Super-resolution imaging of cancer-associated carbohydrates using aptamer probes

Nanoscale ◽  
2019 ◽  
Vol 11 (31) ◽  
pp. 14879-14886 ◽  
Author(s):  
Yingying Jing ◽  
Junling Chen ◽  
Lulu Zhou ◽  
Jiayin Sun ◽  
Mingjun Cai ◽  
...  

Relying on fluorophore-conjugated aptamers, we revealed the high expression and clustered distribution of globo H on cancer cell membranes and uncovered the potential interactions between cancer-associated carbohydrates via super-resolution imaging.

ACS Omega ◽  
2020 ◽  
Vol 5 (50) ◽  
pp. 32456-32465
Author(s):  
Yilin Fu ◽  
Peiyan Hua ◽  
Yan Lou ◽  
Zihao Li ◽  
Meng Jia ◽  
...  

2020 ◽  
Author(s):  
Pierre Mangeol ◽  
Dominique Massey-Harroche ◽  
Fabrice Richard ◽  
Pierre-François Lenne ◽  
André Le Bivic

AbstractEpithelial tissues acquire their integrity and function through the apico-basal polarization of their constituent cells. Proteins of the PAR and Crumbs complexes are pivotal to epithelial polarization, but the mechanistic understanding of polarization is challenging to reach, largely because numerous potential interactions between these proteins and others have been found, without clear hierarchy in importance. We identify the regionalized and segregated organization of members of the PAR and Crumbs complexes at epithelial apical junctions by imaging endogenous proteins using STED microscopy on Caco-2 cells, human and murine intestinal samples. Proteins organize in submicrometric clusters, with PAR3 overlapping with the tight junction (TJ) while PALS1-PATJ and aPKC-PAR6β form segregated clusters that are apical of the TJ and present in an alternated pattern related to actin organization. CRB3A is also apical of the TJ and weakly overlaps with other polarity proteins. This organization at the nanoscale level significantly simplifies our view on how polarity proteins could cooperate to drive and maintain cell polarity.


2012 ◽  
Vol 125 (18) ◽  
pp. 4405-4412 ◽  
Author(s):  
A. Rossi ◽  
T. J. Moritz ◽  
J. Ratelade ◽  
A. S. Verkman

2018 ◽  
Vol 115 (27) ◽  
pp. 7033-7038 ◽  
Author(s):  
Qiuyan Yan ◽  
Yanting Lu ◽  
Lulu Zhou ◽  
Junling Chen ◽  
Haijiao Xu ◽  
...  

The glucose transporter GLUT1, a plasma membrane protein that mediates glucose homeostasis in mammalian cells, is responsible for constitutive uptake of glucose into many tissues and organs. Many studies have focused on its vital physiological functions and close relationship with diseases. However, the molecular mechanisms of its activation and transport are not clear, and its detailed distribution pattern on cell membranes also remains unknown. To address these, we first investigated the distribution and assembly of GLUT1 at a nanometer resolution by super-resolution imaging. On HeLa cell membranes, the transporter formed clusters with an average diameter of ∼250 nm, the majority of which were regulated by lipid rafts, as well as being restricted in size by both the cytoskeleton and glycosylation. More importantly, we found that the activation of GLUT1 by azide or MβCD did not increase its membrane expression but induced the decrease of the large clusters. The results suggested that sporadic distribution of GLUT1 may facilitate the transport of glucose, implying a potential association between the distribution and activation. Collectively, our work characterized the clustering distribution of GLUT1 and linked its spatial structural organization to the functions, which would provide insights into the activation mechanism of the transporter.


2009 ◽  
Vol 96 (3) ◽  
pp. 450a
Author(s):  
Travis Gould ◽  
Manasa V. Gudheti ◽  
Mudalige S. Gunewardene ◽  
Samuel T. Hess

2007 ◽  
Vol 177 (4S) ◽  
pp. 223-223
Author(s):  
Sreenivasa R. Chinni ◽  
Hamilto Yamamoto ◽  
Zhong Dong ◽  
Aaron Sabbota ◽  
Sanaa Nabha ◽  
...  

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