Faculty Opinions recommendation of The Mammalian-Specific Protein Armcx1 Regulates Mitochondrial Transport during Axon Regeneration.

2016 ◽  
Author(s):  
Xinnan Wang
Keyword(s):  
Axon Regeneration ◽  
Specific Protein ◽  
Mitochondrial Transport

scholarly journals The Mammalian-Specific Protein Armcx1 Regulates Mitochondrial Transport during Axon Regeneration

Neuron ◽  
2017 ◽  
Vol 94 (3) ◽  
pp. 689 ◽  
Author(s):  
Romain Cartoni ◽  
Michael W. Norsworthy ◽  
Fengfeng Bei ◽  
Chen Wang ◽  
Siwei Li ◽  
...  
Keyword(s):  
Axon Regeneration ◽  
Specific Protein ◽  
Mitochondrial Transport

scholarly journals The Mammalian-Specific Protein Armcx1 Regulates Mitochondrial Transport during Axon Regeneration

Neuron ◽  
2016 ◽  
Vol 92 (6) ◽  
pp. 1294-1307 ◽  
Author(s):  
Romain Cartoni ◽  
Michael W. Norsworthy ◽  
Fengfeng Bei ◽  
Chen Wang ◽  
Siwei Li ◽  
...  
Keyword(s):  
Axon Regeneration ◽  
Specific Protein ◽  
Mitochondrial Transport

scholarly journals Mitochondrial Behavior in Axon Degeneration and Regeneration

2021 ◽  
Vol 13 ◽  
Author(s):  
Biyao Wang ◽  
Minghao Huang ◽  
Dehao Shang ◽  
Xu Yan ◽  
Baohong Zhao ◽  
...  
Keyword(s):  
Axon Regeneration ◽  
Early Stage ◽  
Mitochondrial Dynamics ◽  
Neurological Diseases ◽  
Signal Transmission ◽  
High Energy ◽  
Biological Behavior ◽  
Axon Degeneration ◽  
Mitochondrial Transport ◽  
Cord Injury

Mitochondria are organelles responsible for bioenergetic metabolism, calcium homeostasis, and signal transmission essential for neurons due to their high energy consumption. Accumulating evidence has demonstrated that mitochondria play a key role in axon degeneration and regeneration under physiological and pathological conditions. Mitochondrial dysfunction occurs at an early stage of axon degeneration and involves oxidative stress, energy deficiency, imbalance of mitochondrial dynamics, defects in mitochondrial transport, and mitophagy dysregulation. The restoration of these defective mitochondria by enhancing mitochondrial transport, clearance of reactive oxidative species (ROS), and improving bioenergetic can greatly contribute to axon regeneration. In this paper, we focus on the biological behavior of axonal mitochondria in aging, injury (e.g., traumatic brain and spinal cord injury), and neurodegenerative diseases (Alzheimer's disease, AD; Parkinson's disease, PD; Amyotrophic lateral sclerosis, ALS) and consider the role of mitochondria in axon regeneration. We also compare the behavior of mitochondria in different diseases and outline novel therapeutic strategies for addressing abnormal mitochondrial biological behavior to promote axonal regeneration in neurological diseases and injuries.

scholarly journals Facilitation of axon regeneration by enhancing mitochondrial transport and rescuing energy deficits

2016 ◽  
Vol 214 (1) ◽  
pp. 103-119 ◽  
Author(s):  
Bing Zhou ◽  
Panpan Yu ◽  
Mei-Yao Lin ◽  
Tao Sun ◽  
Yanmin Chen ◽  
...  
Keyword(s):  
Axon Regeneration ◽  
Genetic Manipulation ◽  
Atp Depletion ◽  
Sciatic Nerve Crush ◽  
Nerve Crush ◽  
Mitochondrial Transport ◽  
Anchoring Protein ◽  
Mature Neuron ◽  
Mature Neurons

Although neuronal regeneration is a highly energy-demanding process, axonal mitochondrial transport progressively declines with maturation. Mature neurons typically fail to regenerate after injury, thus raising a fundamental question as to whether mitochondrial transport is necessary to meet enhanced metabolic requirements during regeneration. Here, we reveal that reduced mitochondrial motility and energy deficits in injured axons are intrinsic mechanisms controlling regrowth in mature neurons. Axotomy induces acute mitochondrial depolarization and ATP depletion in injured axons. Thus, mature neuron-associated increases in mitochondria-anchoring protein syntaphilin (SNPH) and decreases in mitochondrial transport cause local energy deficits. Strikingly, enhancing mitochondrial transport via genetic manipulation facilitates regenerative capacity by replenishing healthy mitochondria in injured axons, thereby rescuing energy deficits. An in vivo sciatic nerve crush study further shows that enhanced mitochondrial transport in snph knockout mice accelerates axon regeneration. Understanding deficits in mitochondrial trafficking and energy supply in injured axons of mature neurons benefits development of new strategies to stimulate axon regeneration.

