Ji, A. X., and Prive, G. G. (2013). Crystal structure of KLHL3 in complex with Cullin3. PLoS One 8:e60445. doi: 10.1371/journal.pone.0060445 Atarashi, K., Mulrow, P. J., and Franco-Saenz, R. (1985). Effect of atrial peptides on aldosterone production. J. Clin. Invest. 76, 1807–1811. Belin de Chantemele, E. J., Mintz, J. D., Rainey, W. E., and Stepp, D. W. (2011). Impact of leptin-mediated sympatho-activation on cardiovascular function in obese mice. Hypertension 58, 271–279. doi: 10.1161/HYPERTENSIONAHA.110.168427 Cherradi, N., Bideau, M., Arnaudeau, S., Demaurex, N., James, R. W., Azhar, S., et al. (2001). Angiotensin II promotes selective uptake of high density lipoprotein cholesterol esters in bovine adrenal glomerulosa and human adrenocortical carcinoma cells through induction of scavenger receptor class B type I. Endocrinology 142, 4540–4549. doi: 10.1210/endo.142.10.8412

ring review - Wareable Prevention Circul+ smart ring review - Wareable

I am diabetic and my blood pressure went down as well as my blood sugar just for wearing this ring. I work in a toxic environmentthat is very stressful and wearing the HealthGo has helped me relax and be calmer! It has also reduced my stress level." Gyles, S. L., Burns, C. J., Whitehouse, B. J., Sugden, D., Marsh, P. J., Persaud, S. J., et al. (2001). ERKs regulate cyclic AMP-induced steroid synthesis through transcription of the steroidogenic acute regulatory (StAR) gene. J. Biol. Chem. 276, 34888–34895. doi: 10.1074/jbc.M102063200 A filing at the US Patent and Trademark Office (spotted by TechRadar) reveals a heart rate sensing smart ring, with a host of biometric features. Chartier, L., Schiffrin, E., Thibault, G., and Garcia, R. (1984). Atrial natriuretic factor inhibits the stimulation of aldosterone secretion by angiotensin II, ACTH and potassium in vitro and angiotensin II-induced steroidogenesis in vivo. Endocrinology 115, 2026–2028. But it’s not any old SpO2 monitor. The patent talks about a photodetector sensor that enables transmissive examination of blood oxygen levels, which is more accurate than the type of SpO2 sensor found on wrist wearables that uses reflected light.

Chraibi, A., Vallet, V., Firsov, D., Hess, S. K., and Horisberger, J. D. (1998). Protease modulation of the activity of the epithelial sodium channel expressed in Xenopus oocytes. J. Gen. Physiol. 111, 127–138. Daniel is in his 50s and has been having high blood pressure for years. He was tired of feeling tired, having headaches, and feeling like his body wasn't working the way it should. Daniel tried everything from changing his diet to taking medication, but nothing seemed to work long-term. That's when he found HealthGo™ Blood Pressure Regulator Ring, and he couldn't be happier! Obesity is a well-known cause of hypertension and is characterized by high aldosterone levels ( Goodfriend et al., 1998; Kurukulasuriya et al., 2011). One possibility is that adipocytes affect aldosterone production since they are active endocrine tissues ( Ronti et al., 2006). Indeed, Ehrhart-Bornstein et al. (2003) showed that isolated adipocyte secretory products could dramatically increase aldosterone production independent of ANG II in adrenocortical cells (NCI-H295R; Ehrhart-Bornstein et al., 2003). 2,13-epoxy-9-keto-10 (trans)-octadecenoic acid (EKODE) has also been shown to increase aldosterone production in a GC line. EKODE is produced by the oxidation of linoleic acid by hepatocytes. Incubation of adrenal cells with EKODE increased aldosterone production independently of ANG II. Interestingly, adult humans have a positive correlation with blood EKODE and aldosterone levels ( Goodfriend et al., 2004). However, EKODE is unlikely the molecule responsible for the effect seen by Ehrhart-Bornstein et al. (2003), as adipocyte secretory products were not oxidized by hepatocytes. A subsequent study showed that adipocyte-derived factors from SHR/cp rats (model of metabolic syndrome with hypertension) stimulate aldosterone production by increasing ADS expression and STAR activation despite ANG II receptor inhibition. Adipocyte-derived factors from normal rats failed to replicate these results ( Nagase et al., 2006). These effects might be mediated by leptin, which is a protein hormone secreted by adipocytes and is abnormally high in obese individuals ( Martinez-Rumayor et al., 2008; Huby et al., 2015). These in vitro studies have been validated and extended by in vivo investigations. For example, leptin infusion increased expression of ADS and serum aldosterone in a dose-dependent manner in mice with no effect on ANG II, K +, and corticosterone levels ( Belin de Chantemele et al., 2011; Huby et al., 2015). Huby et al. (2015) concluded that “leptin is a new regulatory factor of aldosterone secretion that acts directly in the adrenal cortex to promote ADS expression and aldosterone production” ( Huby et al., 2015). The leptin stimulatory effect on ADS and aldosterone was not abolished upon administration of ANG II or β adrenergic receptor inhibitors in mice, further supporting the notion of leptin as a novel effector of aldosterone production ( Huby et al., 2015). Leptin achieves these effects possibly through CaMK II, as leptin increased intracellular Ca 2+ concentration and elevated expression calmodulin and CaMK II ( Huby et al., 2015). Agreeably administration of leptin receptor antagonism abrogated leptin-mediated aldosterone secretion and lowered blood pressure in mice ( Huby et al., 2016). These studies carry crucial importance as hypertension in the obese population is a devastating health issue ( Kurukulasuriya et al., 2011). The patent states that: “Systems can utilize the ring to monitor the oxygen saturation, pulse, blood pressure, glucose levels and lipd concentration” of the wearer.

