scholarly journals BDNF stabilizes synapses and maintains the structural complexity of optic axons in vivo

Development ◽  
2005 ◽  
Vol 132 (19) ◽  
pp. 4285-4298 ◽  
Author(s):  
B. Hu
Molecules ◽  
2021 ◽  
Vol 26 (16) ◽  
pp. 4774
Author(s):  
Eric E. Simanek

For two decades, methods for the synthesis and characterization of dendrimers based on [1,3,5]-triazine have been advanced by the group. Motivated by the desire to generate structural complexity on the periphery, initial efforts focused on convergent syntheses, which yielded pure materials to generation three. To obtain larger generations of dendrimers, divergent strategies were pursued using iterative reactions of monomers, sequential additions of triazine and diamines, and ultimately, macromonomers. Strategies for the incorporation of bioactive molecules using non-covalent and covalent strategies have been explored. These bioactive materials included small molecule drugs, peptides, and genetic material. In some cases, these constructs were examined in both in vitro and in vivo models with a focus on targeting prostate tumor subtypes with paclitaxel conjugates. In the materials realm, the use of triazine dendrimers anchored on solid surfaces including smectite clay, silica, mesoporous alumina, polystyrene, and others was explored for the separation of volatile organics from gas streams or the sequestration of atrazine from solution. The combination of these organics with metal nanoparticles has been probed. The goal of this review is to summarize these efforts.


1984 ◽  
Vol 106 (2) ◽  
pp. 485-499 ◽  
Author(s):  
Jerry Silver ◽  
Urs Rutishauser
Keyword(s):  

10.1038/nn735 ◽  
2001 ◽  
Vol 4 (11) ◽  
pp. 1093-1101 ◽  
Author(s):  
Berta Alsina ◽  
Thuy Vu ◽  
Susana Cohen-Cory

1990 ◽  
Vol 110 (2) ◽  
pp. 437-448 ◽  
Author(s):  
R A Nixon ◽  
I Fischer ◽  
S E Lewis

Microtubule-associated proteins (MAPs) in neurons establish functional associations with microtubules, sometimes at considerable distances from their site of synthesis. In this study we identified MAP 1A in mouse retinal ganglion cells and characterized for the first time its in vivo dynamics in relation to axonally transported tubulin. A soluble 340-kD polypeptide was strongly radiolabeled in ganglion cells after intravitreal injection of [35S]methionine or [3H]proline. This polypeptide was identified as MAP 1A on the basis of its co-migration on SDS gels with MAP 1A from brain microtubules; its co-assembly with microtubules in the presence of taxol or during cycles of assembly-disassembly; and its cross-reaction with well-characterized antibodies against MAP 1A in immunoblotting and immunoprecipitation assays. Glial cells of the optic nerve synthesized considerably less MAP 1A than neurons. The axoplasmic transport of MAP 1A differed from that of tubulin. Using two separate methods, we observed that MAP 1A advanced along optic axons at a rate of 1.0-1.2 mm/d, a rate typical of the Group IV (SCb) phase of transport, while tubulin moved 0.1-0.2 mm/d, a group V (SCa) transport rate. At least 13% of the newly synthesized MAP 1A entering optic axons was incorporated uniformly along axons into stationary axonal structures. The half-residence time of stationary MAP 1A in axons (55-60 d) was 4.6 times longer than that of MAP 1A moving in Group IV, indicating that at least 44% of the total MAP 1A in axons is stationary. These results demonstrate that cytoskeletal proteins that become functionally associated with each other in axons may be delivered to these sites at different transport rates. Stable associations between axonal constituents moving at different velocities could develop when these elements leave the transport vector and incorporate into the stationary cytoskeleton.


Author(s):  
C. J. Stratton ◽  
W. H. J. Douglas ◽  
J. A. McAteer

Surfactant studies in general, and particularly those on the type II cell are hindered by the intrinsic cellular heterogeneity and structural complexity of the lung. Indeed, electron microscopic investigations of the lung encounter problems with both non-uniform sampling, and the technical difficulty of preserving intra- and extracellular surfactant through the dehydration steps. Fetal lung organotypic cultures provide a highly enriched type II cell population in which the in vivo cellular relationship of an intact epithelial-mesenchymal interface is maintained. The new lipid-carbohydrate retaining electron microscopic procedures have been shown to preserve most of the structural components of biomembranes and carbohydrate gels, and thus retain the natural appearance of both intra- and extracellular surfactant.Human fetal lung (18 and 18. 5 weeks gestational age) was: enzymatically dissociated (0. 1% trypsin, 0. 1% collagenase, 1. 0% chicken serum in Moscona's saline); filtered; centrifuged (160 x G for 6 minutes); incubated at 37°C for one hour; resuspended in culture medium (Ham's F12K + 10% FBS); and cultured on a Gelfoam collagen sponge.


2021 ◽  
Author(s):  
luis felipe santos mendes ◽  
Mariana R B Batista ◽  
Emanuel Kava ◽  
Lucas Bleicher ◽  
Mariana C Micheletto ◽  
...  

