An X-ray microanalysis survey of the concentration of elements in the cytoplasm of different mammalian cell types

1979 ◽  
Vol 101 (3) ◽  
pp. 493-501 ◽  
Author(s):  
Ivan L. Cameron ◽  
Thomas B. Pool ◽  
Nancy K. R. Smith
Keyword(s):  
Mammalian Cell ◽  
Cell Types ◽  
X Ray

scholarly journals In situ differentiation of iridophore crystallotypes underlies zebrafish stripe patterning

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Dvir Gur ◽  
Emily J. Bain ◽  
Kory R. Johnson ◽  
Andy J. Aman ◽  
H. Amalia Pasoili ◽  
...  
Keyword(s):  
Skin Color ◽  
Cell Types ◽  
Color Pattern ◽  
Single Type ◽  
Sequencing Analysis ◽  
X Ray Diffraction ◽  
X Ray ◽  
Cryogenic Scanning Electron Microscopy ◽  
Different Cell Types

AbstractSkin color patterns are ubiquitous in nature, impact social behavior, predator avoidance, and protection from ultraviolet irradiation. A leading model system for vertebrate skin patterning is the zebrafish; its alternating blue stripes and yellow interstripes depend on light-reflecting cells called iridophores. It was suggested that the zebrafish’s color pattern arises from a single type of iridophore migrating differentially to stripes and interstripes. However, here we find that iridophores do not migrate between stripes and interstripes but instead differentiate and proliferate in-place, based on their micro-environment. RNA-sequencing analysis further reveals that stripe and interstripe iridophores have different transcriptomic states, while cryogenic-scanning-electron-microscopy and micro-X-ray diffraction identify different crystal-arrays architectures, indicating that stripe and interstripe iridophores are different cell types. Based on these results, we present an alternative model of skin patterning in zebrafish in which distinct iridophore crystallotypes containing specialized, physiologically responsive, organelles arise in stripe and interstripe by in-situ differentiation.

Thin-section, freeze-fracture, and energy dispersive x-ray analysis studies of the protein bodies of tomato seeds

1980 ◽  
Vol 58 (6) ◽  
pp. 699-711 ◽  
Author(s):  
Ernest Spitzer ◽  
John N. A. Lott
Keyword(s):  
Freeze Fracture ◽  
Protein Body ◽  
Cell Types ◽  
Energy Dispersive ◽  
Protein Bodies ◽  
Elemental Content ◽  
Tomato Seed ◽  
Endosperm Tissue ◽  
X Ray ◽  
Edx Analysis

Protein bodies of dry seeds of tomato (Lycopersicon esculentum) from radicle, hypocotyl, cotyledon, and endosperm tissue were extensively studied using thin-sectioning, freeze-fracturing and energy dispersive x-ray (EDX) analysis. Protein bodies varied in size, were oval to circular in section, and generally consisted of a proteinaceous matrix, globoid crystal, and protein crystalloid components. Size, shape, and arrangements of globoid crystals and protein crystalloids varied even within the same cell. Globoid crystals were generally oval to circular in section. They were always surrounded by a proteinaceous matrix. In a given protein body the number present ranged from a few to numerous. A protein body generally contained only one protein crystalloid. In section, protein crystalloids were irregular or angular in shape. They were composed of substructural particles which formed lattice planes. EDX analysis of tomato seed globoid crystals revealed the presence of P, K, and Mg in all cases, a fact that is consistent with globoid crystals being phytin-rich. Rarely, small amounts of calcium were found along with P, K, and Mg in globoid crystals of each of the tissue regions considered. The distribution pattern of cells with Ca containing globoid crystals was random. Small amounts of Fe and Mn were also found in the globoid crystals of protein bodies from certain cell types. These two elements, unlike calcium, were specific in terms of their distribution. Globoid crystals from the protodermal cells often contained Mn and Fe. The globoid crystals from provascular tissue of radicle, hypocotyl, and cotyledon regions often contained Fe while globoid crystals in the first layer of large cells surrounding these provascular areas always contained Fe. Results from EDX analysis of the proteinaceous material from the protein bodies are presented and discussed as are variations in elemental content due to different fixations.

