scholarly journals Degradation of extracellular chondroitin sulfate delays recovery of network activity after perturbation

2015 ◽  
Vol 114 (2) ◽  
pp. 1346-1352 ◽  
Author(s):  
Amber E. Hudson ◽  
Clare Gollnick ◽  
Jean-Philippe Gourdine ◽  
Astrid A. Prinz
Keyword(s):  
Extracellular Matrix ◽  
Chondroitin Sulfate ◽  
Neural Circuitry ◽  
Model System ◽  
Chondroitin Sulfate Proteoglycans ◽  
Network Activity ◽  
Neuronal Circuit ◽  
Cancer Borealis ◽  
Cellular Effects

Chondroitin sulfate proteoglycans (CSPGs) are widely studied in vertebrate systems and are known to play a key role in development, plasticity, and regulation of cortical circuitry. The mechanistic details of this role are still elusive, but increasingly central to the investigation is the homeostatic balance between network excitation and inhibition. Studying a simpler neuronal circuit may prove advantageous for discovering the mechanistic details of the cellular effects of CSPGs. In this study we used a well-established model of homeostatic change after injury in the crab Cancer borealis to show first evidence that CSPGs are necessary for network activity homeostasis. We degraded CSPGs in the pyloric circuit of the stomatogastric ganglion with the enzyme chondroitinase ABC (chABC) and found that removal of CSPGs does not influence the ongoing rhythm of the pyloric circuit but does limit its capacity for recovery after a networkwide perturbation. Without CSPGs, the postperturbation rhythm is slower than in controls and rhythm recovery is delayed. In addition to providing a new model system for the study of CSPGs, this study suggests a wider role for CSPGs, and perhaps the extracellular matrix in general, beyond simply plastic reorganization (as observed in mammals) and into a foundational regulatory role of neural circuitry.

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.

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.

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 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 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.

scholarly journals Role of chondroitin sulfate proteoglycans (CSPGs) in synaptic plasticity and neurotransmission in mammalian spinal cord.

2009 ◽  
Author(s):  
Arsen Hunanyan ◽  
Guillermo Garcia-Alias ◽  
Joel Levine ◽  
James Fawcett ◽  
Lorne Mendell ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Synaptic Plasticity ◽  
Chondroitin Sulfate ◽  
Chondroitin Sulfate Proteoglycans

scholarly journals Role of Chondroitin Sulfate Proteoglycans in Axonal Conduction in Mammalian Spinal Cord

2010 ◽  
Vol 30 (23) ◽  
pp. 7761-7769 ◽  
Author(s):  
A. S. Hunanyan ◽  
G. Garcia-Alias ◽  
V. Alessi ◽  
J. M. Levine ◽  
J. W. Fawcett ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Chondroitin Sulfate ◽  
Chondroitin Sulfate Proteoglycans ◽  
Axonal Conduction

scholarly journals The Role of Chondroitin Sulfate Proteoglycans in Nervous System Development

2020 ◽  
Vol 69 (1) ◽  
pp. 61-80 ◽  
Author(s):  
Caitlin P. Mencio ◽  
Rowan K. Hussein ◽  
Panpan Yu ◽  
Herbert M. Geller
Keyword(s):  
Nervous System ◽  
Chondroitin Sulfate ◽  
Neural Development ◽  
Synapse Formation ◽  
Current Knowledge ◽  
System Development ◽  
Nervous System Development ◽  
Chondroitin Sulfate Proteoglycans ◽  
Cell Proliferation And Differentiation

The orderly development of the nervous system is characterized by phases of cell proliferation and differentiation, neural migration, axonal outgrowth and synapse formation, and stabilization. Each of these processes is a result of the modulation of genetic programs by extracellular cues. In particular, chondroitin sulfate proteoglycans (CSPGs) have been found to be involved in almost every aspect of this well-orchestrated yet delicate process. The evidence of their involvement is complex, often contradictory, and lacking in mechanistic clarity; however, it remains obvious that CSPGs are key cogs in building a functional brain. This review focuses on current knowledge of the role of CSPGs in each of the major stages of neural development with emphasis on areas requiring further investigation:

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