scholarly journals AP-2α is required after lens vesicle formation to maintain lens integrity

2014 ◽  
Vol 243 (10) ◽  
pp. 1298-1309 ◽  
Author(s):  
Christine L. Kerr ◽  
Mizna A. Zaveri ◽  
Michael L. Robinson ◽  
Trevor Williams ◽  
Judith A. West-Mays
Keyword(s):  
Vesicle Formation ◽  
Lens Vesicle

A STUDY OF THE INHIBITORY EFFECTS OF CHICK WHOLE EYE EXTRACT ON THE DEVELOPMENT OF THE LENS OF THE CHICK EMBRYO IN VITRO

1966 ◽  
Vol 44 (4) ◽  
pp. 661-676 ◽  
Author(s):  
Robert P. Thompson
Keyword(s):  
Chick Embryo ◽  
Nutrient Medium ◽  
Inhibitory Effect ◽  
Reactive System ◽  
Vesicle Formation ◽  
Inhibitory Effects ◽  
Muscle Extract ◽  
Lens Vesicle ◽  
And Control

To demonstrate the phenomenon of homologous inhibition by clearly interpretable results in a readily reactive system, experiments were carried out to study the effect of chick whole eye extract on the development of the vesicular lens of the chick embryo in vitro. The heads of embryos of 11 through 13 somites were explanted onto nutrient medium diluted with varying amounts of the extract, and cultured for 30 hours. A total of 35 embryos exposed to concentrations of 1:1, 1:2, and 1:4 (extract to medium) showed complete inhibition of lens vesicle formation. Of a total of 53 embryos on concentrations of 1:8, 1:16, 1:32, and 1:64, more than 50% showed inhibition of vesicle formation. The inhibitory effect disappeared at a concentration of 1:128. Control material exposed to some equivalent concentrations of nutrient medium – saline mixtures showed inhibition of vesicle formation in only 15% of 33 embryos. Of a total of 27 control embryos exposed to ventricular muscle extract, approximately one-third showed inhibition of vesicle formation at concentrations of 1:8 and 1:16, with the inhibitory effect disappearing at 1:32. The implications of this result are discussed. Other factors and control experiments are described and their value is assessed.

Appearance of Antigens during Development of the Lens

Development ◽  
1959 ◽  
Vol 7 (2) ◽  
pp. 264-274
Author(s):  
Jan Langman
Keyword(s):  
Cellular Level ◽  
Cylindrical Shape ◽  
Vesicle Formation ◽  
Retinal Surface ◽  
Clear Cut ◽  
Somite Stage ◽  
Apical Cytoplasm ◽  
Lens Vesicle ◽  
Lens Placode ◽  
Placode Formation

Those cells of the head ectoderm of chick embryos which are to give rise to the lens show the first signs of differentiation at the 13–16-somite Stage: the nuclei become cylindrical and move gradually toward the base of the cells, while the vacuoles present in the cytoplasm decrease in size and number. During the 16–20-somite stage the changes become clear-cut as the cells transform from a cuboidal to a high cylindrical shape and the nuclei elongate and move perpendicularly to the retinal surface (placode formation; Plate 1, fig. 1b; McKeehan, 1951; Van Doorenmaalen, 1958; Langman et al., 1957). During the 20–30-somite stage the lens placode invaginates and gradually forms a lens vesicle which remains attached to the ectoderm until the 30–31-somite stage, but separates from it at the 32–33-somite stage (lens vesicle formation; Plate 1, figs. 1c, 2b, 2c). At the cellular level it was noted that acidophilic fibres appear in the apical cytoplasm at the 23–24-somite stage.

Intracellular trafficking and cytoplasmic streaming under abiotic stress conditions

2019 ◽  
Vol 6 (04) ◽  
Author(s):  
JESHIMA KHAN YASIN ◽  
ANIL KUMAR SINGH
Keyword(s):  
Plasma Membrane ◽  
Abiotic Stress ◽  
Confocal Microscopy ◽  
Fusion Protein ◽  
Intracellular Trafficking ◽  
Cytoplasmic Streaming ◽  
Living Cells ◽  
Stress Conditions ◽  
Vesicle Formation ◽  
External Stimuli

Cytoplasmic streaming is one among the vital activities of the living cells. In plants cytolplasmic streaming could clearly be seen in hypocotyls of growing seedlings. To observe cytoplsmic streaming and its correlated intracellular trafficking an investigation was conducted in legumes in comparison with GFP-AtRab75 and 35S::GFP:δTIP tonoplast fusion protein expressing arabidopsis lines. These seedlings were observed under confocal microscopy with different buffer incubation treatments and under different stress conditions. GFP expressing 35S::GFP:δTIP tonoplast lines were looking similar to the control lines and differ under stress conditions. Movement of cytoplasmic invaginations within the tonoplast and cytoplasmic sub vesicle or bulb budding during cytoplasmic streaming was observed in hypocotyls of At-GFP tonoplast plants. We found the cytoplasmic bulbs/ vesicles or sub vesicle formation from the plasma membrane. The streaming speed also depends on the incubation medium in which the specimen was incubated, indicating that the external stimuli as well as internal stimuli can alter the speed of streaming

scholarly journals In Vitro Incorporation of GPI-Anchored Proteins Into Human Erythrocytes and Their Fate in the Membrane