Protein bodies in Datura stramonium seeds: structure and mineral nutrient composition

1991 ◽  
Vol 69 (11) ◽  
pp. 2545-2554 ◽  
Author(s):  
Sara Maldonado ◽  
John N. A. Lott
Keyword(s):  
Distribution Patterns ◽  
Cell Types ◽  
Datura Stramonium ◽  
Energy Dispersive ◽  
Protein Bodies ◽  
Mineral Nutrient ◽  
Electron Microscopic ◽  
Element Analysis ◽  
X Ray ◽  
Endosperm Protein

The structure of protein bodies in the endosperm and embryo of Datura stramonium was studied with a variety of light-and electron-microscopic techniques. Protein bodies had one to several globoid crystals and one or two protein crystalloids in the proteinaceous matrix. Although the embryo protein bodies rarely had more than two globoid crystals, the endosperm protein bodies had varying sizes and numbers of globoid crystals, even within the same cell. Energy-dispersive X-ray analysis of globoid crystals revealed the presence of P, K, and Mg in all cases. Traces of Fe, Mn, and Zn were also found in globoid crystals of protein bodies from certain cell types. The distribution patterns of these three elements were quite specific; for example, Mn traces were found only in the globoid crystals of the protoderm. Neutron-activation analysis of endosperm and embryo tissues was used to quantitatively measure the concentration of Ca, Cl, Cu, I, K, Mg, Mn, Na, and S. The results from structural studies and the element analysis studies are discussed in the context of solanaceous seeds in particular but also with relation to seeds in general. Key words: protein bodies, Datura stramonium, seed, globoid crystals, energy-dispersive X-ray analysis, Solanaceae.

scholarly journals Electron probe x-ray microanalysis of small granulated cells in rat sympathetic ganglia after sequential aldehyde and dichromate treatment.

1977 ◽  
Vol 25 (4) ◽  
pp. 275-279 ◽  
Author(s):  
J D Lever ◽  
R M Santer ◽  
K S Lu ◽  
R Presley
Keyword(s):  
Adrenal Medulla ◽  
Electron Probe ◽  
Potassium Dichromate ◽  
Cell Types ◽  
Sympathetic Ganglia ◽  
Type Ii ◽  
Treatment Sequence ◽  
X Ray ◽  
Small Granulated Cells

Rat adrenal medulla and celiac-mesenteric sympathetic ganglia were fixed by a glutaraldehyde/formaldehyde-potassium dichromate-osmium treatment sequence and plastic-embedded. Fine sections were examined by electron probe x-ray microanalysis. Comparable peaks for chromium (Kalpha = 5.4 keV) were obtained from cytoplasmic fields containing membrane-bounded inclusion granules in both adrenomedullary noradrenaline cells and a type (type II) of sympathetic small granulated cell whose inclusion granules closely resemble those of the adrenomedullary noradrenaline cell. Chromium was not detected in granules within adrenomedullary adrenaline cells nor in two other sympathetic small granualted cell types. In no material was chromium detected in agranular cytoplasmic or nuclear fields. Since chromium binds to the Schiff monobase formed by glutaraldehyde and noradrenaline during fixation, we infer that noradrenaline is present in the granules of the type II sympathetic small granulated cell, as well as in adrenomedullary noradrenaline cells.

scholarly journals Role of Ced-3/ICE-family proteases in staurosporine-induced programmed cell death.

