scholarly journals Labelling by axonal transport of myelin-associated proteins in the rabbit visual pathway

1981 ◽  
Vol 196 (2) ◽  
pp. 537-545 ◽  
Author(s):  
P P Giorgi ◽  
H DuBois
Keyword(s):  
Axonal Transport ◽  
Sodium Dodecyl ◽  
Specific Radioactivity ◽  
Visual Pathway ◽  
Water Soluble ◽  
Labelling Pattern ◽  
Myelin Proteins ◽  
Survival Times ◽  
Anterograde Axonal Transport ◽  
Associated Proteins

After intraocular injections of [3H]leucine, six regions of the visual pathway of adult rabbit were used to study the spatio-temporal pattern of the slow anterograde axonal transport of radioactive proteins associated with the particulate fraction, the water-soluble fraction and the myelin fraction. Unlike other fractions, myelin-associated labelled proteins represented a time-constant (for a given region) percentage of total tissue radioactivity. This percentage increased from the first half to the second half of the optic nerve and remained high in the chiasma and tract. The peak specific radioactivity of myelin decreased in the same direction. Myelin proteins were separated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and the labelling patterns obtained in different regions and at different survival times were compared. At the peak of myelin radioactivity of a given region the label was typically associated with four protein bands, L1, L2, L3 and L4, of 40000, 44000, 62000, and 68000 mol.wts. respectively. The basic protein, the proteolipid protein and the W1 component (mol.wt. 51000-53000) of the Wolfgram proteins were not significantly labelled. The radioactivity associated with the W2 component (mol.wt 60000) of the Wolfgram proteins could be derived from the closely migrating L3 component. At shorter survival times no clear labelling pattern could be detected. At longer survival times radioactivity was almost totally localized around band L3. The results presented underline the importance of choosing appropriate experimental conditions to obtain a consistent labelling pattern of myelin-associated proteins and to investigate the possible mechanism responsible for this phenomenon.

scholarly journals Role of MAP1B in axonal retrograde transport of mitochondria

2006 ◽  
Vol 397 (1) ◽  
pp. 53-59 ◽  
Author(s):  
Eva-María Jiménez-Mateos ◽  
Christian González-Billault ◽  
Hana N. Dawson ◽  
Michael P. Vitek ◽  
Jesús Avila
Keyword(s):  
Axonal Transport ◽  
Retrograde Transport ◽  
Precise Control ◽  
Microtubule Associated Proteins ◽  
Anterograde Axonal Transport ◽  
Associated Proteins ◽  
Regulation Of Transport ◽  
The Stability ◽  
Additional Role

The MAPs (microtubule-associated proteins) MAP1B and tau are well known for binding to microtubules and stabilizing these structures. An additional role for MAPs has emerged recently where they appear to participate in the regulation of transport of cargos on the microtubules found in axons. In this role, tau has been associated with the regulation of anterograde axonal transport. We now report that MAP1B is associated with the regulation of retrograde axonal transport of mitochondria. This finding potentially provides precise control of axonal transport by MAPs at several levels: controlling the anterograde or retrograde direction of transport depending on the type of MAP involved, controlling the speed of transport and controlling the stability of the microtubule tracks upon which transport occurs.

scholarly journals Interaction of autoantibodies to thyrotropin receptor with a hydrophilic subunit of the thyrotropin receptor

1985 ◽  
Vol 228 (1) ◽  
pp. 111-117 ◽  
Author(s):  
E Davies Jones ◽  
F A Hashim ◽  
Y Kajita ◽  
F M Creagh ◽  
P R Buckland ◽  
...  
Keyword(s):  
Gradient Centrifugation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Water Soluble ◽  
Tsh Receptor ◽  
Human Thyroid ◽  
Thyrotropin Receptor ◽  
Freezing And Thawing ◽  
Sucrose Density Gradient Centrifugation ◽  
A Subunit

Reduction of human thyroid membranes with dithiothreitol caused the release of a water-soluble glycoprotein which neutralized the thyrotropin (TSH) receptor-binding and thyroid-stimulating activities of Graves‘ serum. Analysis of the protein by gel filtration and sucrose density gradient centrifugation allowed estimates of 3.45 nm for the Stokes’ radius, 3.6 S for the s20,w and 47 000 +/- 5000 (mean +/- S.D.; n = 4) for the Mr. The material released by dithiothreitol treatment could be crosslinked to 125I-labelled TSH coupled to N-hydroxysuccinimidyl 4-azidobenzoate (125I-HSAB-TSH), suggesting that it contained a component of the TSH receptor. Furthermore, analysis of the crosslinked material by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis indicated that it contained the TSH receptor A subunit (Mr 50 000). Several factors suggested therefore that the glycoprotein released by dithiothreitol treatment of human thyroid membranes was the TSH receptor A subunit. In particular, (a) both preparations were hydrophilic and were released from membranes by reduction, (b) they had similar Mr values and (c) both preparations crosslinked to 125I-HSAB-TSH. Material similar to the TSH receptor A subunit was released from thyroid membranes by treatment with papain, probably as a result of cleavage of the receptor A subunit at a site close to the interchain disulphide bridge. A similar mechanism, involving thyroid proteinases, was probably involved in release of material with similar properties to the TSH receptor A subunit during freezing and thawing of human thyroid homogenates.

