scholarly journals Sequential deletion of CD63 identifies topologically distinct scaffolds for surface engineering of exosomes in living human cells

Nanoscale ◽  
2020 ◽  
Vol 12 (22) ◽  
pp. 12014-12026 ◽  
Author(s):  
Natalie Curley ◽  
Daniel Levy ◽  
Mai Anh Do ◽  
Annie Brown ◽  
Zachary Stickney ◽  
...  
Keyword(s):  
Surface Engineering ◽  
Transmembrane Protein ◽  
Human Cells ◽  
Engineering Applications

The native exosome transmembrane protein, CD63 can be modified for surface engineering applications.

scholarly journals Nanoarchitectonics meets cell surface engineering: shape recognition of human cells by halloysite-doped silica cell imprints

2019 ◽  
Vol 10 ◽  
pp. 1818-1825 ◽  
Author(s):  
Elvira Rozhina ◽  
Ilnur Ishmukhametov ◽  
Svetlana Batasheva ◽  
Farida Akhatova ◽  
Rawil Fakhrullin
Keyword(s):  
Cell Surface ◽  
Hela Cells ◽  
Surface Engineering ◽  
Human Cells ◽  
Live Cells ◽  
Liquid Media ◽  
Cell Surface Engineering ◽  
Produce Cell ◽  
Silica Cell ◽  
Clay Nanotubes

Cell surface engineering, as a practical manifestation of nanoarchitectonics, is a powerful tool to modify and enhance properties of live cells. In turn, cells may serve as sacrificial templates to fabricate cell-mimicking materials. Herein we report a facile method to produce cell-recognising silica imprints capable of the selective detection of human cells. We used HeLa cells to template silica inorganic shells doped with halloysite clay nanotubes. The shells were destroyed by sonication resulting in the formation of polydisperse hybrid imprints that were used to recognise HeLa cells in liquid media supplemented with yeast. We believe that methodology reported here will find applications in biomedical and clinical research.

scholarly journals Yeast as a Tool for Deeper Understanding of Human Manganese-Related Diseases

Genes ◽  
2019 ◽  
Vol 10 (7) ◽  
pp. 545
Author(s):  
Thines ◽  
Deschamps ◽  
Stribny ◽  
Morsomme
Keyword(s):  
Molecular Mechanisms ◽  
Transmembrane Protein ◽  
Friedreich Ataxia ◽  
Human Cells ◽  
Congenital Disorder ◽  
Yeast Cells ◽  
Enzymatic Antioxidant ◽  
Congenital Disorder Of Glycosylation ◽  
Biological Importance ◽  
Insight Into

The biological importance of manganese lies in its function as a key cofactor for numerous metalloenzymes and as non-enzymatic antioxidant. Due to these two essential roles, it appears evident that disturbed manganese homeostasis may trigger the development of pathologies in humans. In this context, yeast has been extensively used over the last decades to gain insight into how cells regulate intra-organellar manganese concentrations and how human pathologies may be related to disturbed cellular manganese homeostasis. This review first summarizes how manganese homeostasis is controlled in yeast cells and how this knowledge can be extrapolated to human cells. Several manganese-related pathologies whose molecular mechanisms have been studied in yeast are then presented in the light of the function of this cation as a non-enzymatic antioxidant or as a key cofactor of metalloenzymes. In this line, we first describe the Transmembrane protein 165-Congenital Disorder of Glycosylation (TMEM165-CDG) and Friedreich ataxia pathologies. Then, due to the established connection between manganese cations and neurodegeneration, the Kufor–Rakeb syndrome and prion-related diseases are finally presented.

Fibrous filter techniques for aerosol collection in surface engineering applications

2009 ◽  
Vol 2 (1/2) ◽  
pp. 155
Author(s):  
Monica Rodriguez ◽  
Rod Handy ◽  
Mark J. Jackson ◽  
Dave Goodman ◽  
Grant Robinson
Keyword(s):  
Surface Engineering ◽  
Fibrous Filter ◽  
Engineering Applications

Manufacturing of metal-based microparts: Fabrication strategies and surface engineering applications

2013 ◽  
Vol 237 ◽  
pp. 390-401 ◽  
Author(s):  
Yang Mu ◽  
Ke Chen ◽  
Bin Lu ◽  
W.J. Meng ◽  
G.L. Doll
Keyword(s):  
Surface Engineering ◽  
Engineering Applications

scholarly journals Transmembrane protein TMEM170A is a newly discovered regulator of ER and nuclear envelope morphogenesis in human cells

2016 ◽  
Vol 129 (8) ◽  
pp. 1552-1565 ◽  
Author(s):  
Andri Christodoulou ◽  
Rachel Santarella-Mellwig ◽  
Niovi Santama ◽  
Iain W. Mattaj
Keyword(s):  
Nuclear Envelope ◽  
Transmembrane Protein ◽  
Human Cells

P-glycoprotein–actin association through ERM family proteins: a role in P-glycoprotein function in human cells of lymphoid origin

Blood ◽  
2002 ◽  
Vol 99 (2) ◽  
pp. 641-648 ◽  
Author(s):  
Francesca Luciani ◽  
Agnese Molinari ◽  
Francesco Lozupone ◽  
Annarica Calcabrini ◽  
Luana Lugini ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Actin Cytoskeleton ◽  
Antisense Oligonucleotides ◽  
Transmembrane Protein ◽  
Human Cells ◽  
Lymphoid Cells ◽  
Ion Pump ◽  
Resistant Variant ◽  
Resistance Phenotype ◽  
P Glycoprotein

Abstract P-glycoprotein is a 170-kd glycosylated transmembrane protein, expressed in a variety of human cells and belonging to the adenosine triphosphate–binding cassette transporter family, whose membrane expression is functionally associated with the multidrug resistance phenotype. However, the mechanisms underlying the regulation of P-glycoprotein functions remain unclear. On the basis of some evidence suggesting P-glycoprotein–actin cytoskeleton interaction, this study investigated the association of P-glycoprotein with ezrin, radixin, and moesin, a class of proteins that cross-link actin filaments with plasma membrane in a human cell line of lymphoid origin and that have been shown to link other ion-pump–related proteins. To this purpose, a multidrug-resistant variant of CCRF-CEM cells (CEM-VBL100) was used as a model to investigate the following: (1) the cellular localizations of P-glycoprotein and ezrin, radixin, and moesin and their molecular associations; and (2) the effects of ezrin, radixin, and moesin antisense oligonucleotides on multidrug resistance and P-glycoprotein function. The results showed that: (1) P-glycoprotein colocalized and coimmunoprecipitated with ezrin, radixin, and moesin; and (2) treatment with antisense oligonucleotides for ezrin, radixin, and moesin restored drug susceptibility consistently with inhibition of both drug efflux and actin–P-glycoprotein association and induction of cellular redistribution of P-glycoprotein. These data suggest that P-glycoprotein association with the actin cytoskeleton through ezrin, radixin, and moesin is key in conferring to human lymphoid cells a multidrug resistance phenotype. Strategies aimed at inhibiting P-glycoprotein–actin association may be helpful in increasing the efficiency of both antitumor and antiviral therapies.

Sign in / Sign up

Export Citation Format

Share Document