Blood Pressure Regulator Ring,Healthgo Blood Healthgo Blood Pressure Regulator Ring,Healthgo Blood

WNK4 is a serine/threonine kinase, mutations of which have been identified as a potential cause for PHA II ( Wilson et al., 2001; Lopez-Cayuqueo et al., 2018). The underlying mechanism behind this disease may be explained by a negative regulation of ENaC through WNK4 ( Figure 4). Both in vivo and in vitro studies have shown a significant reduction of ENaC surface expression upon interacting with WNK4 ( Ring et al., 2007a). ENaC-WNK4 interaction requires an intact COOH terminus of β and ϒ subunits but not the PY motif, differing from ENaC-Nedd4-2 interaction requiring the PY motif. In the presence of aldosterone, SGK1 phosphorylates WNK4 and abrogates its negative regulation of ENaC ( Ring et al., 2007a, b; Yu et al., 2013). The clinical relevance of ENaC-WNK4 interaction is illustrated by PHA II-associated R1185C mutation of WNK4, which decreases WNK4’s inhibitory effect on ENaC by enhancing SGK1-mediated phosphorylation of WNK4 at S1217 ( Na et al., 2013). Aldosterone also increases the expression of kidney-specific WNK1 (kinase-deficient variant), which consequently increases transepithelial Na + transport in cortical collecting duct cells potentially through regulation of ENaC ( Naray-Fejes-Toth et al., 2004). WNK1 appears to increase ENaC surface expression by activating SGK1 through a non-catalytic mechanism ( Xu et al., 2005a, b). This appears to be dependent on phosphatidylinositol 3-kinase, as its inhibition abrogates this effect ( Xu et al., 2005b). Both WNK4 and WNK1 are implicated in PHA II ( Wilson et al., 2001). Two other genes, KLHL3 and CUL3, encoding kelch-like 3 (Kelch) and cullin 3 (cul3) proteins, respectively, may explain the mechanism by which WNK4 and WNK1 cause PHA II. Cul3 is an integral member of cul3-RING ubiquitin ligase, an E3 ubiquitin ligase. It forms a scaffold for the RING finger protein and ubiquitin conjugating enzyme E2 ( Genschik et al., 2013). Kelch is an adaptor protein that connects cul3-RING ubiquitin ligase to its targets ( Ji and Prive, 2013). Mutations in KLHL3 and CUL3 have been implicated in PHA II and appear to cause hypertension and electrolyte disbalance ( Boyden et al., 2012; Louis-Dit-Picard et al., 2012). One mechanism by which these mutations cause PHA II is through Wnk1 and Wnk4, as both of these proteins are targets of Cul3-RING ubiquitin ligase ( Ohta et al., 2013; Shibata et al., 2013b). PHA II causing mutations in KLHL3 decreases Wnk4 binding to Cul3-RING ubiquitin ligase, decreasing WNK4 degradation and increasing its levels resulting in hypertension ( Mori et al., 2013; Wakabayashi et al., 2013; Wu and Peng, 2013; Susa et al., 2014).