1996 ◽  
Vol 133 (5) ◽  
pp. 1041-1051 ◽  
Author(s):  
M D Jacobsen ◽  
M Weil ◽  
M C Raff
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Mammalian Cell ◽  
Mammalian Cells ◽  
Apoptotic Cell ◽  
Interleukin 1 ◽  
Cell Types ◽  
Cysteine Proteases ◽  
A Cell ◽  
Bona Fide

In the accompanying paper by Weil et al. (1996) we show that staurosporine (STS), in the presence of cycloheximide (CHX) to inhibit protein synthesis, induces apoptotic cell death in a large variety of nucleated mammalian cell types, suggesting that all nucleated mammalian cells constitutively express all of the proteins required to undergo programmed cell death (PCD). The reliability of that conclusion depends on the evidence that STS-induced, and (STS + CHS)-induced, cell deaths are bona fide examples of PCD. There is rapidly accumulating evidence that some members of the Ced-3/Interleukin-1 beta converting enzyme (ICE) family of cysteine proteases are part of the basic machinery of PCD. Here we show that Z-Val-Ala-Asp-fluoromethylketone (zVAD-fmk), a cell-permeable, irreversible, tripeptide inhibitor of some of these proteases, suppresses STS-induced and (STS + CHX)-induced cell death in a wide variety of mammalian cell types, including anucleate cytoplasts, providing strong evidence that these are all bona fide examples of PCD. We show that the Ced-3/ICE family member CPP32 becomes activated in STS-induced PCD, and that Bcl-2 inhibits this activation. Most important, we show that, in some cells at least, one or more CPP32-family members, but not ICE itself, is required for STS-induced PCD. Finally, we show that zVAD-fmk suppresses PCD in the interdigital webs in developing mouse paws and blocks the removal of web tissue during digit development, suggesting that this inhibition will be a useful tool for investigating the roles of PCD in various developmental processes.

scholarly journals 20 YEARS OF LEPTIN: Insights into signaling assemblies of the leptin receptor

2014 ◽  
Vol 223 (1) ◽  
pp. T9-T23 ◽  
Author(s):  
Frank Peelman ◽  
Lennart Zabeau ◽  
Kedar Moharana ◽  
Savvas N Savvides ◽  
Jan Tavernier
Keyword(s):  
Electron Microscopy ◽  
Energy Homeostasis ◽  
Leptin Receptor ◽  
Structural Information ◽  
Cell Types ◽  
Activation Mechanism ◽  
Peripheral Cell ◽  
X Ray ◽  
X Ray Crystallography ◽  
X Ray Scattering

Leptin plays a central role in the control of body weight and energy homeostasis, but is a pleiotropic cytokine with activities on many peripheral cell types. In this review, we discuss the interaction of leptin with its receptor, and focus on the structural and mechanistic aspects of the extracellular aspects of leptin receptor (LR) activation. We provide an extensive overview of all structural information that has been obtained for leptin and its receptor via X-ray crystallography, electron microscopy, small-angle X-ray scattering, homology modeling, and mutagenesis studies. The available knowledge is integrated into putative models toward a recapitulation of the LR activation mechanism.

scholarly journals Radiosensitizing performance of uncoated and citrate-coated SPIONs in cancerous and non-cancerous cells

2019 ◽  
pp. 1-9
Author(s):  
Carola Kryschi ◽  
W. Neuhuber ◽  
Damjana Drobne ◽  
Luitpold V. R. Distel ◽  
Stefanie Klein ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Tumor Cells ◽  
High Performance ◽  
Reactive Oxygen ◽  
Superparamagnetic Iron Oxide ◽  
Cell Types ◽  
Oxygen Species ◽  
X Ray ◽  
Adsorption Affinity ◽  
Water Dispersibility

Superparamagnetic iron oxide nanoparticles were shown to exhibit a high performance as X-ray dosage enhancer in tumor cells. The radio-enhancing potential of uncoated and citrate-coated SPIONs was comprehensively studied for tumor and healthy cells. Pristine and citrate-coated SPIONs drastically differ in their water dispersibility and adsorption affinity for proteins. The activities of antioxidant enzymes in the healthy cells were shown to be significantly distinct from those in the tumor cells as containing a much higher H2O2 concentration. Pristine SPIONs catalyzed the Fenton reaction of hydrogen peroxide to the highly reactive hydroxyl radical in all cell types. In contrast, intracellular citrate-stabilized SPIONs were shown t o be non-toxic and to do not affect the formation of reactive oxygen species. X-ray irradiation of citrate-stabilized SPIONs, when internalized by tumor cells, significantly boost the formation of hydroxyl radicals, whereas the healthy cells preserved their initial levels of reactive oxygen species.

