Kim, J.-H. Hong, Y.-H. Lee, J.-H. Kim, D.-H. Nam, G. Jeong, S.M. Lee, B.-H. Lee, S.-M. Nah, S.-Y. 2024-01-21T05:37:13Z 2024-01-21T05:37:13Z 2021-09-02 2005-02 1016-8478 https://pubs.kist.re.kr/handle/201004/136806 We showed recently that ginsenosides inhibit the activity of various types of ion channel. Here we have investigated the role of the carbohydrate component of ginsenoside Rg3 in the inhibition of Na+ channels. The channels were expressed in Xenopus oocytes by injecting cRNAs encoding rat brain Nav1.2α and β1 subunits, and analyzed by the two-electrode voltage clamp technique. Treatment with Rg3 reversibly inhibited the inward Na+ peak current (INa) with an IC50 of 32.2 ± 4.5 μM, and the inhibition was voltage-dependent. To examine the role of the sugar moiety, we prepared a straight chain form of the second glucose and a conjugate of this glucose with 3-(4-hydroxyphenyl) propionic acid hydrazide (HPPH). Neither derivative inhibited INa. Treatment with the carbohydrate portion of ginsenoside Rg3, sophorose [β-D-glucopyranosyl (1→2)-β-glucopyranoside], or the aglycone (protopanaxadiol), on their own or in combination had no effect on I Na. These observations indicate that the carbohydrate portion of ginsenoside Rg3 plays an important role in its effect on the Na + channel. ？KSMCB 2005. English KOREAN SOC MOLECULAR & CELLULAR BIOLOGY aglycone carbohydrate ginsenoside Rg 3 glucose hydrazide derivative protein subunit RNA sodium channel sophorose sugar ginsenoside ginsenoside Rg 3 glucan nerve protein protopanaxadiol sapogenin sodium channel sodium channel, voltage gated, type II, alpha 1 sodium channel, voltage-gated, type II, alpha 1 sophorose triterpene animal cell animal tissue article brain tissue chemical structure controlled study drug inhibition electrode nonhuman oocyte rat voltage clamp Xenopus animal chemistry drug effect nerve cell patch clamp physiology structure activity relation Animalia Animals Ginsenosides Glucans Nerve Tissue Proteins Neurons Oocytes Patch-Clamp Techniques Sapogenins Sodium Channels Structure-Activity Relationship Triterpenes Xenopus A role for the carbohydrate portion of ginsenoside Rg3 in Na+ channel inhibition Article 1 Molecules and Cells, v.19, no.1, pp.137 - 142 Molecules and Cells 19 1 137 142 scie scopus kci ART001189962 000227439900018 2-s2.0-22844450289 Biochemistry & Molecular Biology Cell Biology Biochemistry & Molecular Biology Cell Biology Article aglycone carbohydrate ginsenoside Rg 3 glucose hydrazide derivative protein subunit RNA sodium channel sophorose sugar ginsenoside ginsenoside Rg 3 glucan nerve protein protopanaxadiol sapogenin sodium channel sodium channel, voltage gated, type II, alpha 1 sodium channel, voltage-gated, type II, alpha 1 sophorose triterpene animal cell animal tissue article brain tissue chemical structure controlled study drug inhibition electrode nonhuman oocyte rat voltage clamp Xenopus animal chemistry drug effect nerve cell patch clamp physiology structure activity relation Animalia Animals Ginsenosides Glucans Nerve Tissue Proteins Neurons Oocytes Patch-Clamp Techniques Sapogenins Sodium Channels Structure-Activity Relationship Triterpenes Xenopus Aglycone Brain Na+ Channel Carbohydrate Portion Ginsenoside Rg3