scholarly journals Erratum of the article: Expressional and Functional Characterization of Intracellular pH Regulators and Effetcs of Ethanol in Human Oral Epidermoid Carcinoma Cells

2019 ◽  
Vol 52 (6) ◽  
pp. 1584-1584
2018 ◽  
Vol 47 (5) ◽  
pp. 2056-2068 ◽  
Author(s):  
Shiao-Pieng Lee ◽  
Shih-Chi Chao ◽  
Shu-Fu Huang ◽  
Yen-Lin Chen ◽  
Yi-Ting Tsai ◽  
...  

Background/Aims: To functionally characterize intracellular pH (pHi) regulating mechanisms, such as Na+-H+ exchanger (NHE) and Na+-HCO3- co-transporter (NBC), and further examine effects of ethanol on the pHi regulating mechanism in human oral epidermoid carcinoma (OEC-M1) cells. Methods: OEC-M1 cells were a gift from Tri-Service General Hospital. Changes of pHi were detected by microspectrofluroimetry with a pH-sensitive fluorescent dye, BCECF. Isoforms of transporters were examined by Western blot technique. Results: i) the steady-state pHi value shifted from alkaline (7.35∼7.49) to acidic (7.0∼7.03) following acid/base impacts; ii) in HEPES-buffer system, pHi recovery following induced-acidification was totally blocked by either removing [Na]o+ or adding HOE 694 (a NHE1 specific inhibitor), which demonstrates existence of NHE1; iii) in HCO3-/CO2-buffer system, the pHi recovery following induced-acidification was entirely blocked by either removing [Na]o+ or adding HOE 694 plus DIDS (a NBC specific inhibitor), which suggests existence of Na+- and HCO3–dependent acid-extruder, i.e. NBC; iv) the isoforms of the two acid extruders were NHE1, NBCn1, NBCe1 and NDCBE; v) ethanol (10-1000 mM) showed a biphasic and concentration-dependent effect on resting pHi (i.e. increase then decrease) by changing the activity of NHE1 and NBC accordingly; vi) treatment with ethanol for 24 hr (<unterline>></unterline> 300 mM) significantly inhibited the expression of NHE1, NBCn1 and NDCBE, while up-regulated NBCe1. Conclusions: Ethanol affects pHi in a concentration-dependent manner by changing function and expression of NHE1 and NBC isoforms in OEC-M1 cells.


2004 ◽  
Vol 205 (2) ◽  
pp. 215-226 ◽  
Author(s):  
Jung Hoon Yoon ◽  
Youn Bae Kim ◽  
Myong Soo Kim ◽  
Joo Cheol Park ◽  
Joong Ki Kook ◽  
...  

Biochemistry ◽  
2015 ◽  
Vol 54 (18) ◽  
pp. 2895-2902 ◽  
Author(s):  
Huaxia Luo ◽  
Yu Sun ◽  
Guifeng Wei ◽  
Jianjun Luo ◽  
Xinling Yang ◽  
...  

2006 ◽  
Vol 449 (1) ◽  
pp. 48-61
Author(s):  
Riccardo Alessandro ◽  
Maria Antonietta Di Bella ◽  
Anna Maria Flugy ◽  
Simona Fontana ◽  
Francesca Damiani ◽  
...  

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Qingfeng Chen ◽  
Weizhong Zeng ◽  
Ji She ◽  
Xiao-chen Bai ◽  
Youxing Jiang

The otopetrin (OTOP) proteins were recently characterized as proton channels. Here we present the cryo-EM structure of OTOP3 from Xenopus tropicalis (XtOTOP3) along with functional characterization of the channel. XtOTOP3 forms a homodimer with each subunit containing 12 transmembrane helices that can be divided into two structurally homologous halves; each half assembles as an α-helical barrel that could potentially serve as a proton conduction pore. Both pores open from the extracellular half before becoming occluded at a central constriction point consisting of three highly conserved residues – Gln232/585-Asp262/Asn623-Tyr322/666 (the constriction triads). Mutagenesis shows that the constriction triad from the second pore is less amenable to perturbation than that of the first pore, suggesting an unequal contribution between the two pores to proton transport. We also identified several key residues at the interface between the two pores that are functionally important, particularly Asp509, which confers intracellular pH-dependent desensitization to OTOP channels.


Author(s):  
Juergen Berlanda ◽  
Tobias Kiesslich ◽  
Christian Benno Oberdanner ◽  
Franz Josef Obermair ◽  
Barbara Krammer ◽  
...  

Toxins ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 661 ◽  
Author(s):  
Salomón Huancahuire-Vega ◽  
Luciana M. Hollanda ◽  
Mauricio Gomes-Heleno ◽  
Edda E. Newball-Noriega ◽  
Sergio Marangoni

This work reports the purification and biochemical and functional characterization of ACP-TX-I and ACP-TX-II, two phospholipases A2 (PLA2) from Agkistrodon contortrix pictigaster venom. Both PLA2s were highly purified by a single chromatographic step on a C18 reverse phase HPLC column. Various peptide sequences from these two toxins showed similarity to those of other PLA2 toxins from viperid snake venoms. ACP-TX-I belongs to the catalytically inactive K49 PLA2 class, while ACP-TX-II is a D49 PLA2, and is enzymatically active. ACP-TX-I PLA2 is monomeric, which results in markedly diminished myotoxic and inflammatory activities when compared with dimeric K49 PLA2s, confirming the hypothesis that dimeric structure contributes heavily to the profound myotoxicity of the most active viperid K49 PLA2s. ACP-TX-II exhibits the main pharmacological actions reported for this protein family, including in vivo local myotoxicity, edema-forming activity, and in vitro cytotoxicity. ACP-TX-I PLA2 is cytotoxic to A549 lung carcinoma cells, indicating that cytotoxicity to these tumor cells does not require enzymatic activity.


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