Interactions of β tubulin isotypes with glutathione in differentiated neuroblastoma cells subject to oxidative stress
Microtubules are a major component of the neuronal cytoskeleton. Tubulin, the subunit protein of microtubules, is an α/β heterodimer. Both α and β exist as families of isotypes, whose members are encoded by different genes and have different amino acid sequences. The βII and βIII isotypes are very p...
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| Published in | Cytoskeleton (Hoboken, N.J.) Vol. 75; no. 7; pp. 283 - 289 |
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| Abstract | Microtubules are a major component of the neuronal cytoskeleton. Tubulin, the subunit protein of microtubules, is an α/β heterodimer. Both α and β exist as families of isotypes, whose members are encoded by different genes and have different amino acid sequences. The βII and βIII isotypes are very prominent in the nervous system. Our previous work has suggested that βII may play a role in neuronal differentiation, but the role of βIII in neurons is not well understood. In the work reported here, we examined the roles of the different β‐tubulin isotypes in response to glutamate/glycine treatment, and found that both βII and βIII bind to glutathione in the presence of ROS, especially βIII. In contrast, βI did not bind to glutathione. Our results suggest that βII and βIII, but especially βIII, may play an important role in the response of neuronal cells to stress. In view of the high levels of βII and βIII expressed in the nervous system it is conceivable that these tubulin isotypes may use their sulfhydryl groups to scavenge ROS and protect neuronal cells against oxidative stress. |
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| AbstractList | Microtubules are a major component of the neuronal cytoskeleton. Tubulin, the subunit protein of microtubules, is an α/β heterodimer. Both α and β exist as families of isotypes, whose members are encoded by different genes and have different amino acid sequences. The βII and βIII isotypes are very prominent in the nervous system. Our previous work has suggested that βII may play a role in neuronal differentiation, but the role of βIII in neurons is not well understood. In the work reported here, we examined the roles of the different β‐tubulin isotypes in response to glutamate/glycine treatment, and found that both βII and βIII bind to glutathione in the presence of ROS, especially βIII. In contrast, βI did not bind to glutathione. Our results suggest that βII and βIII, but especially βIII, may play an important role in the response of neuronal cells to stress. In view of the high levels of βII and βIII expressed in the nervous system it is conceivable that these tubulin isotypes may use their sulfhydryl groups to scavenge ROS and protect neuronal cells against oxidative stress. Microtubules are a major component of the neuronal cytoskeleton. Tubulin, the subunit protein of microtubules, is an α/β heterodimer. Both α and β exist as families of isotypes, whose members are encoded by different genes and have different amino acid sequences. The βII and βIII isotypes are very prominent in the nervous system. Our previous work has suggested that βII may play a role in neuronal differentiation, but the role of βIII in neurons is not well understood. In the work reported here, we examined the roles of the different β-tubulin isotypes in response to glutamate/glycine treatment, and found that both βII and βIII bind to glutathione in the presence of ROS, especially βIII. In contrast, βI did not bind to glutathione. Our results suggest that βII and βIII, but especially βIII, may play an important role in the response of neuronal cells to stress. In view of the high levels of βII and βIII expressed in the nervous system it is conceivable that these tubulin isotypes may use their sulfhydryl groups to scavenge ROS and protect neuronal cells against oxidative stress.Microtubules are a major component of the neuronal cytoskeleton. Tubulin, the subunit protein of microtubules, is an α/β heterodimer. Both α and β exist as families of isotypes, whose members are encoded by different genes and have different amino acid sequences. The βII and βIII isotypes are very prominent in the nervous system. Our previous work has suggested that βII may play a role in neuronal differentiation, but the role of βIII in neurons is not well understood. In the work reported here, we examined the roles of the different β-tubulin isotypes in response to glutamate/glycine treatment, and found that both βII and βIII bind to glutathione in the presence of ROS, especially βIII. In contrast, βI did not bind to glutathione. Our results suggest that βII and βIII, but especially βIII, may play an important role in the response of neuronal cells to stress. In view of the high levels of βII and βIII expressed in the nervous system it is conceivable that these tubulin isotypes may use their sulfhydryl groups to scavenge ROS and protect neuronal cells against oxidative stress. |
| Author | Guo, Jiayan Ludueña, Richard F. Asmis, Reto Kim, Hong Seok |
| AuthorAffiliation | 1 Department of Biochemistry, University of Texas Health Science Center at San Antonio, San Antonio, TX 72290-3900, USA 3 Department of Molecular Medicine, College of Medicine, Inha University, Incheon 22212, Republic of Korea 2 Department of Clinical Laboratory Science, University of Texas Health Science Center at San Antonio, San Antonio, TX 72290-3900, USA |
| AuthorAffiliation_xml | – name: 2 Department of Clinical Laboratory Science, University of Texas Health Science Center at San Antonio, San Antonio, TX 72290-3900, USA – name: 3 Department of Molecular Medicine, College of Medicine, Inha University, Incheon 22212, Republic of Korea – name: 1 Department of Biochemistry, University of Texas Health Science Center at San Antonio, San Antonio, TX 72290-3900, USA |
| Author_xml | – sequence: 1 givenname: Jiayan surname: Guo fullname: Guo, Jiayan organization: University of Texas Health Science Center at San Antonio – sequence: 2 givenname: Hong Seok surname: Kim fullname: Kim, Hong Seok organization: Inha University – sequence: 3 givenname: Reto surname: Asmis fullname: Asmis, Reto organization: University of Texas Health Science Center at San Antonio – sequence: 4 givenname: Richard F. surname: Ludueña fullname: Ludueña, Richard F. email: luduena@uthscsa.edu organization: University of Texas Health Science Center at San Antonio |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29663696$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_3390_ijms241814161 crossref_primary_10_3389_fnmol_2022_838393 crossref_primary_10_1080_10715762_2019_1623398 crossref_primary_10_3389_fcell_2022_870088 crossref_primary_10_1089_ars_2021_0199 |
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| Keywords | tubulin microtubules glutathionylation oxidative stress |
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| SubjectTerms | Cytoskeleton Glutathione glutathionylation Glycine Isotypes Microtubules Nervous system Neuroblastoma Neuroblasts Oxidative stress Sulfhydryl groups Tubulin |
| Title | Interactions of β tubulin isotypes with glutathione in differentiated neuroblastoma cells subject to oxidative stress |
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