The bovine herpesvirus type 1 envelope protein Us9 acidic domain is crucial for anterograde axonal transport

2011 ◽  
Vol 152 (3-4) ◽  
pp. 270-279 ◽  
Author(s):  
S.I. Chowdhury ◽  
M.C.S. Brum ◽  
C. Coats ◽  
A. Doster ◽  
Huiyong Wei ◽  
...  
Keyword(s):  
Axonal Transport ◽  
Envelope Protein ◽  
Bovine Herpesvirus ◽  
Herpesvirus Type ◽  
Acidic Domain ◽  
Anterograde Axonal Transport ◽  
Bovine Herpesvirus Type 1

Isolation and Tissue Specificity of Chromatin Associated Proteins in Vicia faba

1975 ◽  
Vol 53 (1) ◽  
pp. 91-95 ◽  
Author(s):  
Barbara Grahek Mischke ◽  
Oscar G. Ward
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Vicia Faba ◽  
Tissue Specificity ◽  
Gene Action ◽  
Sodium Dodecyl ◽  
Acid Extraction ◽  
Dodecyl Sulfate ◽  
Associated Proteins ◽  
Different Tissues

A method is described that permits extraction of one class of non-histones in 8 M urea −0.14 M mercaptoethanol prior to acid extraction of histones and a second class in 0.05 M Tris – 1% sodium dodecyl sulfate following acid extraction of histones. Comparisons of histones and non-histones extracted by this method with those obtained by other procedures demonstrate two important advantages of the method: (1) histones obtained by this method are not contaminated by acid-soluble non-histones, and (2) non-histones are not subjected to acid or phenol during extraction. Changes in the distributions of chromatin-associated proteins in different tissues suggest that some species represent regulators of gene action.

scholarly journals Anterograde Axonal Transport in Neuronal Homeostasis and Disease

2020 ◽  
Vol 13 ◽  
Author(s):  
Laurent Guillaud ◽  
Sara Emad El-Agamy ◽  
Miki Otsuki ◽  
Marco Terenzio
Keyword(s):  
Axonal Transport ◽  
Neuronal Homeostasis ◽  
Anterograde Axonal Transport

scholarly journals Preparation of Co-Amorphous Systems by Freeze-Drying

Pharmaceutics ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 941
Author(s):  
Melvin Wostry ◽  
Hanna Plappert ◽  
Holger Grohganz
Keyword(s):  
Amino Acid ◽  
Freeze Drying ◽  
Sodium Dodecyl ◽  
Solid Content ◽  
Water Soluble ◽  
Tween 20 ◽  
Scanning Calorimetry ◽  
Total Solid Content ◽  
Amorphous Systems ◽  
Freeze Dried

Freeze-drying was evaluated as a production technique for co-amorphous systems of a poorly water-soluble drug. Naproxen was freeze-dried together with arginine and lysine as co-former. To increase the solubility of naproxen in the starting solution, the applicability of five surfactants was investigated, namely sodium dodecyl sulfate, pluronic F-127, polyoxyethylene (40) stearate, tween 20 and TPGS 1000. The influence of the surfactant type, surfactant concentration and total solid content to be freeze-dried on the solid state of the sample was investigated. X-ray powder diffraction and differential scanning calorimetry showed that the majority of systems formed co-amorphous one-phase systems. However, at higher surfactant concentrations, and depending on the surfactant type, surfactant reflections were observed in the XRPD analysis upon production. Crystallization of both naproxen and amino acid occurred from some combinations under storage. In conclusion, freeze-drying was shown to be a feasible technique for the production of a selection of co-amorphous drug–amino acid formulations.

scholarly journals In Vitro Characterization of Rabbit Thrombin, Antithrombin III, and Thrombin-Antithrombin III Complex, and Determination of Their Survival Times in Vivo

1977 ◽  
Author(s):  
Christine N. Vogel ◽  
Kingdon S. Henry ◽  
Roger L. Lundblad
Keyword(s):  
Gel Electrophoresis ◽  
Half Life ◽  
Antithrombin Iii ◽  
Specific Activity ◽  
Sodium Dodecyl ◽  
In Vivo Studies ◽  
Survival Times ◽  
At Iii

Our intention is to study the interaction of rabbit thrombin with antithrombin III (AT-III) in vitro and in vivo. After activation of crude prothrombin with tissue thromboplastin and CaCl2, thrombin was purified and showed two species of thrombin with molecular weights of 36,000 and 39,000 daltons as determined by sodium dodecyl sulfate discontinuous gel electrophoresis. Rabbit AT-III was purified using a heparin agarose column and had a molecular weight of 55,000 daltons. The inhibition of thrombin by AT-III was followed by fibrinogen clotting assays and an AT-III-thrombin complex was observed on gel electrophoresis. For the in vivo studies both thrombin and AT-III were radiolabelled with Na125i using the solid state lactoperoxidase method and retained 99% of the pre-iodinated specific activity. Radiolabelled thrombin and a radiolabelled AT-III-thrombin complex were injected into different rabbits. The rate of removal of both was very similar with a half-life of approximately 9 hours. When radiolabelled AT-III was injected, the half-life was approximately 60 hours. Since the disappearance rate of thrombin more closely approximates that of the preformed AT-III-thrombin complex and is clearly shorter than the turnover rate of AT-III, the possibility is raised that thrombin combines in vivo with a native inhibitor such as AT-III and may in fact be removed from the circulation as a complex rather than as a native molecule.

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