et al, 2013;Bermudez-Fajardo et al, 2007;Mendoza-Naranjo et al, 2007;Neijssen et al, 2005).…”

Section: Cx43mentioning

confidence: 99%

Role of connexin 43 in different forms of intercellular communication – gap junctions, extracellular vesicles and tunnelling nanotubes

Ribeiro-Rodrigues

Martins‐Marques

Morel

et al. 2017

Journal of Cell Science

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141

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Communication is important to ensure the correct and efficient flow of information, which is required to sustain active social networks. A fine-tuned communication between cells is vital to maintain the homeostasis and function of multicellular or unicellular organisms in a community environment. Although there are different levels of complexity, intercellular communication, in prokaryotes to mammalians, can occur through secreted molecules (either soluble or encapsulated in vesicles), tubular structures connecting close cells or intercellular channels that link the cytoplasm of adjacent cells. In mammals, these different types of communication serve different purposes, may involve distinct factors and are mediated by extracellular vesicles, tunnelling nanotubes or gap junctions. Recent studies have shown that connexin 43 (Cx43, also known as GJA1), a transmembrane protein initially described as a gap junction protein, participates in all these forms of communication; this emphasizes the concept of adopting strategies to maximize the potential of available resources by reutilizing the same factor in different scenarios. In this Review, we provide an overview of the most recent advances regarding the role of Cx43 in intercellular communication mediated by extracellular vesicles, tunnelling nanotubes and gap junctions.

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“…More commonly, a connexon docks to a connexon expressed by an adjacent cell thereby forming a gap junction channel allowing for cytoplasmic exchange of ions and small metabolites between neighboring cells [6]. As such, gap junction channels are critically involved in direct cell-cell communication and synchronization of tissue responses [7, 8]. …”

Section: Introductionmentioning

confidence: 99%

Cx47 fine-tunes the handling of serum lipids but is dispensable for lymphatic vascular function

et al. 2017

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Mutations in the gap junction protein connexin47 (Cx47) are associated with lymphedema. However, the role of Cx47 in lymphatic pathophysiology is unknown. We demonstrate that Cx47 is expressed in lymphatic endothelial cells by whole-mount immunostaining and qPCR. To determine if Cx47 plays a role in lymphatic vessel function we analysed Cx47-/- mice. Cx47-deficiency did not affect lymphatic contractility (contractile amplitude or frequency) or lymphatic morphology (vessel diameter or number of valves). Interstitial fluid drainage or dendritic cell migration through lymphatic vessels was also not affected by Cx47-deficiency. Cx47 is dispensable for long-chain fatty acid absorption from the gut but rather promotes serum lipid handling as prolonged elevated triglyceride levels were observed in Cx47-deficient mice after oral lipid tolerance tests. When crossed with Apolipoprotein E-deficient (Apoe-/-) mice, LDL-cholesterol was decreased in young Cx47-/-Apoe-/- adults as compared to Apoe-/- mice, which was inverted later in life. Finally, advanced atherosclerotic plaques in thoracic-abdominal aortas of 15 months-old mice tended to be larger in Cx47-/-Apoe-/- mice. These plaques contained fewer macrophages but similar amounts of T lymphocytes, collagen and lipids than plaques of Apoe-/- mice. In conclusion, Cx47 is expressed in lymphatic endothelium and seems modestly implicated in multiple aspects of lymphatic pathophysiology.

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Role of connexins and pannexins in cardiovascular physiology

Cited by 39 publications

References 162 publications

Deletion of endothelial arginase 1 does not improve vasomotor function in diabetic mice

Deletion of endothelial arginase 1 does not improve vasomotor function in diabetic mice

Role of connexin 43 in different forms of intercellular communication – gap junctions, extracellular vesicles and tunnelling nanotubes

Cx47 fine-tunes the handling of serum lipids but is dispensable for lymphatic vascular function

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