scholarly journals Phosphate Transport across the Plasma Membrane of Wheat Leaf Protoplasts

1985 ◽  
Vol 77 (4) ◽  
pp. 1013-1015 ◽  
Author(s):  
Alan H. Goldstein ◽  
Andre D. Hunziker
Keyword(s):  
Plasma Membrane ◽  
Phosphate Transport ◽  
Wheat Leaf ◽  
Leaf Protoplasts

scholarly journals Exoamylase Activity in Vacuoles Isolated from Pea and Wheat Leaf Protoplasts

1986 ◽  
Vol 82 (4) ◽  
pp. 1119-1121 ◽  
Author(s):  
Paul Ziegler ◽  
Erwin Beck
Keyword(s):  
Wheat Leaf ◽  
Leaf Protoplasts

Identification of chitosan oligosaccharides binding proteins from the plasma membrane of wheat leaf cell

2018 ◽  
Vol 111 ◽  
pp. 1083-1090 ◽  
Author(s):  
Dongdong Liu ◽  
Siming Jiao ◽  
Gong Cheng ◽  
Xueming Li ◽  
Zhichao Pei ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Proteins ◽  
Leaf Cell ◽  
Chitosan Oligosaccharides ◽  
Wheat Leaf

Organelles associated with the plasma membrane of tobacco leaf protoplasts

1983 ◽  
Vol 2 (6) ◽  
pp. 292-295 ◽  
Author(s):  
L. C. Fowke ◽  
P. J. Rennie ◽  
F. Constabel
Keyword(s):  
Plasma Membrane ◽  
Tobacco Leaf ◽  
Leaf Protoplasts

scholarly journals Control of phosphate transport across the plasma membrane of Chara corallina

1998 ◽  
Vol 49 (318) ◽  
pp. 13-19 ◽  
Author(s):  
T. Mimura ◽  
R. J. Reid ◽  
F. A. Smith
Keyword(s):  
Plasma Membrane ◽  
Phosphate Transport ◽  
Chara Corallina

Regulation of swelling of etiolated-wheat-leaf protoplasts by phytochrome and gibberellic acid

Planta ◽  
1983 ◽  
Vol 158 (5) ◽  
pp. 416-421 ◽  
Author(s):  
S. D. Blakeley ◽  
B. Thomas ◽  
J. L. Hall ◽  
D. Vince-Prue
Keyword(s):  
Gibberellic Acid ◽  
Wheat Leaf ◽  
Leaf Protoplasts

scholarly journals A single Na+-Pi cotransporter in Toxoplasma plays key roles in phosphate import and control of parasite osmoregulation

2020 ◽  
Vol 16 (12) ◽  
pp. e1009067
Author(s):  
Beejan Asady ◽  
Claudia F. Dick ◽  
Karen Ehrenman ◽  
Tejram Sahu ◽  
Julia D. Romano ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Critical Role ◽  
Inorganic Ions ◽  
Phosphate Transport ◽  
Cellular Functions ◽  
Growth Defects ◽  
Binding Domains ◽  
Cytoplasmic Vesicles ◽  
Survival Mode ◽  
And Control

Inorganic ions such as phosphate, are essential nutrients required for a broad spectrum of cellular functions and regulation. During infection, pathogens must obtain inorganic phosphate (Pi) from the host. Despite the essentiality of phosphate for all forms of life, how the intracellular parasite Toxoplasma gondii acquires Pi from the host cell is still unknown. In this study, we demonstrated that Toxoplasma actively internalizes exogenous Pi by exploiting a gradient of Na+ ions to drive Pi uptake across the plasma membrane. The Na+-dependent phosphate transport mechanism is electrogenic and functionally coupled to a cipargarmin sensitive Na+-H+-ATPase. Toxoplasma expresses one transmembrane Pi transporter harboring PHO4 binding domains that typify the PiT Family. This transporter named TgPiT, localizes to the plasma membrane, the inward buds of the endosomal organelles termed VAC, and many cytoplasmic vesicles. Upon Pi limitation in the medium, TgPiT is more abundant at the plasma membrane. We genetically ablated the PiT gene, and ΔTgPiT parasites are impaired in importing Pi and synthesizing polyphosphates. Interestingly, ΔTgPiT parasites accumulate 4-times more acidocalcisomes, storage organelles for phosphate molecules, as compared to parental parasites. In addition, these mutants have a reduced cell volume, enlarged VAC organelles, defects in calcium storage and a slightly alkaline pH. Overall, these mutants exhibit severe growth defects and have reduced acute virulence in mice. In survival mode, ΔTgPiT parasites upregulate several genes, including those encoding enzymes that cleave or transfer phosphate groups from phosphometabolites, transporters and ions exchangers localized to VAC or acidocalcisomes. Taken together, these findings point to a critical role of TgPiT for Pi supply for Toxoplasma and also for protection against osmotic stresses.

Oxidant-induced alterations in glucose and phosphate transport in LLC-PK1 cells: mechanisms of injury

1993 ◽  
Vol 265 (3) ◽  
pp. F377-F384 ◽  
Author(s):  
S. P. Andreoli ◽  
J. A. McAteer ◽  
S. A. Seifert ◽  
S. A. Kempson
Keyword(s):  
Hydrogen Peroxide ◽  
Plasma Membrane ◽  
Atpase Activity ◽  
Membrane Vesicles ◽  
Iron Chelator ◽  
Phosphate Transport ◽  
Atp Depletion ◽  
Oxidant Injury ◽  
Sodium Dependent ◽  
Permeable Iron

To determine the effects of oxidant injury on specialized functions of proximal tubular epithelial cells, we determined sodium-dependent uptake of glucose ([alpha-14C]methylglucoside) and phosphate (32Pi) in LLC-PK1 cells after exposure to 0-500 microM hydrogen peroxide. Oxidant stress resulted in significant (P < 0.01) inhibition of glucose and phosphate transport. Decreased transport of glucose and phosphate was associated with marked ATP depletion, decreased activity of the sodium pump as determined by 86Rb uptake, direct inhibition of Na(+)-K(+)-adenosinetriphosphatase (Na(+)-K(+)-ATPase) activity, and an increase in intracellular sodium content, whereas intracellular potassium content declined. Decreased glucose and phosphate transport, inhibition of 86Rb uptake and Na(+)-K(+)-ATPase activity, and altered intracellular ion content were prevented by catalase and partially prevented by the membrane-permeable iron chelator phenathroline, whereas the slowly membrane-permeable iron chelator deferoxamine had little or no effect. To determine whether oxidant injury could also inhibit transporter function at the membrane level, plasma membrane vesicles were isolated from LLC-PK1 cells exposed to 500 microM hydrogen peroxide. Such membrane vesicles exhibited decreased sodium-dependent glucose transport, whereas sodium-dependent phosphate transport was not altered. We conclude that oxidant injury results in ATP depletion and inactivation of Na(+)-K(+)-ATPase which leads to disruption of the normal ion gradients sufficient to interfere with glucose and phosphate transport. Glucose transport is also inhibited by disruption of transporter activity within the plasma membrane. These alterations are mediated in part by the intracellular generation of an iron-dependent radical.

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