The pH of Plant Cells The pH of Animal Cells

Author(s):  
James Small ◽  
Floyd J. Wiercinski
Keyword(s):  
Author(s):  
Laura Jerpseth ◽  
Ketan Thakare ◽  
Zhijian Pei ◽  
Hongmin Qin

Abstract In bioprinting, biomaterials are deposited layer-by-layer to fabricate structures. Bioprinting has many potential applications in drug screening, tissue engineering, and regenerative medicine. Both animal cells and plant cells can be used to synthesize bioinks. Green bioprinting uses bioinks that have been synthesized using plant cells. Constructs fabricated via green bioprinting contain immobilized plant cells, with these cells arranged at desired locations. The constructs provide scaffolds for cell growth. Printing parameters affecting the growth of cells in green bioprinted constructs include print speed, needle diameter, extrusion temperature, and extrusion pressure. This paper reports a study to examine effects of extrusion pressure on cell growth (measured by cell count) in bioprinted constructs, using bioink containing Chlamydomonas reinhardtii algae cells. Three levels of extrusion pressure were used: 3, 5, and 7 bar. Cell counts in the bioprinted constructs were measured on the third and sixth days after bioprinting. It was found that, as extrusion pressure increased, cell count decreased on both the third and sixth days after bioprinting. Furthermore, the difference in cell counts between the third and the sixth days decreased as extrusion pressure increased. These trends suggest that increasing extrusion pressure during green bioprinting negatively affects cell growth. A possible reason for these trends is physical damage to or death of cells in the bioprinted constructs when extrusion pressure became higher.


MRS Bulletin ◽  
1999 ◽  
Vol 24 (10) ◽  
pp. 27-31 ◽  
Author(s):  
David Boal

Despite a variety of shapes and sizes, the generic mechanical structure of cells is remarkably similar from one cell type to the next. All cells are bounded by a plasma membrane, a fluid sheet that controls the passage of materials into and out of the cell. Plant cells and bacteria reinforce this membrane with a cell wall, permitting the cell to operate at an elevated osmotic pressure. Simple cells, such as the bacterium shown in Figure 1a, possess a fairly homogeneous interior containing the cell's genetic blueprint and protein workhorses, but no mechanical elements. In contrast, as can be seen in Figure 1b, plant and animal cells contain internal compartments and a filamentous cytoskeleton—a network of biological ropes, cables, and poles that helps maintain the cell's shape and organize its contents.Four principal types of filaments are found in the cytoskeleton: spectrin, actin, microtubules, and a family of intermediate filaments. Not all filaments are present in all cells. The chemical composition of the filaments shows only limited variation from one cell to another, even in organisms as diverse as humans and yeasts. Membranes have a more variable composition, consisting of a bi-layer of dual-chain lipid molecules in which are embedded various proteins and frequently a moderate concentration of cholesterol. The similarity of the cell's mechanical elements in chemical composition and physical characteristics encourages us to search for universal strategies that have developed in nature for the engineering specifications of the cell. In this article, we concentrate on the cytoskeleton and its filaments.


1988 ◽  
Vol 106 (3) ◽  
pp. 715-721 ◽  
Author(s):  
O Baron-Epel ◽  
D Hernandez ◽  
L W Jiang ◽  
S Meiners ◽  
M Schindler

Fluorescence photobleaching was employed to examine the intercellular movement of fluorescein and carboxyfluorescein between contiguous soybean root cells (SB-1 cell line) growing in tissue culture. Results of these experiments demonstrated movement of these fluorescent probes between cytoplasmic (symplastic) compartments. This symplastic transport was inhibited with Ca2+ in the presence of ionophore A23187, and also with the tumor promoter 12-O-tetradecanoyl-phorbol-13-acetate (TPA). Both of these agents have previously been demonstrated to inhibit gap junction-mediated cell-cell communication in animal cells. In a companion experiment, a fluorescent phospholipid analogue, N-4-nitrobenzo-2-oxa-1,3-diazole phosphatidylcholine (NBD-PC), was incorporated into soybean cell membranes to examine whether dynamic membrane continuity existed between contacting cells, a transport route not existing between animal cells. Photobleaching single soybean cells growing in a filamentous strand demonstrated that phospholipid did exchange between contiguous cells.


Author(s):  
Mehdi Doumane ◽  
Léia Colin ◽  
Alexis Lebecq ◽  
Aurélie Fangain ◽  
Joseph Bareille ◽  
...  

ABSTRACTPhosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] is a low abundant lipid present at the plasma membrane of eukaryotic cells. Extensive studies in animal cells revealed the pleiotropic functions of PI(4,5)P2. In plant cells, PI(4,5)P2 is involved in various cellular processes including the regulation of cell polarity and tip growth, clathrin-mediated endocytosis, polar auxin transport, actin dynamics or membrane-contact sites. To date, most studies investigating the role of PI(4,5)P2 in plants have relied on mutants lacking enzymes responsible for PI(4,5)P2 synthesis and degradation. However, such genetic perturbations only allow steady-state analysis of plants undergoing their life cycle in PI(4,5)P2 deficient conditions and the corresponding mutants are likely to induce a range of non-causal (untargeted) effects driven by compensatory mechanisms. In addition, there are no small molecule inhibitors that are available in plants to specifically block the production of this lipid. Thus, there is currently no system to fine tune PI(4,5)P2 content in plant cells. Here we report a genetically encoded and inducible synthetic system, iDePP (Inducible Depletion of PI(4,5)P2 in Plants), that efficiently removes PI(4,5)P2 from the plasma membrane in different organs of Arabidopsis thaliana, including root meristem, root hair and shoot apical meristem. We show that iDePP allows the inducible depletion of PI(4,5)P2 in less than three hours. Using this strategy, we reveal that PI(4,5)P2 is critical for cortical microtubule organization. Together, we propose that iDePP is a simple and efficient genetic tool to test the importance of PI(4,5)P2 in given cellular or developmental responses but also to evaluate the importance of this lipid in protein localization.Research OrganismA. thaliana


