scholarly journals Neutrophil recruitment and intracellular vesicle transport: A short overview

2020 ◽  
Vol 50 (6) ◽  
Author(s):  
Sergi Masgrau‐Alsina ◽  
Markus Sperandio ◽  
Ina Rohwedder
Keyword(s):  
Vesicle Transport ◽  
Neutrophil Recruitment ◽  
Short Overview ◽  
Intracellular Vesicle ◽  
Intracellular Vesicle Transport

Distinct intracellular vesicle transport mechanisms are selectively modified by spastin and spastin mutations

2010 ◽  
Vol 226 (2) ◽  
pp. 362-368 ◽  
Author(s):  
Julia C. Fuerst ◽  
Andreas W. Henkel ◽  
Armin Stroebel ◽  
Oliver Welzel ◽  
Teja W. Groemer ◽  
...  
Keyword(s):  
Vesicle Transport ◽  
Transport Mechanisms ◽  
Intracellular Vesicle ◽  
Intracellular Vesicle Transport

scholarly journals A novel HSP90 chaperone complex regulates intracellular vesicle transport

2008 ◽  
Vol 121 (5) ◽  
pp. 717-723 ◽  
Author(s):  
G. P. Lotz ◽  
A. Brychzy ◽  
S. Heinz ◽  
W. M. J. Obermann
Keyword(s):  
Vesicle Transport ◽  
Intracellular Vesicle ◽  
Hsp90 Chaperone ◽  
Chaperone Complex ◽  
Intracellular Vesicle Transport

Actin sequestering protein, profilin, regulates intracellular vesicle transport in Leishmania

2020 ◽  
Vol 238 ◽  
pp. 111280 ◽  
Author(s):  
Bindu Ambaru ◽  
Anupriya Gopalsamy ◽  
T.V.Satish Tammana ◽  
Hosahalli S. Subramanya ◽  
Chhitar M. Gupta
Keyword(s):  
Vesicle Transport ◽  
Intracellular Vesicle ◽  
Intracellular Vesicle Transport

VISUALIZING THE UPTAKE AND INTRACELLULAR VESICLE TRANSPORT OF CARBON NANOTUBES TOWARD THE PERINUCLEAR REGION INSIDE CELLS

NANO ◽  
2014 ◽  
Vol 09 (01) ◽  
pp. 1450001 ◽  
Author(s):  
JUN LI ◽  
BIN KANG ◽  
SHUQUAN CHANG ◽  
YAODONG DAI
Keyword(s):  
Carbon Nanotubes ◽  
Living Cells ◽  
Vesicle Transport ◽  
Endocytic Pathway ◽  
Perinuclear Region ◽  
Microtubule Organizing Center ◽  
Ph Change ◽  
Intracellular Vesicle ◽  
Early Endosomes ◽  
Intracellular Vesicle Transport

We directly visualized the uptake and intracellular vesicle transport of shortened single walled carbon nanotubes in living cells through a dual-labeling system. With a stable labeling of fluorescein isothiocyanate and a pH-sensitive stacking of doxorubicin on carbon nanotubes, the location of internalized nanotubes inside the cell and the microenvironment especially the pH change of the nanotube-embedded vesicles could be monitored at the same time. Results showed that after internalization through endocytic pathway, carbon nanotubes tended to transport from the early endosomes to later acidic lysosomes and these vesicles moved along the microtubule track toward a perinuclear region where is a microtubule-organizing center. These results might provide a novel understanding for the intracellular interaction of carbon nanotubes and living cells.

scholarly journals Molecular cloning of the mouse homologue of Rab3c

2001 ◽  
Vol 27 (1) ◽  
pp. 117-122 ◽  
Author(s):  
NJ Pavlos ◽  
J Xu ◽  
JM Papadimitriou ◽  
MH Zheng
Keyword(s):  
Skeletal Development ◽  
In Situ Hybridisation ◽  
Matrix Vesicles ◽  
Matrix Vesicle ◽  
Predicted Amino Acid Sequence ◽  
Multiple Sequence ◽  
Intracellular Vesicle ◽  
Intracellular Vesicle Transport ◽  
The Brain

Small GTP-binding proteins of the Rab subfamily are key regulators of intracellular vesicle transport. Here we report the isolation of a cDNA clone encoding the complete Rab3c isoform from mouse embryo using a degenerative PCR-based approach. Multiple sequence alignment revealed that the predicted amino acid sequence was identical to the previously identified rat Rab3c isoform and 98% identical to the published bovine Rab3c GTPase from brain. Furthermore by in situ hybridisation, Rab3c mRNA was detectable within various regions of the brain, cartilage and highly enriched within intestinal villi of foetal tissues. Chondrocytes in the hypertrophic zone, but not reserve or proliferative zones, expressed high levels of Rab3c. This pattern of expression corresponds with the genesis of matrix vesicles during endochondral ossification.In all, our results suggest that in addition to its functional role during regulated secretion in brain, Rab3c may play a part in matrix vesicle trafficking during skeletal development.

scholarly journals Fusion of sequentially internalized vesicles in alveolar macrophages.