Kleyman, T. R., and Eaton, D. C. (2020). Regulating ENaC’s gate. Am. J. Physiol. Cell Physiol. 318, C150–C162. doi: 10.1152/ajpcell.00418.2019 And that’s perhaps why putting the features of a Fitbit into a smart ring isn’t technically difficult, there are warnings that users and consumers may not be as interested in the form factor. Holland, O. B., and Carr, B. (1993). Modulation of aldosterone synthase messenger ribonucleic acid levels by dietary sodium and potassium and by adrenocorticotropin. Endocrinology 132, 2666–2673. Aldosterone stimulates Na + transport by regulating the expression and activity of ENaC. Aldosterone stimulates the expression and stability of SGK1, which directly and indirectly increases the expression and activity of ENaC. SGK1 phosphorylates Nedd4-2, a ubiquitin ligase that ubiquitinates a PY motif of ENaC and targets it for degradation. Upon phosphorylation by SGK1, Nedd4-2 loses its affinity to ENaC thereby increasing the number of channels in the PM. SGK1 also phosphorylates WNK4, a negative regulator of ENaC activity. Upon phosphorylation by SGK1, WNK4 weakens its interaction with ENaC. SGK1 itself is expressed in many tissues but is immediately targeted for degradation by ERAD. Aldosterone prevents its degradation by increasing the expression of GILZ, which reduces ER localization of SGK1 and directs it to ENaC. Dot1a-Af9-Af17-mediated epigenetic control of ENaC and Na + handling is regulated in aldosterone-dependent and -independent manners. The former involves reduction of Dot1a-Af9 complex formation through aldosterone-induced downregulation of Dot1a and Af9 and SGK1-mediated Af9 phosphorylation. The latter is achieved by competitive protein–protein interactions between Dot1a-Af9 and Dot1a-Af17. Author Contributions The ring has been given an IP65 dust and water resistance rating, which means you do get some extra durability protection here, but ultimately it's not something you can wear in the shower or go swimming with.

Blood Pressure Regulator Ring – Volikon + Juxow HealthGo™ Blood Pressure Regulator Ring – Volikon + Juxow

Fakitsas, P., Adam, G., Daidie, D., van Bemmelen, M. X., Fouladkou, F., Patrignani, A., et al. (2007). Early aldosterone-induced gene product regulates the epithelial sodium channel by deubiquitylation. J. Am. Soc. Nephrol. 18, 1084–1092. doi: 10.1681/ASN.2006080902It uses the fingerstopress key points called ‘Acu Points’ on the skin surface rhythmically, to stimulate the body’s natural self-curative abilities. When these acupressure points for high BP are pressed, they release muscular tension and promote the circulation of blood to aid healing. Chang, S. S., Grunder, S., Hanukoglu, A., Rosler, A., Mathew, P. M., Hanukoglu, I., et al. (1996). Mutations in subunits of the epithelial sodium channel cause salt wasting with hyperkalaemic acidosis, pseudohypoaldosteronism type 1. Nat. Genet. 12, 248–253. Greenlee, M. M., Lynch, I. J., Gumz, M. L., Cain, B. D., and Wingo, C. S. (2011). Mineralocorticoids stimulate the activity and expression of renal H +, K + –ATPases. J. Am. Soc. Nephrol. 22, 49–58. doi: 10.1681/ASN.2010030311 Hodges, R. R., Horikawa, Y., Rios, J. D., Shatos, M. A., and Dartt, D. A. (2007). Effect of protein kinase C and ca(2+) on p42/p44 MAPK, Pyk2, and Src activation in rat conjunctival goblet cells. Exp. Eye Res. 85, 836–844. doi: 10.1016/j.exer.2007.08.019