Gap junction mediated miRNA intercellular transfer and gene regulation: A novel mechanism for intercellular genetic communication

Liang Zong; Yan Zhu; Ruqiang Liang; Hong-Bo Zhao

doi:10.1038/srep19884

Gap junction mediated miRNA intercellular transfer and gene regulation: A novel mechanism for intercellular genetic communication

Scientific Reports ◽

10.1038/srep19884 ◽

2016 ◽

Vol 6 (1) ◽

Cited By ~ 56

Author(s):

Liang Zong ◽

Yan Zhu ◽

Ruqiang Liang ◽

Hong-Bo Zhao

Keyword(s):

Gene Regulation ◽

Gap Junction ◽

Intercellular Transfer ◽

Genetic Communication

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MicroRNA Intercellular Transfer and Bioelectrical Regulation of Model Multicellular Ensembles by the Gap Junction Connectivity

The Journal of Physical Chemistry B ◽

10.1021/acs.jpcb.7b04774 ◽

2017 ◽

Vol 121 (32) ◽

pp. 7602-7613 ◽

Cited By ~ 8

Author(s):

Javier Cervera ◽

Salvador Meseguer ◽

Salvador Mafe

Keyword(s):

Gap Junction ◽

Intercellular Transfer

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Connexin26 gap junction mediates miRNA intercellular genetic communication in the cochlea and is required for inner ear development

Scientific Reports ◽

10.1038/srep15647 ◽

2015 ◽

Vol 5 (1) ◽

Cited By ~ 20

Author(s):

Yan Zhu ◽

Liang Zong ◽

Ling Mei ◽

Hong-Bo Zhao

Keyword(s):

Gap Junction ◽

Inner Ear ◽

Ear Development ◽

Inner Ear Development ◽

Genetic Communication

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Transfected connexin45 alters gap junction permeability in cells expressing endogenous connexin43.

The Journal of Cell Biology ◽

10.1083/jcb.130.4.987 ◽

1995 ◽

Vol 130 (4) ◽

pp. 987-995 ◽

Cited By ~ 123

Author(s):

M Koval ◽

S T Geist ◽

E M Westphale ◽

A E Kemendy ◽

R Civitelli ◽

...

Keyword(s):

Gap Junction ◽

Lucifer Yellow ◽

Direct Interaction ◽

Full Length ◽

Osteosarcoma Cell ◽

Dye Transfer ◽

Fluorescent Reporter ◽

Intercellular Transfer ◽

Carboxyl Terminal ◽

Gap Junctional

Many cells express multiple connexins, the gap junction proteins that interconnect the cytosol of adjacent cells. Connexin43 (Cx43) channels allow intercellular transfer of Lucifer Yellow (LY, MW = 443 D), while connexin45 (Cx45) channels do not. We transfected full-length or truncated chicken Cx45 into a rat osteosarcoma cell line ROS-17/2.8, which expresses endogenous Cx43. Both forms of Cx45 were expressed at high levels and colocalized with Cx43 at plasma membrane junctions. Cells transfected with full-length Cx45 (ROS/Cx45) and cells transfected with Cx45 missing the 37 carboxyl-terminal amino acids (ROS/Cx45tr) showed 30-60% of the gap junctional conductance exhibited by ROS cells. Intercellular transfer of three negatively charged fluorescent reporter molecules was examined. In ROS cells, microinjected LY was transferred to an average of 11.2 cells/injected cell, while dye transfer between ROS/Cx45 cells was reduced to 3.9 transfer between ROS/Cx45 cells was reduced to 3.9 cells. In contrast, ROS/Cx45tr cells transferred LY to > 20 cells. Transfer of calcein (MW = 623 D) was also reduced by approximately 50% in ROS/Cx45 cells, but passage of hydroxycoumarin carboxylic acid (HCCA; MW = 206 D) was only reduced by 35% as compared to ROS cells. Thus, introduction of Cx45 altered intercellular coupling between cells expressing Cx43, most likely the result of direct interaction between Cx43 and Cx45. Transfection of Cx45tr and Cx45 had different effects in ROS cells, consistent with a role of the carboxyl-terminal domain of Cx45 in determining gap junction permeability or interactions between connexins. These data suggest that coexpression of multiple connexins may enable cells to achieve forms of intercellular communication that cannot be attained by expression of a single connexin.

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The Nature of the Intramembrane Particle

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s1431927600003020 ◽

1980 ◽

Vol 38 ◽

pp. 688-691

Author(s):

A.J. Verkleij

Keyword(s):

Escherichia Coli ◽

Tight Junction ◽

Gap Junction ◽

The Other ◽

Fracture Face ◽

Band 3 Protein ◽

Satisfactory Explanation ◽

Freeze Fracturing ◽

Intramembrane Particle ◽

Luminal Membrane

Freeze-fracturing splits membranes into two helves, thus allowing an examination of the membrane interior. The 5-10 rm particles visible on both monolayers are widely assumed to be proteinaceous in nature. Most membranes do not reveal impressions complementary to particles on the opposite fracture face, if the membranes are fractured under conditions without etching. Even if it is considered that shadowing, contamination or fracturing itself might obscure complementary pits', there is no satisfactory explanation why under similar physical circimstances matching halves of other membranes can be visualized. A prominent example of uncomplementarity is found in the erythrocyte manbrane. It is wall established that band 3 protein and possibly glycophorin represents these nonccmplanentary particles. On the other hand a number of membrane types show pits opposite the particles. Scme well known examples are the ";gap junction',"; tight junction, the luminal membrane of the bladder epithelial cells and the outer membrane of Escherichia coli.

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