scholarly journals Semaphorin 3A Binds to the Perineuronal Nets via Chondroitin Sulfate Type E Motifs in Rodent Brains

2013 ◽  
Vol 288 (38) ◽  
pp. 27384-27395 ◽  
Author(s):  
Gunnar Dick ◽  
Chin Lik Tan ◽  
Joao Nuno Alves ◽  
Erich M. E. Ehlert ◽  
Gregory M. Miller ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Chondroitin Sulfate ◽  
Rat Brain ◽  
Core Protein ◽  
Axon Growth ◽  
Chondroitin Sulfate Proteoglycans ◽  
Perineuronal Nets ◽  
Chondroitinase Abc ◽  
Blocking Antibody ◽  
Guidance Molecule

Chondroitin sulfate (CS) and the CS-rich extracellular matrix structures called perineuronal nets (PNNs) restrict plasticity and regeneration in the CNS. Plasticity is enhanced by chondroitinase ABC treatment that removes CS from its core protein in the chondroitin sulfate proteoglycans or by preventing the formation of PNNs, suggesting that chondroitin sulfate proteoglycans in the PNNs control plasticity. Recently, we have shown that semaphorin3A (Sema3A), a repulsive axon guidance molecule, localizes to the PNNs and is removed by chondroitinase ABC treatment (Vo, T., Carulli, D., Ehlert, E. M., Kwok, J. C., Dick, G., Mecollari, V., Moloney, E. B., Neufeld, G., de Winter, F., Fawcett, J. W., and Verhaagen, J. (2013) Mol. Cell. Neurosci. 56C, 186–200). Sema3A is therefore a candidate for a PNN effector in controlling plasticity. Here, we characterize the interaction of Sema3A with CS of the PNNs. Recombinant Sema3A interacts with CS type E (CS-E), and this interaction is involved in the binding of Sema3A to rat brain-derived PNN glycosaminoglycans, as demonstrated by the use of CS-E blocking antibody GD3G7. In addition, we investigate the release of endogenous Sema3A from rat brain by biochemical and enzymatic extractions. Our results confirm the interaction of Sema3A with CS-E containing glycosaminoglycans in the dense extracellular matrix of rat brain. We also demonstrate that the combination of Sema3A and PNN GAGs is a potent inhibitor of axon growth, and this inhibition is reduced by the CS-E blocking antibody. In conclusion, Sema3A binding to CS-E in the PNNs may be a mechanism whereby PNNs restrict growth and plasticity and may represent a possible point of intervention to facilitate neuronal plasticity.

scholarly journals Transient accumulation of perisinusoidal chondroitin sulfate proteoglycans during liver regeneration and development.

1996 ◽  
Vol 44 (9) ◽  
pp. 969-980 ◽  
Author(s):  
T Yada ◽  
N Koide ◽  
K Kimata
Keyword(s):  
Extracellular Matrix ◽  
Chondroitin Sulfate ◽  
Partial Hepatectomy ◽  
Rat Liver ◽  
Core Protein ◽  
Chondroitin Sulfate Proteoglycans ◽  
Neonatal Rat ◽  
Complete Restoration ◽  
Extracellular Matrix Components ◽  
And Function

After partial hepatectomy, the liver is capable of complete restoration of normal hepatic size, architecture, and function (regeneration). To study roles of the extracellular matrix in regeneration, the temporal and spatial sequences of deposition of several components, including collagen I, III, and IV, fibronectin, laminin, heparan sulfate proteoglycan (perlecan), and chondroitin sulfate proteoglycans were characterized by light microscopic immunohistochemistry in rat liver after 70% partial hepatectomy. Consistent with previous reports, there was a brisk mitosis of hepatocytes after the partial hepatectomy. Of the extracellular matrix components studied, 1B5 epitope generated by chondroitinase ABC digestion on chondroitin sulfate proteoglycans exhibited the most dramatic changes; the epitope was detectable as early as 1.5 hr after partial hepatectomy and its immunoreactivity reached a maximum at 24 hr, then declined gradually. This transient expression of the 1B5 epitope was also detected in neonatal rat liver during development. By Western blotting, the 1B5 epitope was found on two forms of the core protein of chondroitin sulfate proteoglycans with apparent molecular masses of 163 KD and 152 KD, which were also regulated in the same temporal manner.

scholarly journals Chondroitin 6-Sulfation Regulates Perineuronal Net Formation by Controlling the Stability of Aggrecan

