Abstract
Toad urothelium barrier is the model to mimic and investigate urothelium permeability. Thiazide blocked ionic transportation in polarized membrane state. Jellyfish venom causes pores to be adjusted to urothelium permeability which improved polarization. This study aimed at CfTX-1 peptide in urothelium permeability evoked polarizations. Thiazide pretreated toad urothelium permeability to ions were investigated in modified Ussing chamber. Thiazide urothelium were further intervened by CfTX-1 peptide and treated with G-protein receptor agonists. 0.1 mol CaCl2 activated transurothelium potential differences were recorded by unipolar lead and computerized by fast Fourier transform technique. Apical chamber was settled as anode. The amplitude of potential differences were evaluated to determine the urothelium polarizations. The results indicated that CaCl2 activation induced a positive monophasic wave in thiazide urothelium, which suggested the urothelium was slightly polarized and significantly enhancive in adrenergic receptor treated urothelium. Furthermore, CfTX-1 peptide enhanced transurothelium potential difference in thiazide urothelium, therefore, urothelium were supra polarized. NPPB treatment significantly attenuated this supra polarization, which suggested that the Cl- influx was the main stream ionic compound of this polarization. It is concluded that CfTX-1 peptide was considered to generate supra polarization in thiazide urothelium. This mechanism is useful to study the improvement of drug delivery crossing urothelium barrier. Key words: CfTX-1 partial sequence, toad urothelium, supra polarization, Cl- permeability.
Highlights
As the Chironex fleckeri Toxin 1 (CfTX-1) Nterminal was function as the cellular outer membrane porin protein (OmpD), this study forward investigated this partial sequence of CfTX-1 evoking ionic permeability induced TPD in HCTZ urothelium
The results revealed that the CfTX-1 peptide represented enhanced positive peak potentials in anode on apical membrane, generated supra polarization on HCTZ urothelium
CfTX-1 peptide is a partial sequence of Chironex fleckeri toxins, which was identified from Aurelia aurita nematocysts from Qiongzhou Strait, Hainan province, China
Summary
(Helmholz et al, 2007), have a preferentially postsynaptic action at the neuromuscular junction by inhibiting acetylcholine binding to postsynaptic acetylcholine receptors (Ponce et al, 2013). Jellyfish venom, such as Carybdea rastoni, Chiropsalmus quadrigatus, contained diversified toxic isoforms were classified into at least two distinct subfamilies, type I and II. The structural homology of Chironex fleckeri toxins and Cry toxins suggest that the toxins may have a similar pore-forming mechanism of action involving helices from the N-terminal domain (Brinkman, 2014), while structural variability within the toxin family may modulate receptor specificity. CfTX-like toxins may be involved in oligomerization and pore formation on erythrocytes, and other susceptible cells (Brinkman, 2007)
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