1990 ◽  
Vol 110 (4) ◽  
pp. 1013-1022 ◽  
Author(s):  
D M Ward ◽  
D P Hackenyos ◽  
J Kaplan
Keyword(s):  
Endocytic Pathway ◽  
Receptor Complexes ◽  
Intracellular Vesicle ◽  
Late Endosomes ◽  
Early Endosomes ◽  
Changing Patterns ◽  
Intracellular Vesicle Transport ◽  
Shift Technique ◽  
Ligand Addition ◽  
Density Shift

Previously we reported that internalized ligand-receptor complexes are transported within the alveolar macrophage at a rate that is independent of the ligand and/or receptor but is dependent on the endocytic apparatus (Ward, D. M., R. S. Ajioka, and J. Kaplan. 1989. J. Biol. Chem. 264:8164-8170). To probe the mechanism of intracellular vesicle transport, we examined the ability of vesicles internalized at different times to fuse. The mixing of ligands internalized at different times was studied using the 3,3'-diaminobenzidine/horseradish peroxidase density shift technique. The ability of internalized vesicles to fuse was dependent upon their location in the endocytic pathway. When ligands were administered as tandem pulses a significant amount of mixing (20-40%) of vesicular contents was observed. The pattern of mixing was independent of the ligands employed (transferrin, mannosylated BSA, or alpha macroglobulin), the order of ligand addition, and temperature (37 degrees C or 28 degrees C). Fusion was restricted to a brief period immediately after internalization. The amount of fusion in early endosomes did not increase when cells, given tandem pulses, were chased such that the ligands further traversed the early endocytic pathway. Little fusion, also, was seen when a chase was interposed between the two ligand pulses. The temporal segregation of vesicle contents seen in early endosomes was lost within late endosomes. Extensive mixing of vesicle contents was observed in the later portion of the endocytic pathway. This portion of the pathway is defined by the absence of internalized transferrin and is composed of ligands en route to lysosomes. Incubation of cells in iso-osmotic medium in which Na+ was replaced by K+ inhibited movement of internalized ligands to the lysosome, resulting in ligand accumulation within the late endocytic pathway. The accumulation of ligand was correlated with extensive mixing of sequentially internalized ligands. Although significant amounts of ligand degradation were observed, this compartment was devoid of conventional lysosomal markers such as acid glycosidases. These results indicate changing patterns of vesicle fusion within the endocytic pathway, with a complete loss of temporal ligand segregation in a prelysosomal compartment.

scholarly journals The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network

2001 ◽  
Vol 155 (7) ◽  
pp. 1239-1250 ◽  
Author(s):  
Pak Phi Poon ◽  
Steven F. Nothwehr ◽  
Richard A. Singer ◽  
Gerald C. Johnston
Keyword(s):  
Gtp Hydrolysis ◽  
Transport Pathways ◽  
Intracellular Vesicle ◽  
Immunofluorescence Studies ◽  
Endosomal Transport ◽  
Essential Function ◽  
Golgi Network ◽  
Intracellular Vesicle Transport ◽  
Mutant Cells ◽  
Adp Ribosylation Factor

Many intracellular vesicle transport pathways involve GTP hydrolysis by the ADP-ribosylation factor (ARF) type of monomeric G proteins, under the control of ArfGAP proteins. Here we show that the structurally related yeast proteins Gcs1 and Age2 form an essential ArfGAP pair that provides overlapping function for TGN transport. Mutant cells lacking the Age2 and Gcs1 proteins cease proliferation, accumulate membranous structures resembling Berkeley bodies, and are unable to properly process and localize the vacuolar hydrolase carboxypeptidase (CPY) and the vacuolar membrane protein alkaline phosphatase (ALP), which are transported from the TGN to the vacuole by distinct transport routes. Immunofluorescence studies localizing the proteins ALP, Kex2 (a TGN resident protein), and Vps10 (the CPY receptor for transport from the TGN to the vacuole) suggest that inadequate function of this ArfGAP pair leads to a fragmentation of TGN, with effects on secretion and endosomal transport. Our results demonstrate that the Gcs1 + Age2 ArfGAP pair provides overlapping function for transport from the TGN, and also indicate that multiple activities at the TGN can be maintained with the aid of a single ArfGAP.

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