2016 ◽  
Vol 2016 ◽  
pp. 1-13 ◽  
Author(s):  
Shinji Miyata ◽  
Hiroshi Kitagawa
Keyword(s):  
Extracellular Matrix ◽  
Chondroitin Sulfate ◽  
Neural Plasticity ◽  
Adult Brain ◽  
Chondroitin Sulfate Proteoglycans ◽  
Perineuronal Nets ◽  
Perineuronal Net ◽  
A Disintegrin And Metalloproteinase ◽  
The Stability ◽  
Thrombospondin Motif

Perineuronal nets (PNNs) are lattice-like extracellular matrix structures composed of chondroitin sulfate proteoglycans (CSPGs). The appearance of PNNs parallels the decline of neural plasticity, and disruption of PNNs reactivates neural plasticity in the adult brain. We previously reported that sulfation patterns of chondroitin sulfate (CS) chains on CSPGs influenced the formation of PNNs and neural plasticity. However, the mechanism of PNN formation regulated by CS sulfation remains unknown. Here we found that overexpression of chondroitin 6-sulfotransferase-1 (C6ST-1), which catalyzes 6-sulfation of CS chains, selectively decreased aggrecan, a major CSPG in PNNs, in the aged brain without affecting other PNN components. Both diffuse and PNN-associated aggrecans were reduced by overexpression of C6ST-1. C6ST-1 increased 6-sulfation in both the repeating disaccharide region and linkage region of CS chains. Overexpression of 6-sulfation primarily impaired accumulation of aggrecan in PNNs, whereas condensation of other PNN components was not affected. Finally, we found that increased 6-sulfation accelerated proteolysis of aggrecan by a disintegrin and metalloproteinase domain with thrombospondin motif (ADAMTS) protease. Taken together, our results indicate that sulfation patterns of CS chains on aggrecan influenced the stability of the CSPG, thereby regulating formation of PNNs and neural plasticity.

scholarly journals HDAC6 and Miro1: Another interaction causing trouble in neurons

2019 ◽  
Vol 218 (6) ◽  
pp. 1769-1770 ◽  
Author(s):  
Ludo Van Den Bosch
Keyword(s):  
Extracellular Matrix ◽  
Chondroitin Sulfate ◽  
Axonal Transport ◽  
Axonal Growth ◽  
Growth Cones ◽  
Chondroitin Sulfate Proteoglycans ◽  
Cell Biol ◽  
Myelin Associated Glycoprotein

Myelin-associated glycoprotein and chondroitin sulfate proteoglycans in the extracellular matrix can prevent regeneration of injured axons. In this issue, Kalinski et al. (2019. J. Cell Biol. https://doi.org/10.1083/jcb.201702187) report that inhibition of HDAC6 prevents the deacetylation of Miro1, increases mitochondrial axonal transport, and restores the size of axonal growth cones.

Acute and long-lasting changes in extracellular-matrix chondroitin-sulphate proteoglycans induced by injection of chondroitinase ABC in the adult rat brain

1998 ◽  
Vol 121 (3) ◽  
pp. 300-310 ◽  
Author(s):  
G. Brückner ◽  
Andreas Bringmann ◽  
Wolfgang Härtig ◽  
Gerlinde Köppe ◽  
Bertrand Delpech ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Rat Brain ◽  
Chondroitin Sulphate ◽  
Chondroitinase Abc ◽  
Adult Rat ◽  
Chondroitin Sulphate Proteoglycans ◽  
Adult Rat Brain

scholarly journals Membrane-associated chondroitin sulfate proteoglycans of human lung fibroblasts.

1989 ◽  
Vol 108 (3) ◽  
pp. 1165-1173 ◽  
Author(s):  
G David ◽  
V Lories ◽  
A Heremans ◽  
B Van der Schueren ◽  
J J Cassiman ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Human Lung ◽  
Core Protein ◽  
Human Fibroblasts ◽  
Chondroitin Sulfate Proteoglycans ◽  
Lung Fibroblasts ◽  
Hydrophobic Membrane ◽  
Human Lung Fibroblasts ◽  
Core Proteins

