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Bioimaging for Advanced Explorations in Materials and Life Science

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Materials Science".

Deadline for manuscript submissions: closed (31 October 2023) | Viewed by 2413

Special Issue Editors


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Guest Editor
Department of Materials Science and Engineering, National Tsing Hua University, Hsinchu 40402, Taiwan
Interests: biomaterial; tissue engineering; nanomedicine

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Guest Editor
Master Program for Biomedical Engineering, China Medical University, Taichung 40402, Taiwan
Interests: regenerative medicine; cancer theranostics; immunotherapy; fluorescence techniques

Special Issue Information

Dear Colleagues, 

Bioimaging relates to methods that non-invasively visualize biological processes in real time. It is often used to gain information on the 3D structure of the observed specimen without too much physical interference. Recent developments using imaging by light and electromagnetics in medicine and biology have explored new horizons in biomedical research. For example, bioimaging has led to the design of an increasing number of nanosensors for monitoring intracellular ion and metabolite transportation. Resolutions ranging from nanometer to millimeter provide multiscale spatial information for accurately and precisely depicting the architecture of living organisms. Single-molecule/particle tracking techniques can even reveal the dynamics and kinetics of biomolecules in living cells, tissues, and organs.

The present Special Issue will focus on the innovative applications of biomaterials and the characterizations of their corresponding functions using state-of-the-art imaging techniques. The marriage of biomaterials and imaging techniques will also intrigue our investigation into the interplays of biology and materials science and may ignite the invention of advanced functional biomaterials. In this Special Issue, methods and materials for imaging-based characterization of molecular signatures that occur during cellular proliferation, differentiation, and internalization are very welcome (including but not limited to this application). Broad applications in tissue engineering, drug delivery, and nanomedicine are also invited in this Special Issue.

Prof. Dr. Tzu-wei Wang
Dr. Yen-Liang Liu
Guest Editors

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Keywords

  • bioimaging
  • real time
  • biomaterials
  • molecular biology

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Published Papers (1 paper)

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Research

16 pages, 4378 KiB  
Article
Opioid-Modulated Receptor Localization and Erk1/2 Phosphorylation in Cells Coexpressing μ-Opioid and Nociceptin Receptors
by Guan-Yu Zhuo, Ming-Chi Chen, Tzu-Yu Lin, Shih-Ting Lin, Daniel Tzu-Li Chen and Cynthia Wei-Sheng Lee
Int. J. Mol. Sci. 2023, 24(2), 1048; https://doi.org/10.3390/ijms24021048 - 5 Jan 2023
Cited by 4 | Viewed by 1937
Abstract
We attempted to examine the alterations elicited by opioids via coexpressed μ-opioid (MOP) and nociceptin/orphanin FQ (NOP) receptors for receptor localization and Erk1/2 (p44/42 MAPK) in human embryonic kidney (HEK) 293 cells. Through two-photon microscopy, the proximity of MOP and NOP receptors was [...] Read more.
We attempted to examine the alterations elicited by opioids via coexpressed μ-opioid (MOP) and nociceptin/orphanin FQ (NOP) receptors for receptor localization and Erk1/2 (p44/42 MAPK) in human embryonic kidney (HEK) 293 cells. Through two-photon microscopy, the proximity of MOP and NOP receptors was verified by fluorescence resonance energy transfer (FRET), and morphine but not buprenorphine facilitated the process of MOP-NOP heterodimerization. Single-particle tracking (SPT) further revealed that morphine or buprenorphine hindered the movement of the MOP-NOP heterodimers. After exposure to morphine or buprenorphine, receptor localization on lipid rafts was detected by immunocytochemistry, and phosphorylation of Erk1/2 was determined by immunoblotting in HEK 293 cells expressing MOP, NOP, or MOP+NOP receptors. Colocalization of MOP and NOP on lipid rafts was enhanced by morphine but not buprenorphine. Morphine stimulated the phosphorylation of Erk1/2 with a similar potency in HEK 293 cells expressing MOP and MOP+NOP receptors, but buprenorphine appeared to activate Erk1/2 solely through NOP receptors. Our results suggest that opioids can fine-tune the cellular localization of opioid receptors and phosphorylation of Erk1/2 in MOP+NOP-expressing cells. Full article
(This article belongs to the Special Issue Bioimaging for Advanced Explorations in Materials and Life Science)
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