scholarly journals Mammalian cell proliferation requires noncatalytic functions of O-GlcNAc transferase

2021 ◽  
Vol 118 (4) ◽  
pp. e2016778118
Author(s):  
Zebulon G. Levine ◽  
Sarah C. Potter ◽  
Cassandra M. Joiner ◽  
George Q. Fei ◽  
Behnam Nabet ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Cell Growth ◽  
Mammalian Cell ◽  
Control Cell ◽  
Cell Types ◽  
Cell Physiology ◽  
Enzymatic Reactions ◽  
A Cell ◽  
Glcnac Transferase ◽  
Catalytic Functions

O-GlcNAc transferase (OGT), found in the nucleus and cytoplasm of all mammalian cell types, is essential for cell proliferation. Why OGT is required for cell growth is not known. OGT performs two enzymatic reactions in the same active site. In one, it glycosylates thousands of different proteins, and in the other, it proteolytically cleaves another essential protein involved in gene expression. Deconvoluting OGT’s myriad cellular roles has been challenging because genetic deletion is lethal; complementation methods have not been established. Here, we developed approaches to replace endogenous OGT with separation-of-function variants to investigate the importance of OGT’s enzymatic activities for cell viability. Using genetic complementation, we found that OGT’s glycosyltransferase function is required for cell growth but its protease function is dispensable. We next used complementation to construct a cell line with degron-tagged wild-type OGT. When OGT was degraded to very low levels, cells stopped proliferating but remained viable. Adding back catalytically inactive OGT rescued growth. Therefore, OGT has an essential noncatalytic role that is necessary for cell proliferation. By developing a method to quantify how OGT’s catalytic and noncatalytic activities affect protein abundance, we found that OGT’s noncatalytic functions often affect different proteins from its catalytic functions. Proteins involved in oxidative phosphorylation and the actin cytoskeleton were especially impacted by the noncatalytic functions. We conclude that OGT integrates both catalytic and noncatalytic functions to control cell physiology.

scholarly journals Salinity tolerance in chickpea is associated with the ability to ‘exclude’ Na from leaf mesophyll cells

2019 ◽  
Vol 70 (18) ◽  
pp. 4991-5002 ◽  
Author(s):  
Lukasz Kotula ◽  
Peta L Clode ◽  
Juan De La Cruz Jimenez ◽  
Timothy D Colmer
Keyword(s):  
Salinity Tolerance ◽  
Structural Damage ◽  
Leaf Tissue ◽  
Cell Types ◽  
Epidermal Cells ◽  
Salinity Treatment ◽  
Mesophyll Cells ◽  
X Ray ◽  
Leaf Mesophyll ◽  
Excessive Accumulation

Abstract Salinity tolerance is associated with Na ‘exclusion’ from, or ‘tissue tolerance’ in, leaves. We investigated whether two contrasting chickpea genotypes, salt-tolerant Genesis836 and salt-sensitive Rupali, differ in leaf tissue tolerance to NaCl. We used X-ray microanalysis to evaluate cellular Na, Cl, and K concentrations in various cell types within leaflets and also in secretory trichomes of the two chickpea genotypes in relation to photosynthesis in control and saline conditions. TEM was used to assess the effects of salinity on the ultrastructure of chloroplasts. Genesis836 maintained net photosynthetic rates (A) for the 21 d of salinity treatment (60 mM NaCl), whereas A in Rupali substantially decreased after 11 d. Leaflet tissue [Na] was low in Genesis836 but had increased markedly in Rupali. In Genesis836, Na was accumulated in epidermal cells but was low in mesophyll cells, whereas in Rupali cellular [Na] was high in both cell types. The excessive accumulation of Na in mesophyll cells of Rupali corresponded to structural damage to the chloroplasts. Maintenance of photosynthesis and thus salinity tolerance in Genesis836 was associated with an ability to ‘exclude’ Na from leaflets and in particular from the photosynthetically active mesophyll cells, and to compartmentalize Na in epidermal cells.

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