A diverse set of developmentally regulated proteoglycans is expressed in the rat central nervous system

Herndon, Mary E.; Lander, Arthur D.

doi:10.1016/0896-6273(90)90148-9

Cited by 243 publications

(179 citation statements)

References 63 publications

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“…CSPG core proteins have also been shown to be diverse on the basis of differences in molecular weight on SDS-PAGE (Oohira et al, 1988;Gowda et al, 1989;Herndon and Lander, 1990;Hockfield et al, 1990). The epitopes for antibodies Cat-301 and Cat-315 are most likely core protein and not carbohydrate, as indicated by the retention of immunoreactivity after enzymatic or chemical deglycosylation.…”

Section: Discussionmentioning

confidence: 99%

A Family of Activity-Dependent Neuronal Cell-Surface Chondroitin Sulfate Proteoglycans in Cat Visual Cortex

et al. 1997

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Monoclonal antibody Cat-301 recognizes a chondroitin sulfate proteoglycan (CSPG) expressed on the extracellular surface of cell bodies and proximal dendrites of specific subsets of neurons in many areas of the mammalian CNS, including the cat visual cortex. The Cat-301 CSPG is first detected at the close of the critical period in development, a period during which the pattern of neuronal activity determines the mature synaptic circuitry and neuronal phenotype. In the cat visual cortex, dark-rearing from birth prolongs the duration of the critical period and attenuates the expression of the Cat-301 antigen, implicating the Cat-301 CSPG in the cellular mechanisms that terminate the period of synaptic plasticity. Because the Cat-301 antigen is expressed on only a limited subset of neurons, we have further examined the molecular heterogeneity among neuronal cell-surface CSPGs and have asked (1) whether other neuronal subsets carry distinct CSPGs and (2) whether the activity-dependent expression of the Cat-301 CSPG is a property generalizable to related cell-surface CSPGs. Here, we report two new monoclonal antibodies, Cat-315 and Cat-316, which together with Cat-301 define a family of at least seven related yet distinct CSPGs. These three antibodies define nonidentical subsets of neurons in the cat visual cortex. The expression of normal levels of these CSPGs is reduced by darkrearing. Together, these data show that the family of cellsurface CSPGs is molecularly diverse, that different sets of neurons express distinct complements of cell-surface antigens, and that the regulation of CSPG expression by activity may be a general feature of neuronal cell-surface CSPGs.

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Section: Discussionmentioning

confidence: 99%

A Family of Activity-Dependent Neuronal Cell-Surface Chondroitin Sulfate Proteoglycans in Cat Visual Cortex

et al. 1997

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“…4 and 5). An unusually large number (>25) of different HSPGs (31) that are expressed in the nervous system have been implicated in many aspects of neural development, including neurogenesis, axon elongation and pathfinding, and synapse formation (32). Most notably, agrins identified in neuromuscular synapses have been demonstrated to mediate acetylcholine receptor clustering (33).…”

Section: Discussionmentioning

confidence: 99%

PTPσ functions as a presynaptic receptor for the glypican-4/LRRTM4 complex and is essential for excitatory synaptic transmission

Pramanik

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Leukocyte common antigen-related receptor protein tyrosine phosphatases-comprising LAR, PTPδ, and PTPσ-are synaptic adhesion molecules that organize synapse development. Here, we identify glypican 4 (GPC-4) as a ligand for PTPσ. GPC-4 showed strong (nanomolar) affinity and heparan sulfate (HS)-dependent interaction with the Ig domains of PTPσ. PTPσ bound only to proteolytically cleaved GPC-4 and formed additional complex with leucine-rich repeat transmembrane protein 4 (LRRTM4) in rat brains. Moreover, single knockdown (KD) of PTPσ, but not LAR, in cultured neurons significantly reduced the synaptogenic activity of LRRTM4, a postsynaptic ligand of GPC-4, in heterologous synapse-formation assays. Finally, PTPσ KD dramatically decreased both the frequency and amplitude of excitatory synaptic transmission. This effect was reversed by wild-type PTPσ, but not by a HS-binding-defective PTPσ mutant. Our results collectively suggest that presynaptic PTPσ, together with GPC-4, acts in a HS-dependent manner to maintain excitatory synapse development and function.PTPσ | glypican | LRRTM4 | synaptic cell adhesion | heparan sulfate

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“…The total proteoglycan fraction was isolated from soluble extracts of rat brain at various ages by a protocol using DEAESepharose chromatography and sequential washing steps, as described originally by Herndon and Lander (1990). Details of the protocol have been published previously (Yamada et al, 1994).…”

Section: Methodsmentioning

confidence: 99%

“…Key words: brevican; chondroitin sulfate proteoglycan; cerebellar development; glomerulus; astrocytes; neurite outgrowth A diverse array of proteoglycans is expressed in developing and adult brain (Herndon and Lander, 1990;Margolis and Margolis, 1993). Among these, the aggrecan family proteoglycans or "lecticans" (Ruoslahti, 1996) are especially diverse and abundant.…”

Section: The Burnham Institute La Jolla California 92037mentioning

confidence: 99%

The Brain Chondroitin Sulfate Proteoglycan Brevican Associates with Astrocytes Ensheathing Cerebellar Glomeruli and Inhibits Neurite Outgrowth from Granule Neurons

et al. 1997

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Brevican is a nervous system-specific chondroitin sulfate proteoglycan that belongs to the aggrecan family and is one of the most abundant chondroitin sulfate proteoglycans in adult brain. To gain insights into the role of brevican in brain development, we investigated its spatiotemporal expression, cell surface binding, and effects on neurite outgrowth, using rat cerebellar cortex as a model system. Immunoreactivity of brevican occurs predominantly in the protoplasmic islet in the internal granular layer after the third postnatal week. Immunoelectron microscopy revealed that brevican is localized in close association with the surface of astrocytes that form neuroglial sheaths of cerebellar glomeruli where incoming mossy fibers interact with dendrites and axons from resident neurons. In situ hybridization showed that brevican is synthesized by these astrocytes themselves. In primary cultures of cerebellar astrocytes, brevican is detected on the surface of these cells. Binding assays with exogenously added brevican revealed that primary astrocytes and several immortalized neural cell lines have cell surface binding sites for brevican core protein. These cell surface brevican binding sites recognize the C-terminal portion of the core protein and are independent of cell surface hyaluronan. These results indicate that brevican is synthesized by astrocytes and retained on their surface by an interaction involving its core protein. Purified brevican inhibits neurite outgrowth from cerebellar granule neurons in vitro, an activity that requires chondroitin sulfate chains. We suggest that brevican presented on the surface of neuroglial sheaths may be controlling the infiltration of axons and dendrites into maturing glomeruli.

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A diverse set of developmentally regulated proteoglycans is expressed in the rat central nervous system

Cited by 243 publications

References 63 publications

A Family of Activity-Dependent Neuronal Cell-Surface Chondroitin Sulfate Proteoglycans in Cat Visual Cortex

A Family of Activity-Dependent Neuronal Cell-Surface Chondroitin Sulfate Proteoglycans in Cat Visual Cortex

PTPσ functions as a presynaptic receptor for the glypican-4/LRRTM4 complex and is essential for excitatory synaptic transmission

The Brain Chondroitin Sulfate Proteoglycan Brevican Associates with Astrocytes Ensheathing Cerebellar Glomeruli and Inhibits Neurite Outgrowth from Granule Neurons

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