Blood ◽  
1998 ◽  
Vol 91 (5) ◽  
pp. 1784-1792 ◽  
Author(s):  
Gianluca Civenni ◽  
Samuel T. Test ◽  
Urs Brodbeck ◽  
Peter Bütikofer
Keyword(s):  
Membrane Vesicle ◽  
Human Erythrocytes ◽  
Membrane Extraction ◽  
Membrane Microdomains ◽  
Membrane Insertion ◽  
Vesicle Formation ◽  
Calcium Loading ◽  
Lipid Moiety ◽  
Triton X

Abstract In many different cells, glycosylphosphatidylinositol (GPI)-anchored molecules are clustered in membrane microdomains that resist extraction by detergents at 4°C. In this report, we identified the presence of such domains in human erythrocytes and examined the ability of exogenously-added GPI-anchored molecules to colocalize with the endogenous GPI-anchored proteins in these detergent-insoluble complexes. We found that the addition to human erythrocytes of three purified GPI-anchored proteins having different GPI lipid moieties resulted in their efficient and correct incorporation into the membrane. The extent of membrane insertion was dependent on the intactness of the GPI lipid moiety. However, unlike the endogenous GPI-anchored proteins, the in vitro incorporated GPI molecules were not resistant to membrane extraction by Triton X-100 at 4°C. In addition, in contrast to the endogenous GPI-anchored proteins, they were not preferentially released from erythrocytes during vesiculation induced by calcium loading of the cells. These results suggest that in vitro incorporated GPI-linked molecules are excluded from pre-existing GPI-enriched membrane areas in human erythrocytes and that these microdomains may represent the sites of membrane vesicle formation.

scholarly journals Mutational analysis of caveolin-induced vesicle formation

FEBS Letters ◽  
1998 ◽  
Vol 434 (1-2) ◽  
pp. 127-134 ◽  
Author(s):  
Shengwen Li ◽  
Ferruccio Galbiati ◽  
Daniela Volonte' ◽  
Massimo Sargiacomo ◽  
Jeffrey A Engelman ◽  
...  
Keyword(s):  
Mutational Analysis ◽  
Vesicle Formation

Vesicle formation in the Golgi apparatus

1989 ◽  
Vol 141 (4) ◽  
pp. 463-504 ◽  
Author(s):  
George F. Oster ◽  
Louis Y. Cheng ◽  
Hsiao-Ping H. Moore ◽  
Alan S. Perelson
Keyword(s):  
Golgi Apparatus ◽  
Vesicle Formation

IL-25 Hermansky-Pudlak syndrome: a model for abnormal vesicle formation and trafficking

2003 ◽  
Vol 16 (5) ◽  
pp. 584-584 ◽  
Author(s):  
M. Huizing ◽  
A. Helip-Wooley ◽  
H. Dorward ◽  
D. Claassen ◽  
R. Hess ◽  
...  
Keyword(s):  
Vesicle Formation ◽  
Hermansky Pudlak Syndrome

scholarly journals GTPase cross talk regulates TRAPPII activation of Rab11 homologues during vesicle biogenesis

2016 ◽  
Vol 215 (4) ◽  
pp. 499-513 ◽  
Author(s):  
Laura L. Thomas ◽  
J. Christopher Fromme
Keyword(s):  
Cross Talk ◽  
Vesicle Formation ◽  
Nucleotide Exchange ◽  
Endocytic Recycling ◽  
Direct Role ◽  
Definitive Evidence ◽  
Nucleotide Exchange Factor ◽  
Vesicle Biogenesis ◽  
Simultaneous Activation ◽  
Bona Fide

Rab guanosine triphosphatases (GTPases) control cellular trafficking pathways by regulating vesicle formation, transport, and tethering. Rab11 and its paralogs regulate multiple secretory and endocytic recycling pathways, yet the guanine nucleotide exchange factor (GEF) that activates Rab11 in most eukaryotic cells is unresolved. The large multisubunit transport protein particle (TRAPP) II complex has been proposed to act as a GEF for Rab11 based on genetic evidence, but conflicting biochemical experiments have created uncertainty regarding Rab11 activation. Using physiological Rab-GEF reconstitution reactions, we now provide definitive evidence that TRAPPII is a bona fide GEF for the yeast Rab11 homologues Ypt31/32. We also uncover a direct role for Arf1, a distinct GTPase, in recruiting TRAPPII to anionic membranes. Given the known role of Ypt31/32 in stimulating activation of Arf1, a bidirectional cross talk mechanism appears to drive biogenesis of secretory and endocytic recycling vesicles. By coordinating simultaneous activation of two essential GTPase pathways, this mechanism ensures recruitment of the complete set of effectors needed for vesicle formation, transport, and tethering.

Vesicle formation by double long-chain amidines

1986 ◽  
pp. 1060 ◽  
Author(s):  
Fabienne Defrise-Quertain ◽  
Philippe Duquenoy ◽  
Robert Brasseur ◽  
Philippe Brak ◽  
Bernard Caillaux ◽  
...  
Keyword(s):  
Vesicle Formation ◽  
Long Chain
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