Densitometric Identification of Primitive Erythroblasts After Reaction With Diaminobenzidine

1973 ◽  
Vol 31 ◽  
pp. 328-329
Author(s):  
John A. Trotter
Keyword(s):  
Red Blood Cells ◽  
Analytical Method ◽  
Blood Cells ◽  
Guinea Pigs ◽  
Specific Protein ◽  
Visual Examination ◽  
Hemoglobin Synthesis ◽  
Peroxidatic Activity ◽  
Small Density

Hemoglobin is the specific protein of red blood cells. Those cells in which hemoglobin synthesis is initiated are the earliest cells that can presently be considered to be committed to erythropoiesis. In order to identify such early cells electron microscopically, we have made use of the peroxidatic activity of hemoglobin by reacting the marrow of erythropoietically stimulated guinea pigs with diaminobenzidine (DAB). The reaction product appeared as a diffuse and amorphous electron opacity throughout the cytoplasm of reactive cells. The detection of small density increases of such a diffuse nature required an analytical method more sensitive and reliable than the visual examination of micrographs. A procedure was therefore devised for the evaluation of micrographs (negatives) with a densitometer (Weston Photographic Analyzer).

Specific Labeling of Protein Domains with Antibody Fragments

1981 ◽  
Vol 39 ◽  
pp. 416-417
Author(s):  
U. Aebi ◽  
L.E. Buhle ◽  
W.E. Fowler
Keyword(s):  
Image Processing ◽  
Specific Protein ◽  
Antibody Fragments ◽  
Supramolecular Organization ◽  
Two Dimensional ◽  
Ordered Structures ◽  
Virus Capsids ◽  
Processing Techniques

Many important supramolecular structures such as filaments, microtubules, virus capsids and certain membrane proteins and bacterial cell walls exist as ordered polymers or two-dimensional crystalline arrays in vivo. In several instances it has been possible to induce soluble proteins to form ordered polymers or two-dimensional crystalline arrays in vitro. In both cases a combination of electron microscopy of negatively stained specimens with analog or digital image processing techniques has proven extremely useful for elucidating the molecular and supramolecular organization of the constituent proteins. However from the reconstructed stain exclusion patterns it is often difficult to identify distinct stain excluding regions with specific protein subunits. To this end it has been demonstrated that in some cases this ambiguity can be resolved by a combination of stoichiometric labeling of the ordered structures with subunit-specific antibody fragments (e.g. Fab) and image processing of the electron micrographs recorded from labeled and unlabeled structures.

Immunocytochemical localization of p65 with one-nanometer gold particles following silver development

1989 ◽  
Vol 47 ◽  
pp. 1042-1043
Author(s):  
Richard W. Burry ◽  
Diane M. Hayes
Keyword(s):  
Plasma Membrane ◽  
Bovine Serum Albumin ◽  
Calf Serum ◽  
Specific Protein ◽  
Immunocytochemical Localization ◽  
Electron Microscopic ◽  
Gold Particles ◽  
Pass Through ◽  
Label Distribution ◽  
Phosphate Buffered Saline

Electron microscopic (EM) immunocytochemistry localization of the neuron specific protein p65 could show which organelles contain this antigen. Antibodies (Ab) labeled with horseradish peroxidase (HRP) followed by chromogen development show a broad diffuse label distribution within cells and restricting identification of organelles. Particulate label (e.g. 10 nm colloidal gold) is highly desirable but not practical because penetration into cells requires destroying the plasma membrane. We report pre-embedding immunocytochemistry with a particulate marker, 1 nm gold, that will pass through membranes treated with saponin, a mild detergent.Cell cultures of the rat cerebellum were fixed in buffered 4% paraformaldehyde and 0.1% glutaraldehyde (Glut.). The buffer for all incubations and rinses was phosphate buffered saline with: 1% calf serum, 0.2% saponin, 0.1% gelatin, 50 mM glycine 1 mg/ml bovine serum albumin, and (not in the HRP labeled cultures) 0.02% sodium azide. The monoclonal #48 to p65 was used with three label systems: HRP, 1 nm avidin gold with IntenSE M development, and 1 nm avidin gold with Danscher development.

Sign in / Sign up

Export Citation Format

Share Document