Effect of Zinc on Lead Acetate Induced Liver and Stomach Injury in Adult Mice: Electron microscopic and Biochemical Study

2021 ◽  
Vol 41 (2) ◽  
pp. 207-222
Author(s):  
Abeer Ahmed ◽  
Miriam Riad
Keyword(s):  
Lead Acetate ◽  
Biochemical Study ◽  
Electron Microscopic ◽  
Adult Mice

Potentiation of bromotrichloromethane hepatotoxicity in male rats exposed to 10 ppm dietary chlordecone: Electron Microscopic and biochemical study

1990 ◽  
Vol 48 (3) ◽  
pp. 284-285
Author(s):  
O. M. Faroon ◽  
R. W. Henry ◽  
M. G. Soni ◽  
H. M. Mehendale
Keyword(s):  
Free Radical ◽  
Biochemical Study ◽  
Prior Exposure ◽  
Male Rats ◽  
Cellular Injury ◽  
Low Doses ◽  
Mixed Function Oxidase ◽  
Electron Microscopic ◽  
Potent Inducer ◽  
Cellular Energy

Previous work has shown that mirex undergoes photolytic dechlorination to chlordecone (CD) (KeponeR) in the environment. Much work has shown that prior exposure to nontoxic levels of CD causes potentiation of hepatotoxicity and lethality of CCl4, BrCCl3 and other halomethane compounds. Potentiation of bromotrichloromethane hepatotoxicity has been associated with compounds that stimulate the activity of hepatic mixed-function oxidase (MFO). An increase in the metabolism of halomethane by the MFO to a free radical initiates peroxidative decomposition of membranal lipids ending in massive cellular injury. However, not all MFO inducers potentiate BrCCl3 hepatotoxicity. Potentiation by much larger doses of phenobarbital is minimal and th at by a more potent inducer of MFO, mirex, is negligible at low doses. We suggest that the CD and bromotrichloromethane interaction results in a depletion of cellular energy and thereby reducing the cellular ability to undergo mitosis.

scholarly journals Laminin γ3 Chain Binds to Nidogen and Is Located in Murine Basement Membranes

2005 ◽  
Vol 280 (23) ◽  
pp. 22146-22153 ◽  
Author(s):  
Nikolaus Gersdorff ◽  
Eddie Kohfeldt ◽  
Takako Sasaki ◽  
Rupert Timpl ◽  
Nicolai Miosge
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Self Assembly ◽  
Mammalian Cells ◽  
Polyclonal Antibodies ◽  
Basement Membranes ◽  
Electron Microscopic ◽  
Immunogold Staining ◽  
Adult Mice ◽  
Epidermal Growth

Recently a novel laminin γ3 chain was identified in mouse and human and shown to have the same modular structure as the laminin γ1 chain. We expressed two fragments of the γ3 chain in mammalian cells recombinantly. The first, domain VI/V, consisting of laminin N-terminal (domain VI) and four laminin-type epidermal growth factor-like (domain V) and laminin N-terminal modules, was shown to be essential for self-assembly of laminins. The other was domain III3–5, which consists of three laminin-type epidermal growth factor-like modules and is predicted to bind to nidogens. The γ3 VI/V fragment was a poor inhibitor for laminin-1 polymerization as was the β2 VI/V fragment. The γ3 III3–5 fragment bound to nidogen-1 and nidogen-2 with lower affinity than the γ1 III3–5 fragment. These data suggested that laminins containing the γ3 chain may assemble networks independent of other laminins. Polyclonal antibodies raised against γ3 VI/V and γ3 III3–5 showed no cross-reaction with homologous fragments from the γ1 and γ2 chains of laminin and allowed the establishment of γ chain-specific radioimmunoassays and light and electron microscopic immunostaining of tissues. This demonstrated a 20–100-fold lower content of the γ3 chain compared with the γ1 chain in various tissue extracts of adult mice. The expression of γ3 chain was highly tissue-specific. In contrast to earlier assumptions, the antibodies against the γ3 chain showed light microscopic staining exclusively in basement membrane zones of adult and embryonic tissues, such as the brain, kidney, skin, muscle, and testis. Ultrastructural immunogold staining localized the γ3 chain to basement membranes of these tissues.

