The Expression of Receptor Tyrosine Phosphatases Is Responsive to Sciatic Nerve Crush

Haworth, Kim E.; Shu, Kai Keen; Stokes, Alexander J.; Morris, Roger J.; Stoker, Andrew W.

doi:10.1006/mcne.1998.0707

Cited by 26 publications

(21 citation statements)

References 38 publications

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“…] with the previous observations of stable RPTPr expression in neuronal populations of retinal ganglion cells and facial motoneurons after nerve injury (Sapieha et al, 2005;Thompson et al, 2003). However, RPTPr expression was reported to increase in dorsal root ganglia and the sciatic nerve following injury, suggesting that various neuronal cell populations could be differently regulated (Haworth et al, 1998;McLean et al, 2002).…”

Section: Fig 4 Cst Axons In Rptprmentioning

confidence: 51%

Corticospinal tract regeneration after spinal cord injury in receptor protein tyrosine phosphatase sigma deficient mice

Fry

Chagnon

López-Vales

et al. 2009

Glia

138

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Receptor protein tyrosine phosphatase sigma (RPTPsigma) plays a role in inhibiting axon growth during development. It has also been shown to slow axon regeneration after peripheral nerve injury and inhibit axon regeneration in the optic nerve. Here, we assessed the ability of the corticospinal tract (CST) axons to regenerate after spinal hemisection and contusion injury in RPTPsigma deficient (RPTPsigma(-/-)) mice. We show that damaged CST fibers in RPTPsigma(-/-) mice regenerate and appear to extend for long distances after a dorsal hemisection or contusion injury of the thoracic spinal cord. In contrast, no long distance axon regeneration of CST fibers is seen after similar lesions in wild-type mice. In vitro experiments indicate that cerebellar granule neurons from RPTPsigma(-/-) mice have reduced sensitivity to the inhibitory effects of chondroitin sulfate proteoglycan (CSPG) substrate, but not myelin, which may contribute to the growth of CST axons across the CSPG-rich glial scar. Our data suggest that RPTPsigma may function to prevent axonal growth after injury in the adult mammalian spinal cord and could be a target for promoting long distance regeneration after spinal cord injury.

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Section: Fig 4 Cst Axons In Rptprmentioning

confidence: 51%

Corticospinal tract regeneration after spinal cord injury in receptor protein tyrosine phosphatase sigma deficient mice

Fry

Chagnon

López-Vales

et al. 2009

Glia

138

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“…Cell adhesion molecule-like RPTPs are emerging as a major class of molecules involved in regulating neural development, including axon growth and guidance, synaptic function, and nerve repair (41,78,84; also reviewed in references 6, 55, 72, and 79). Currently, little is understood regarding the molecular mechanisms of RPTP signaling, one reason being that in only a few cases are their interaction partners known.…”

Section: Discussionmentioning

confidence: 99%

Heparan Sulfate Proteoglycans Are Ligands for Receptor Protein Tyrosine Phosphatase σ

Aricescu¹,

McKinnell²,

Halfter

et al. 2002

Molecular and Cellular Biology

189

180

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RPTP is a cell adhesion molecule-like receptor protein tyrosine phosphatase involved in nervous system development. Its avian orthologue, known as cPTP or CRYP␣, promotes intraretinal axon growth and controls the morphology of growth cones. The molecular mechanisms underlying the functions of cPTP are still to be determined, since neither its physiological ligand(s) nor its substrates have been described. Nevertheless, a major class of ligand(s) is present in the retinal basal lamina and glial endfeet, the potent native growth substrate for retinal axons. We demonstrate here that cPTP is a heparin-binding protein and that its basal lamina ligands include the heparan sulfate proteoglycans (HSPGs) agrin and collagen XVIII. These molecules interact with high affinity with cPTP in vitro, and this binding is totally dependent upon their heparan sulfate chains. Using molecular modelling and site-directed mutagenesis, a binding site for heparin and heparan sulfate was identified in the first immunoglobulin-like domain of cPTP. HSPGs are therefore a novel class of heterotypic ligand for cPTP, suggesting that cPTP signaling in axons and growth cones is directly responsive to matrix-associated cues.The complex pattern of neural connectivity established during nervous system development relies on the ability of the axon's motile tip, the growth cone, to receive, transduce, and integrate multiple environmental signals. Protein phosphorylation on tyrosine residues plays a key role in these processes (21, 29). Two major families of enzymes, the protein tyrosine kinases and the protein tyrosine phosphatases (PTPs), control cellular phosphotyrosine levels. These enzymes are found in both cytoplasmic and transmembrane (receptor-like) forms, and the biochemical interactions between them lead to a diversity of cellular behaviors (25,76).Receptor protein tyrosine phosphatases (RPTPs) have recently joined the list of molecules involved in neural development and in particular in axon growth and guidance (reviewed in references 6, 68, 72, and 79). Type 2 RPTPs, containing cell adhesion molecule (CAM)-like extracellular regions, may be particularly well equipped to trigger signals involving cell-cell or cell-extracellular matrix contacts (68). Recent experiments with Drosophila have demonstrated the involvement of the RPTPs DLAR and DPTP69D in motor (19, 20, 50), retinal (27, 57), and midline (73) axon guidance. In leech, a LAR generelated RPTP (HmLAR2) is implicated in Comb cell behavior, specifically in process outgrowth and mutual avoidance by sibling growth cones (2, 28). Several vertebrate RPTPs have been shown to promote neurite outgrowth in cell culture, including cPTP (51), RPTP (23), RPTP (10), and RPTP␦ (82). Moreover, it has recently been shown that RPTP␦ also has a potential guidance function, at least in vitro (74).In mice, gene deficiencies in type 2 RPTPs lead to various abnormalities. LAR deficiency leads to a reduction in size of basal forebrain cholinergic neurons, diminished hippocampal innervation, and defects in o...

