Matching Items (35)
Description
Cell fusion is a process that occurs in normal cells as well as in pathological cells. This process does not occur spontaneously, fusogens are required to mediate the process. Syncytin is one of the proteins that was determined to have fusogenic properties. Syncytin is a newly discovered transmembrane protein that is generally expressed in mammalian placenta and it is known for its role in cell fusion during placentation. The recent studies in Ugarova’s laboratory suggest syncytin is expressed in macrophages, thus it may be involved in macrophage cells fusion. This paper provides a literature review of syncytin protein; it also contains an experimental study conducted to determine syncytin expression on both RNA and protein level. The study was conducted on RNA and protein isolated from macrophages isolated from mouse peritoneum. Agarose gel electrophoresis and Western blot analysis were used to determine syncytin expression on RNA and protein level respectively. Using these methods, syncytin expression was determined at different time points during macrophage fusion. The results show that syncytin is not expressed in freshly isolated macrophages, but its expression is initiated during macrophage adhesion in the presence of IL-4.
ContributorsKamayirese, Seraphine (Author) / Ugarova, Tatiana (Thesis director) / Podolnikova, Nataly (Committee member) / Wang, Xu (Committee member) / School of Molecular Sciences (Contributor) / Edson College of Nursing and Health Innovation (Contributor) / Barrett, The Honors College (Contributor)
Created2019-05
Description
We have produced stretchable lithium-ion batteries (LIBs) using the concept of kirigami, i.e., a combination of folding and cutting. The designated kirigami patterns have been discovered and implemented to achieve great stretchability (over 150%) to LIBs that are produced by standardized battery manufacturing. It is shown that fracture due to cutting and folding is suppressed by plastic rolling, which provides kirigami LIBs excellent electrochemical and mechanical characteristics. The kirigami LIBs have demonstrated the capability to be integrated and power a smart watch, which may disruptively impact the field of wearable electronics by offering extra physical and functionality design spaces.
ContributorsSong, Zeming (Author) / Wang, Xu (Author) / Lv, Cheng (Author) / An, Yonghao (Author) / Liang, Mengbing (Author) / Ma, Teng (Author) / He, David (Author) / Zheng, Ying-Jie (Author) / Huang, Shi-Qing (Author) / Yu, Hongyu (Author) / Jiang, Hanqing (Author) / Ira A. Fulton Schools of Engineering (Contributor)
Created2015-06-11
Description
The transient receptor potential channel subfamily V member 1 (TRPV1) functions as the heat and capsaicin receptor. It can be activated by heat, protons, pungent chemicals, and a variety of other endogenous mediators of nociception. TRPV1 is a non-selective cation channel consisting of 6 transmembrane domains (S1-S6), with helices S1-S4 forming the sensing domain and the S5-S6 helices forming the pore domain. Understanding the TRPV1 channel is imperative due to its relation to a variety of human diseases, including cancer, type II diabetes, hyper and hypothermia, and inflammatory disorders of the airways and bladder. Although TRPV1 is the best-studied thermosensitive-TRP channels of all the 28 family members, the molecular underpinning and the contributions of the human TRPV1 pore domain in thermo-sensing remains elusive. Recently, the human TRPV1 sensing domain was found to contribute to heat activation. It was found to undergo a non-denaturing temperature-dependent conformational change. This finding triggered interest in studying the function and the role of the human TRPV1 pore domain in the heat activation process. Specifically, to identify whether heat activation is intrinsic to the pore domain. This thesis paper explores and optimizes the purification protocol of the human TRPV1 pore domain through three different methods. The first method was using a denaturant, the second method was increasing the length of the histidine tags through Q5 insertion, and the third method was incorporating the protein construct into nanodiscs. In addition to the above three methods, size exclusion chromatography and ion-exchange chromatography were utilized after thrombin cleavage to separate the human TRPV1 pore domain from the cleaved MBP deca-histidine tags as well as the impurities.
ContributorsChang, Yu Tzu (Author) / Van Horn, Wade (Thesis director) / Wang, Xu (Committee member) / Cherry, Brian (Committee member) / School of Molecular Sciences (Contributor) / School of Life Sciences (Contributor) / Barrett, The Honors College (Contributor)
Created2020-12
Description
Carbohydrates are one of the four main building blocks of life, and are categorized as monosaccharides (sugars), oligosaccharides and polysaccharides. Each sugar can exist in two alternative anomers (in which a hydroxy group at C-1 takes different orientations) and each pair of sugars can form different epimers (isomers around the stereocentres connecting the sugars). This leads to a vast combinatorial complexity, intractable to mass spectrometry and requiring large amounts of sample for NMR characterization. Combining measurements of collision cross section with mass spectrometry (IM–MS) helps, but many isomers are still difficult to separate. Here, we show that recognition tunnelling (RT) can classify many anomers and epimers via the current fluctuations they produce when captured in a tunnel junction functionalized with recognition molecules. Most importantly, RT is a nanoscale technique utilizing sub-picomole quantities of analyte. If integrated into a nanopore, RT would provide a unique approach to sequencing linear polysaccharides.
ContributorsIm, Jong One (Author) / Biswas, Sovan (Author) / Liu, Hao (Author) / Zhao, Yanan (Author) / Sen, Suman (Author) / Biswas, Sudipta (Author) / Ashcroft, Brian (Author) / Borges, Chad (Author) / Wang, Xu (Author) / Lindsay, Stuart (Author) / Zhang, Peiming (Author) / Biodesign Institute (Contributor) / Single Molecule Biophysics (Contributor) / College of Liberal Arts and Sciences (Contributor) / Department of Physics (Contributor) / School of Molecular Sciences (Contributor)
Created2016-12-21
Description
Structural mechanisms behind variations in glycosaminoglycan (GAG) affinities of decorin-binding protein As (DBPAs) from different Borrelia strains were investigated using NMR. DBPA from strain PBr was revealed to have an additional GAG-binding epitope and a retracted linker allowing more access to its GAG-binding sites.
ContributorsMorgan, Ashli (Author) / Wang, Xu (Author) / Department of Chemistry and Biochemistry (Contributor)
Created2015-05-01