1979 ◽  
Vol 39 (1) ◽  
pp. 235-245
Author(s):  
A.R. Gould

Two methods, which relate grain number to cell cycle phase in Feulgen-stained autoradiographic preparations, have been developed and compared. Both methods automate grain number estimations, one by taking integrated absorbance measurements at different wavelengths, the other by measuring absorption at a single wavelength before and after chemical removal of silver grains. With tritium-labelled tobacco mosaic virus as a probe, a quantitative analysis has been made of the binding of virus particles to plant protoplasts in different compartments of the DNA replication and partition cycle. The preliminary results indicate that the quantity of virus bound by protoplasts is related to their cell cycle phase. Whilst in this case, the methods have been used with plant cells, both techniques are equally applicable to animal cells.


2020 ◽  
Vol 117 (29) ◽  
pp. 17399-17408 ◽  
Author(s):  
Pauline Durand-Smet ◽  
Tamsin A. Spelman ◽  
Elliot M. Meyerowitz ◽  
Henrik Jönsson

The cytoskeleton plays a key role in establishing robust cell shape. In animals, it is well established that cell shape can also influence cytoskeletal organization. Cytoskeletal proteins are well conserved between animal and plant kingdoms; nevertheless, because plant cells exhibit major structural differences to animal cells, the question arises whether the plant cytoskeleton also responds to geometrical cues. Recent numerical simulations predicted that a geometry-based rule is sufficient to explain the microtubule (MT) organization observed in cells. Due to their high flexural rigidity and persistence length of the order of a few millimeters, MTs are rigid over cellular dimensions and are thus expected to align along their long axis if constrained in specific geometries. This hypothesis remains to be testedin cellulo. Here, we explore the relative contribution of geometry to the final organization of actin and MT cytoskeletons in single plant cells ofArabidopsis thaliana. We show that the cytoskeleton aligns with the long axis of the cells. We find that actin organization relies on MTs but not the opposite. We develop a model of self-organizing MTs in three dimensions, which predicts the importance of MT severing, which we confirm experimentally. This work is a first step toward assessing quantitatively how cellular geometry contributes to the control of cytoskeletal organization in living plant cells.


1992 ◽  
Vol 103 (2) ◽  
pp. 407-414 ◽  
Author(s):  
A.K. McNulty ◽  
M.J. Saunders

A major structural component of the inner face of the nuclear envelope in vertebrates and invertebrates is the nuclear lamina, an array of 1–3 extrinsic membrane proteins, lamins A, B and C. These proteins are highly homologous to intermediate filaments and are classified as type V. We report the first purification, antigenic characterization and immunocytochemical localization of putative plant lamin proteins from pea nuclei. We conclude that plant cells contain this ancestral class of intermediate filaments in their nuclei and that regulation of nuclear envelope assembly/disassembly and mitosis in plants may be similar to that in animal cells.


1993 ◽  
Vol 105 (4) ◽  
pp. 891-901 ◽  
Author(s):  
J. Chang-Jie ◽  
S. Sonobe

Microtubules in plant cells, as in animal cells, are dynamic structures. However, our lack of knowledge about the constituents of microtubules in plant cells has prevented us from understanding the mechanisms that control microtubule dynamics. To characterize some of these constituents, a cytoplasmic extract was prepared from evacuolated protoplasts (miniprotoplasts) of tobacco BY-2 cells, and microtubules were assembled in the presence of taxol and disassembled by cold treatment in the presence of Ca2+ and a high concentration of NaCl. SDS-PAGE analysis of triple-cycled microtubule protein revealed the presence of 120 kDa, 110 kDa and a group of 60–65 kDa polypeptides in addition to tubulin. Since these polypeptides had copolymerized with tubulin, through the three cycles of assembly and disassembly, and they bundle microtubules, we tentatively identified the three polypeptides as microtubule-associated proteins (MAPs). To characterize these factors further, triple-cycled microtubule protein was fractionated by Mono-Q anion-exchange chromatography and the microtubule-bundling activity of each fraction was examined. Fractions having microtubule-bundling activity contained only the 65 kDa MAP, an indication that the 65 kDa MAP is responsible for the bundling of microtubules. Purified 65 kDa MAP formed cross-bridge structures between adjacent microtubules in vitro. Polyclonal antibodies were raised in mice against the 65 kDa MAP. Immunofluorescence microscopy revealed that the 65 kDa MAP colocalized with microtubules in BY-2 cells throughout the cell cycle. Western blotting analysis of extracts from several species of plants suggested that the 65 kDa MAP and/or related peptides are widely distributed in the plant kingdom.


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