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Chloride Transport across the Lysosomal Membrane
Published in Bruno Gasnier, Michael X. Zhu, Ion and Molecule Transport in Lysosomes, 2020
Sonali Saha, Anja Blessing, Thomas J. Jentsch
Lysosomes mediate a range of biological processes, such as the degradation of macromolecules, plasma membrane repair, regulation of cellular metabolism and immune response (Appelqvist et al., 2013; Ballabio, 2016; Settembre et al., 2013). For its normal function, the lysosome needs to generate and maintain an acidic luminal pH, a process which requires several ion-transporting proteins embedded in its limiting membrane (Scott and Gruenberg, 2011). Acidification of the lysosomal lumen is directly mediated by a V-type proton ATPase, which needs, however, parallel anion or cation conductive pathways to allow bulk proton transport by compensating the electric charge transported by the ATPase (Grabe and Oster, 2001).
Enzymes
Published in Stephen W. Carmichael, Susan L. Stoddard, The Adrenal Medulla 1986 - 1988, 2017
Stephen W. Carmichael, Susan L. Stoddard
Wang, Moriyama, Mandel et al. (1988) cloned a cDNA that coded for an accessory polypeptide of the proton ATPase from chromaffin vesicles. This cDNA encoded a 32 kDa polypeptide that has an apparent molecular weight of 39 which was previously denoted as subunit IV of the ATPase from chromaffin vesicles. Northern blots revealed the presence of a single mRNA in bovine adrenal medulla.
Amphotericin B Lipid Complex (ABLC)
Published in M. Lindsay Grayson, Sara E. Cosgrove, Suzanne M. Crowe, M. Lindsay Grayson, William Hope, James S. McCarthy, John Mills, Johan W. Mouton, David L. Paterson, Kucers’ The Use of Antibiotics, 2017
To a small extent, AmB inhibits membrane-associated enzymes, such as proton ATPase in fungal cells and Na+/K+-ATPase in mammalian cells (Brajtburg and Bolard, 1996). The polyenes do not penetrate past the fungal cell membrane and do not appear to have direct effects on intermediary metabolism or nucleic acid synthesis (Bates, 1993).
ATP6V1H facilitates osteogenic differentiation in MC3T3-E1 cells via Akt/GSK3β signaling pathway
Published in Organogenesis, 2019
Fusong Jiang, Haojie Shan, Chenhao Pan, Zubin Zhou, Keze Cui, Yuanliang Chen, Haibo Zhong, Zhibin Lin, Nan Wang, Liang Yan, Xiaowei Yu
ATP6V1H is one of the V-type proton ATPase family members, which are crucial for intracellular compartment acidification of eukaryotic cells, protein degradation regulation, facilitating cellular function and development.14,15 About 26.7% (4 in 15) SNPs in ATP6V1H genes in 1625 Han Chinese were significantly involved in low mineral density of spine bone.7 Furthermore, bone remodeling decreased, while bone resorption increased in ATP6V1H ± mice.7 Mechanically, the pH value increased in intracellular osteoclasts, which inhibited TGF-β1 activation and osteoblast formation, while the bone mineralization showed no great difference in ATP6V1H ± mice as compared with ATP6V1H +/+ mice.7
Shining a light on defective autophagy by proteomics approaches: implications for neurodegenerative illnesses
Published in Expert Review of Proteomics, 2019
Fabio Di Domenico, Ilaria Zuliani, Antonella Tramutola
Proteomic studies on PD, achieved so far only limited success in identifying markers able to facilitate disease diagnosis and monitoring, thus a global system biology approach using new models is needed. However, in one of the few proteomics studies performed authors identified the altered expression and HNE modification of autophagic components in different transgenic C. elegans expressing human LRRK2, one of the most common causative gene implied in familial PD [121]. In details, this study brings new knowledge on the possible interaction between LRRK2 (WT and mutated) and tau protein, as mutations in the tau encoding MAPT gene are linked to frontotemporal dementia with Parkinsonism [122]. Data collected in this proteomic work, demonstrated that the co-expression of human WT LRRK2 and tau lead to protein expression changes without altering the redox status, while mutated LRRK2 (G2019S or R1441C) leads to increased protein oxidation [121]. Interestingly, it is shown that LRRK2 expression affects protein biosynthesis and degradation, and the mutations appear to enhance this unfavorable outcome. Indeed, this study reveals the different expression and the increased protein-bound HNE levels of V0-type proton ATPase subunits during the co-expression of LRRK2 WT or mutated and tau, thus suggesting that the expression of LRRK2 led to the accumulation of increased autophagic vacuoles [121]. In support of these findings, it was previously reported that increased oxidative stress could affect the permeability of the lysosomal membrane [82,123]. In a different study, Triplett and coworkers performed the proteomic analysis of PINK1 KO mice brain, a further model of PD, showing that two subunits of V0-type proton ATPase were found to be altered in either phosphorylation or expression: V0-ATPase A and V0-ATPase F [124]. The impaired function of these two V0-ATPase has been well documented to be responsible of dysfunctional autophagy, as an alteration of lysosomal acidic environment [125]. Despite the proteomics analysis of PD models brought only partial comprehension about the potential alterations of the autophagic process involved in the disease, it is indisputable that the reduced acidification of lysosome represents a key factor in the loss of proteostasis during PD onset and progression.