The Golgi complex is a membranous organelle located in the heart of the eukaryotic secretory pathway. A subfamily of the Golgi matrix proteins, called GRASPs, are key players in the stress-induced unconventional secretion, the Golgi dynamics during mitosis/apoptosis, and Golgi ribbon formation. The Golgi ribbon is vertebrate-specific and correlates with the appearance of two GRASP paralogs (GRASP55/GRASP65) and two coiled-coil Golgins (GM130/Golgin45), which interact with each other in vivo. Although essential for the Golgi ribbon formation and the increase in Golgi structural complexity, the molecular details leading to their appearance only in this subphylum are still unknown. Moreover, despite the new functionalities supported by the GRASP paralogy, little is known about the structural and evolutionary differences between these paralogues. In this context, we used ancestor sequence reconstruction and several biophysical/biochemical approaches to assess the evolution of the GRASP structure, flexibility, and how they started anchoring their Golgin partners. Our data showed that the Golgins appeared in evolution and were anchored by the single GRASP ancestor before gorasp gene duplication and divergence in Metazoans. After the gorasp divergence, variations inside the GRASP binding pocket determined which paralogue would recruit each Golgin partner (GRASP55 with Golgin45 and GRASP65 with GM130). These interactions are responsible for the protein's specific Golgi locations and the appearance of the Golgi ribbon. We also suggest that the capacity of GRASPs to form supramolecular structures is a long-standing feature, which likely affects GRASP's participation as a trigger of the stress-induced secretory pathway.


2000 ◽  
Vol 151 (5) ◽  
pp. 1013-1024 ◽  
Author(s):  
Ivelisse Sánchez ◽  
Linda Hassinger ◽  
Ram K. Sihag ◽  
Don W. Cleveland ◽  
Panaiyur Mohan ◽  
...  

The accumulation of neurofilaments required for postnatal radial growth of myelinated axons is controlled regionally along axons by oligodendroglia. Developmentally regulated processes previously suspected of modulating neurofilament number, including heavy neurofilament subunit (NFH) expression, attainment of mature neurofilament subunit stoichiometry, and expansion of interneurofilament spacing cannot be primary determinants of regional accumulation as we show each of these factors precede accumulation by days or weeks. Rather, we find that regional neurofilament accumulation is selectively associated with phosphorylation of a subset of Lys-Ser-Pro (KSP) motifs on heavy neurofilament subunits and medium-size neurofilament subunits (NFMs), rising >50-fold selectively in the expanding portions of optic axons. In mice deleted in NFH, substantial preservation of regional neurofilament accumulation was accompanied by increased levels of the same phosphorylated KSP epitope on NFM. Interruption of oligodendroglial signaling to axons in Shiverer mutant mice, which selectively inhibited this site-specific phosphorylation, reduced regional neurofilament accumulation without affecting other neurofilament properties or aspects of NFH phosphorylation. We conclude that phosphorylation of a specific KSP motif triggered by glia is a key aspect of the regulation of neurofilament number in axons during axonal radial growth.


2020 ◽  
Vol 2020 (11) ◽  
pp. pdb.prot106823
Author(s):  
Rommel Andrew Santos ◽  
Rodrigo Del Rio ◽  
Susana Cohen-Cory

2010 ◽  
Vol 5 (3) ◽  
pp. 328-334 ◽  
Author(s):  
Florencia Palacios ◽  
Germán Cota ◽  
Sofía Horjales ◽  
Analía Lima ◽  
Julio Battistoni ◽  
...  

2014 ◽  
Vol 658 ◽  
pp. 477-482
Author(s):  
Mirela Maria Sava ◽  
Dana Mihaela Suflet ◽  
Yves Berthier ◽  
Ana Maria Trunfio-Sfarghiu

Joint diseases represent a major health problem because they evolve towards the wear of cartilage for which no treatment is really effective. The difficulties in identifying the causes of these diseases are related to the biochemical and structural complexity of synovial fluid that allow cartilage lubrication. Thereby, recent studies show that synovial fluid contains micro-vesicles filled with a glycoprotein gel (hyaluronic acid and protein) surrounded by stacks of lipid bilayers which gives it excellent lubricating properties [1]. On the other side, this stable structure in vivo, becomes unstable in the ex vivo conditions. In this context, the study aims to tests the lubricating properties of synovial fluid constituents in order to identify their role on the tribological behavior of synovial joints and to develop a biomimetic synovial fluid using self-assembly of polyelectrolytes in order to stabilize the ex vivo structure for the potential therapeutic synovial fluid substitutes.Our results show that the new synthetized polysaccharides influence the friction coefficient, the stability and the wear of lipids bilayers, providing lubricating properties superior to synovial fluid biological constituents. In addition, their capacity to be structured in micro-spheres and included in lipid micro-vesicles indicates them as good biomimetic lubricants. This will allow a longer stability of synovial fluid substitutes in ex-vivo conditions in order to achieve the best lubricating properties and to improve the joint diseases treatment.


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