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“…For instance, RPTP␣ and LAR are both expressed in mouse dorsal root ganglia (35-37). Furthermore, both LAR and RPTP␣ have been shown, albeit in different studies, to localize to the growth cone of growing neurons (36,38,39). From Drosophila work, it is clear that different RPTPs cooperate in a fashion that is still unclear (40).…”

Section: Table II Binding Of Rptp␣-d2 To the Juxtamembrane Domain Of mentioning

confidence: 99%

Multiple Interactions between Receptor Protein-tyrosine Phosphatase (RPTP) α and Membrane-distal Protein-tyrosine Phosphatase Domains of Various RPTPs

Blanchetot

Hertog

2000

Journal of Biological Chemistry

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Receptor protein-tyrosine phosphatase (RPTP) ␣ belongs to the large family of receptor protein-tyrosine phosphatases containing two tandem phosphatase domains. Most of the catalytic activity is retained in the first, membrane-proximal domain (RPTP␣-D1), and little is known about the function of the second, membrane-distal domain (RPTP␣-D2). We investigated whether proteins bound to RPTP␣ using the two-hybrid system and found that the second domain of RPTP interacted with the juxtamembrane domain of RPTP␣. We confirmed this interaction by co-immunoprecipitation experiments. Furthermore, RPTP␣ not only interacted with RPTP-D2 but also with RPTP␣-D2, LAR-D2, RPTP␦-D2, and RPTP-D2, members of various RPTP subfamilies, although with different affinities. In the yeast two-hybrid system and in glutathione S-transferase pull-down assays, we show that the RPTP-D2s interacted directly with the wedge structure of RPTP␣-D1 that has been demonstrated to be involved in inactivation of the RPTP␣-D1/RPTP␣-D1 homodimer. The interaction was specific because the equivalent wedge structure in LAR was unable to interact with RPTP␣-D2 or LAR-D2. In vivo, we show that other interaction sites exist as well, including the C terminus of RPTP␣-D2. The observation that RPTP␣, but not LAR, bound to multiple RPTP-D2s with varying affinities suggests a specific mechanism of cross-talk between RPTPs that may regulate their biological function.Protein-tyrosine phosphorylation is a major mechanism of intracellular signaling within superior eukaryotic organisms that has been demonstrated to be involved in a large set of cellular events like migration, proliferation, differentiation, and transformation. Protein-tyrosine phosphatases (PTPs) 1 regulate the level of phosphotyrosine in cellular proteins issued from the action of protein-tyrosine kinase. The PTP family is composed of more than 100 different known members, but this number is constantly growing, and the last estimation is that there are 500 PTPs (1). The PTP group is subdivided in two between the cytosolic and the receptor protein-tyrosine phosphatases (RPTP). The RPTPs are distinguished by their extracellular domains, which can be very large, containing domains such as fibronectin type III-like domains and Immunoglobulinlike repeats in the case of for instance LAR, or very short (e.g. RPTP⑀) and heavily glycosylated such as RPTP␣ (2, 3).RPTP␣ is a widely but dynamically expressed RPTP that dephosphorylates Tyr 527 of c-Src in vitro and that increases c-Src kinase activity when overexpressed in vivo (4, 5). Furthermore, cells derived from RPTP␣ knock-out mice have reduced Src and Fyn activity, indicating that RPTP␣ activates Fyn as well as Src in vivo (6, 7). RPTP␣ is also involved in m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity. Presumably, RPTP␣ directly dephosphorylates Kv1.2, leading to desuppression of its K ϩ channel activity (8).RPTP␣ is itself phosphorylated on Tyr 789 , a GRB2-SH2 consensus binding site. Both the SH2 and the C-terminal SH3 ...

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The Expression of Receptor Tyrosine Phosphatases Is Responsive to Sciatic Nerve Crush

Cited by 26 publications

References 38 publications

Corticospinal tract regeneration after spinal cord injury in receptor protein tyrosine phosphatase sigma deficient mice

Corticospinal tract regeneration after spinal cord injury in receptor protein tyrosine phosphatase sigma deficient mice

Heparan Sulfate Proteoglycans Are Ligands for Receptor Protein Tyrosine Phosphatase σ

Multiple Interactions between Receptor Protein-tyrosine Phosphatase (RPTP) α and Membrane-distal Protein-tyrosine Phosphatase Domains of Various RPTPs

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