Single molecule localizations of voltage-gated sodium channel NaV1.5 on the surfaces of normal and cancer breast cells. Issue 15 (24th March 2023)
- Record Type:
- Journal Article
- Title:
- Single molecule localizations of voltage-gated sodium channel NaV1.5 on the surfaces of normal and cancer breast cells. Issue 15 (24th March 2023)
- Main Title:
- Single molecule localizations of voltage-gated sodium channel NaV1.5 on the surfaces of normal and cancer breast cells
- Authors:
- Li, Xinyu
Zhao, Li
Feng, Rongrong
Du, Xiaowei
Guo, Zelin
Meng, Yu
Zou, Yulan
Liao, Wenchao
Liu, Qiyuan
Sheng, Yaohuan
Zhao, Gaowei
Zhong, Haijian
Zhao, Weidong - Abstract:
- Abstract : The NaV 1.5 on cellular membranes of normal and cancer breast cells can be localized at single molecule spatial resolution level, and the interactions between the NaV 1.5 and antibody can be detected at picoNewton force resolution level. Abstract : Voltage-gated sodium channels (VGSCs) are widely expressed in various types of tumor and cancer cells, and NaV 1.5 is overexpressed in highly metastatic breast cancer cells. There may be positive relations between the expression levels of NaV 1.5 and breast cancer recurrence and metastasis. Herein, NaV 1.5 was detected and localized on the surfaces of normal and cancer breast cells by the single molecule recognition imaging (SMRI) mode of atomic force microscopy (AFM). The results reveal that NaV 1.5 was irregularly distributed on the surfaces of normal and cancer breast cells. The NaV 1.5 has an area percentage of 0.6% and 7.2% on normal and cancer breast cells, respectively, which indicates that there is more NaV 1.5 on cancer cells than on normal cells. The specific interaction forces and binding kinetics in the NaV 1.5–antibody complex system were investigated with the single molecule force spectroscopy (SMFS) mode of AFM, indicating that the stability of the NaV 1.5–antibody on normal breast cells is higher than that on cancer breast cells. All these results will be useful to study the interactions of other ion channel–antibody systems, and will also be useful to understand the role of sodium channels in tumorAbstract : The NaV 1.5 on cellular membranes of normal and cancer breast cells can be localized at single molecule spatial resolution level, and the interactions between the NaV 1.5 and antibody can be detected at picoNewton force resolution level. Abstract : Voltage-gated sodium channels (VGSCs) are widely expressed in various types of tumor and cancer cells, and NaV 1.5 is overexpressed in highly metastatic breast cancer cells. There may be positive relations between the expression levels of NaV 1.5 and breast cancer recurrence and metastasis. Herein, NaV 1.5 was detected and localized on the surfaces of normal and cancer breast cells by the single molecule recognition imaging (SMRI) mode of atomic force microscopy (AFM). The results reveal that NaV 1.5 was irregularly distributed on the surfaces of normal and cancer breast cells. The NaV 1.5 has an area percentage of 0.6% and 7.2% on normal and cancer breast cells, respectively, which indicates that there is more NaV 1.5 on cancer cells than on normal cells. The specific interaction forces and binding kinetics in the NaV 1.5–antibody complex system were investigated with the single molecule force spectroscopy (SMFS) mode of AFM, indicating that the stability of the NaV 1.5–antibody on normal breast cells is higher than that on cancer breast cells. All these results will be useful to study the interactions of other ion channel–antibody systems, and will also be useful to understand the role of sodium channels in tumor metastasis and invasion. … (more)
- Is Part Of:
- Analytical methods. Volume 15:Issue 15(2023)
- Journal:
- Analytical methods
- Issue:
- Volume 15:Issue 15(2023)
- Issue Display:
- Volume 15, Issue 15 (2023)
- Year:
- 2023
- Volume:
- 15
- Issue:
- 15
- Issue Sort Value:
- 2023-0015-0015-0000
- Page Start:
- 1855
- Page End:
- 1860
- Publication Date:
- 2023-03-24
- Subjects:
- Chemistry, Analytic -- Periodicals
Analytical biochemistry -- Periodicals
Chemical laboratories -- Standards -- Periodicals
543.1905 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/AY ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d3ay00208j ↗
- Languages:
- English
- ISSNs:
- 1759-9660
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0897.103700
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 26929.xml