The Pathobiology of Human Neuromas: An Electron Microscopic and Biochemical Study

1985 ◽  
Vol 10 (1) ◽  
pp. 49-53 ◽  
Author(s):  
MARIE A. BADALAMENTE ◽  
L. C. HURST ◽  
J. ELLSTEIN ◽  
C. A. McDEVITT
Keyword(s):  
Alcian Blue ◽  
Biochemical Study ◽  
Blue Staining ◽  
Alcian Blue Staining ◽  
Post Injury ◽  
Electron Microscopic ◽  
Biochemical Analyses

The formation of neuroma scar after trauma or neurorrhaphy is believed to be mediated by the response of collagen forming fibroblasts. In this study of twenty human neuromas, myofibroblasts were identified as a component of the scar. These cells occurred singly or as aggregates. There was a qualitative increase of myofibroblasts during the period from two to six months post-injury. From six months to one and one-half years post-injury, numbers and aggregations of myofibroblasts diminished, concurrent with collagen proliferation. Ultrastructural alcian blue staining and biochemical analyses revealed a glucosamine—glycosaminoglycan matrix within neuromas when compared to control nerves. Myofibroblasts appear to play a part in the pathobiology of human neuromas.

scholarly journals Aging changes of the testis in albino rat: light, electron microscopic, morphometric, immunohistochemical and biochemical study

2020 ◽  
Vol 79 (3) ◽  
pp. 503-515
Author(s):  
S. M. Hussein ◽  
A. B. El-Fadaly ◽  
A. G. Metawea ◽  
B. E. A. Khaled
Keyword(s):  
Biochemical Study ◽  
Electron Microscopic ◽  
Albino Rat

scholarly journals PHAGOCYTOSIS OF LATEX BEADS BY ACANTHAMOEBA

1967 ◽  
Vol 34 (1) ◽  
pp. 219-227 ◽  
Author(s):  
Edward D. Korn ◽  
Robert A. Weisman
Keyword(s):  
Plasma Membrane ◽  
Biochemical Study ◽  
Electron Microscopic ◽  
Latex Beads ◽  
Microscopic Studies

Electron microscopic studies confirm and extend the conclusions derived previously from a quantitative biochemical study of the phagocytosis of polystyrene and polyvinyltoluene latex beads by Acanthamoeba (1). Latex beads 1.305, 1.90, and 2.68 µ in diameter are ingested individually, with each bead tightly surrounded by a membrane derived from the plasma membrane. Latex beads 0.557, 0.264, 0.126, and 0.088 µ in diameter are accumulated at the surface of the ameba and then phagocytosed, with many beads tightly packed within one membrane-bounded vesicle.

Giant Axonal Degeneration: Scanning Electron Microscopic and Biochemical Study of Scalp Hair

Dermatology ◽  
1994 ◽  
Vol 188 (4) ◽  
pp. 258-262 ◽  
Author(s):  
J. Lycklama á Nijeholt ◽  
H.K. Koerten ◽  
F.A. de Wolff
Keyword(s):  
Axonal Degeneration ◽  
Scalp Hair ◽  
Biochemical Study ◽  
Electron Microscopic ◽  
Scanning Electron Microscopic ◽  
Scanning Electron

Observations on the fragmentation of isolated flight-muscle mitochondria from Calliphora erythrocephala (Diptera)

1965 ◽  
Vol 161 (984) ◽  
pp. 403-420 ◽  
Keyword(s):  
Cytochrome Oxidase ◽  
Flight Muscle ◽  
Biochemical Study ◽  
Sucrose Density Gradient ◽  
Negative Staining ◽  
Electron Microscopic ◽  
Concentrated Suspension ◽  
Calliphora Erythrocephala ◽  
Isolated Mitochondria ◽  
Middle Fraction

A combined electron-microscopic and biochemical study has been made of the disintegration of isolated mitochondria from asynchronous flight muscle of the blowfly Calliphora erythrocephala . These mitochondria are particularly suitable because they can be easily isolated free from other intracellular structures and because of the regularity of their closely packed cristae, seen in fixed (sectioned) and unfixed, negatively stained material. Fragmentation occurs on treatm ent with distilled water, or more rapidly and extensively on sonication. The first stage detected in the disruption of the plate-like cristae is the formation of tubular elements, observed in sectioned preparations. These were seen after negative staining as irregular ribbons, studded with the stalked particles, 80 to 95 Å in diameter, first described by Fernández-Morán. Further fragmentation of the tubules yielded rounded fragments, about 200 to 2000 Å in diameter, apparently by transverse splitting and lateral ‘budding’. These were vesicles, as shown in sectioned material, bearing stalked particles seen by negative staining. After removal of the larger fragments by centrifugation, sonicated material was fractionated on a sucrose density gradient. Protein, cytochrome oxidase activity and rate of reduction of ferricyanide by succinate were determined. A middle fraction with the highest enzymatic activity/ml. of sucrose was found to be a concentrated suspension of vesicles, 200 to 500 Å in diameter, still bearing stalked particles. Little recognizable material was seen in a fraction near the top of the gradient with minimal activity and maximal concentration of (‘soluble’) protein. Available evidence indicates that the cytochrome oxidase and succinate-ferricyanide activities become associated with the vesicles. The activity/mg of protein of the most active fraction was not more than double that of the sonicate. The smaller fragments seemed to be more deficient in cytochrome c than the larger. The stalked particles were firmly attached to cristae, tubules and vesicles, and attempts to remove them were unsuccessful.

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