Cultured human fetal lung fibroblasts produce some chondroitin sulfate proteoglycans that are extracted as an aggregate in chaotropic buffers containing 4 M guanidinium chloride. The aggregated proteoglycans are excluded from Sepharose CL4B and 2B, but become included, eluting with a Kav value of 0.53 from Sepharose CL4B, when Triton X-100 is included in the buffer. Conversely, some of the detergent-extractable chondroitin sulfate proteoglycans can be incorporated into liposomes, suggesting the existence of a hydrophobic membrane-intercalated chondroitin sulfate proteoglycan fraction. Purified preparations of hydrophobic chondroitin sulfate proteoglycans contain two major core protein forms of 90 and 52 kD. A monoclonal antibody (F58-7D8) obtained from the fusion of myeloma cells with spleen cells of BALB/c mice that were immunized with hydrophobic proteoglycans recognized the 90- but not the 52-kD core protein. The epitope that is recognized by the antibody is exposed at the surface of cultured human lung fibroblasts and at the surface of several stromal cells in vivo, but also at the surface of Kupffer cells and of epidermal cells. The core proteins of these small membrane-associated chondroitin sulfate proteoglycans are probably distinct from those previously identified in human fibroblasts by biochemical, immunological, and molecular biological approaches.

scholarly journals Integrin Activation Promotes Axon Growth on Inhibitory Chondroitin Sulfate Proteoglycans by Enhancing Integrin Signaling

2011 ◽  
Vol 31 (17) ◽  
pp. 6289-6295 ◽  
Author(s):  
C. L. Tan ◽  
J. C. F. Kwok ◽  
R. Patani ◽  
C. ffrench-Constant ◽  
S. Chandran ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Axon Growth ◽  
Chondroitin Sulfate Proteoglycans ◽  
Integrin Signaling ◽  
Integrin Activation

scholarly journals Kindlin-1 Enhances Axon Growth on Inhibitory Chondroitin Sulfate Proteoglycans and Promotes Sensory Axon Regeneration

2012 ◽  
Vol 32 (21) ◽  
pp. 7325-7335 ◽  
Author(s):  
C. L. Tan ◽  
M. R. Andrews ◽  
J. C. F. Kwok ◽  
T. G. P. Heintz ◽  
L. F. Gumy ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Axon Regeneration ◽  
Axon Growth ◽  
Chondroitin Sulfate Proteoglycans ◽  
Sensory Axon

Interferon Gamma Binds to Extracellular Matrix Chondroitin-Sulfate Proteoglycans, Thus Enhancing Its Cellular Response

1995 ◽  
Vol 15 (9) ◽  
pp. 1456-1465 ◽  
Author(s):  
Eva Hurt Camejo ◽  
Birgitta Rosengren ◽  
Germán Camejo ◽  
Peter Sartipy ◽  
Gunnar Fager ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Chondroitin Sulfate ◽  
Interferon Gamma ◽  
Cellular Response ◽  
Chondroitin Sulfate Proteoglycans

scholarly journals Development and Structural Variety of the Chondroitin Sulfate Proteoglycans-Contained Extracellular Matrix in the Mouse Brain

2015 ◽  
Vol 2015 ◽  
pp. 1-12 ◽  
Author(s):  
Noriko Horii-Hayashi ◽  
Takayo Sasagawa ◽  
Wataru Matsunaga ◽  
Mayumi Nishi
Keyword(s):  
Extracellular Matrix ◽  
Chondroitin Sulfate ◽  
Brain Stem ◽  
Cranial Nerves ◽  
Lectin Histochemistry ◽  
Chondroitin Sulfate Proteoglycans ◽  
Amygdaloid Nucleus ◽  
Critical Periods ◽  
Structural Variety ◽  
The Brain

Chondroitin sulfate proteoglycans (CSPGs) are major components of the extracellular matrix (ECM) in the brain. In adult mammals, CSPGs form the specialized ECM structure perineuronal nets (PNNs) that surround somata and dendrites of certain types of neurons. PNNs restrict synaptic plasticity and regulate the closure of critical periods. Although previous studies have examined the starting period of PNN formation, focusing on primary sensory cortices, there are no systematic studies at the whole brain level. Here, we examined the starting period of PNN formation in male mice ranging in age from postnatal day 3 to week 11, mainly focusing on several cortical areas, limbic structures, hypothalamus, and brain stem, using lectin histochemistry withWisteria floribundaagglutinin (WFA). Results showed that early PNN formation was observed in several reticular formations of the brain stem related to the cranial nerves and primary somatosensory cortices. In the limbic system, PNN formation in the hippocampus started earlier than that of the amygdala. Furthermore, in the medial amygdaloid nucleus and some hypothalamic regions, WFA labeling did not show typical PNN-like forms. The present study suggests spatiotemporal differences at the beginning of PNN formation and a structural variety of CSPG-contained ECM in the brain.

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