Na+,K(+)-ATPase.

Lingrel, Jerry B.; Kuntzweiler, Theresa A.

doi:10.1016/s0021-9258(17)32067-7

Cited by 631 publications

(85 citation statements)

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“…Of particular interest to this work is that the chemical gradient established by the Introduction Questions remain regarding the role of the Na,K-ATPase in the regulation of Ca 2ϩ during the contraction of car-The Na,K-ATPase is a heteromeric enzyme comprised diac muscle. For example, although the mechanism unof a 112 kDa ␣ subunit and a 53 kDa glycosylated ␤ derlying the positive inotropic action of cardiac glycosubunit (Lingrel and Kuntzweiler, 1994). The ␣ subunit is sides (described above) is well accepted, the existence the catalytic component of the holoenzyme, containing of multiple Na,K-ATPase isoforms raises the possibility both the cation and the nucleotide binding sites (Lingrel that a single isoform may mediate this effect.…”

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confidence: 99%

“…The ␣ subunit is sides (described above) is well accepted, the existence the catalytic component of the holoenzyme, containing of multiple Na,K-ATPase isoforms raises the possibility both the cation and the nucleotide binding sites (Lingrel that a single isoform may mediate this effect. Furtherand Kuntzweiler, 1994). Four ␣ subunit isoforms have more, although inhibition of the Na,K-ATPase by cardiac been identified (␣1, ␣2, ␣3, and ␣4), each with a unique glycosides is well documented and increases in intraceltissue distribution (Shull et al, 1986;Sweadner, 1989; lular Na ϩ and Ca 2ϩ have been observed during cardiac Lingrel et al, 1990;Shamraj and Lingrel, 1994).…”

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Identification of a Specific Role for the Na,K-ATPase α2 Isoform as a Regulator of Calcium in the Heart

et al. 1999

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It is well accepted that inhibition of the Na,K-ATPase in the heart, through effects on the Na/Ca exchanger, raises the intracellular Ca2+ concentration and strengthens cardiac contraction. However, the contribution that individual isoforms make to this calcium regulatory role is unknown. Assessing the phenotypes of mouse hearts with genetically reduced levels of Na,K-ATPase alpha 1 or alpha 2 isoforms clearly demonstrates different functional roles for these isoforms in vivo. Heterozygous alpha 2 hearts are hypercontractile as a result of increased calcium transients during the contractile cycle. In contrast, heterozygous alpha 1 hearts are hypocontractile. The different functional roles of these two isoforms are further demonstrated since inhibition of the alpha 2 isoform with ouabain increases the contractility of heterozygous alpha 1 hearts. These results definitively illustrate a specific role for the alpha 2 Na,K-ATPase isoform in Ca2+ signaling during cardiac contraction.

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Identification of a Specific Role for the Na,K-ATPase α2 Isoform as a Regulator of Calcium in the Heart

et al. 1999

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“…Consistent with a lowered permeability of Hg 2+ through an intact endothelial barrier (BBB + ), neuronal organoids that lacked an endothelial barrier (BBB − ) demonstrated significantly higher cell death, measured by reduced ATP production. That ATP production significantly increased in BBB + organoids exposed to mercury II chloride, is consistent with elevated demand for Na‐K‐ATPase activity [ 353 ] to sustain facilitated export of ions. That ATP production in BBB + organoids exposed to mercury II chloride was dependent on barrier activity was confirmed by permeabilizing with histamine, which lowered ATP production, indicating penetration of mercury.…”

Section: In Vitro Methods For the Assessment Of Drug Delivery To The Brainmentioning

confidence: 71%

Physiological and Pathological Factors Affecting Drug Delivery to the Brain by Nanoparticles

Islam

Leach

Smith³

et al. 2021

Advanced Science

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The prevalence of neurological/neurodegenerative diseases, such as Alzheimer's disease is known to be increasing due to an aging population and is anticipated to further grow in the decades ahead. The treatment of brain diseases is challenging partly due to the inaccessibility of therapeutic agents to the brain. An increasingly important observation is that the physiology of the brain alters during many brain diseases, and aging adds even more to the complexity of the disease. There is a notion that the permeability of the blood–brain barrier (BBB) increases with aging or disease, however, the body has a defense mechanism that still retains the separation of the brain from harmful chemicals in the blood. This makes drug delivery to the diseased brain, even more challenging and complex task. Here, the physiological changes to the diseased brain and aged brain are covered in the context of drug delivery to the brain using nanoparticles. Also, recent and novel approaches are discussed for the delivery of therapeutic agents to the diseased brain using nanoparticle based or magnetic resonance imaging guided systems. Furthermore, the complement activation, toxicity, and immunogenicity of brain targeting nanoparticles as well as novel in vitro BBB models are discussed.

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“…shows tissue-specific profile [62]. The overexpression of α1 subunit of Na + /K + -ATPase (ATP1A1) were observed in esophageal squamous cell carcinoma [63], non-small cell lung cancer and hepatocellular carcinoma, contributing to cancer proliferation and migration [64,65].…”

Section: Discussionmentioning

confidence: 99%

Quantitative ubiquitylomics reveals the ubiquitination regulation landscape in oral adenoid cystic carcinoma

et al. 2021

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Adenoid cystic carcinoma (ACC) is an extremely rare salivary gland tumor with a poor prognosis and needs attention on molecular mechanisms. Protein ubiquitination is an evolutionarily conserved post-translational modification (PTM) for substrates degradation and control diverse cellular functions. The board cellular function of ubiquitination network holds great promise to detect potential targets and identify respective receptors. Novel technologies are discovered for in-depth research and characterization the precise and dynamic regulation of ubiquitylomics in multiple cellular processes during cancer initiation, progression and treatment. In this study, 4D label free quantitative techniques of ubiquitination proteomics were used and we identified a total of 4152 ubiquitination sites in 1993 proteins. We also performed a systematic bioinformatics analysis for differential modified proteins and peptides containing quantitative information through the comparation between OACC tumor with adjacent normal tissues, as well as the identification of 8 protein clusters with motif analysis. Our findings offered an important reference of potential biomarkers and effective therapeutic targets for ACC.

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Na+,K(+)-ATPase.

Cited by 631 publications

References 50 publications

Identification of a Specific Role for the Na,K-ATPase α2 Isoform as a Regulator of Calcium in the Heart

Identification of a Specific Role for the Na,K-ATPase α2 Isoform as a Regulator of Calcium in the Heart

Physiological and Pathological Factors Affecting Drug Delivery to the Brain by Nanoparticles

Quantitative ubiquitylomics reveals the ubiquitination regulation landscape in oral adenoid cystic carcinoma

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