Functional difference of receptor-type protein tyrosine phosphatase ζ/β isoforms in neurogenesis of hippocampal neurons

Asai, Hitomi; Yokoyama, Seisuke; Morita, Shoko; Maeda, Nobuaki; Miyata, Seiji

doi:10.1016/j.neuroscience.2009.09.012

Cited by 13 publications

(12 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Images of the neurons immunostained with anti‐GAP‐43, anti‐synapsin and anti‐synaptotagmin antibody were collected with the 63× objective thresholded to outline presynaptic terminals correspondingly. The immunofluorescence area and intensity of GAP‐43, synapsin and synaptotagmin were measured using WinRoof, an image analyzing system (Mitani Corporation, Fukui, Japan), in which threshold intensity was set to include for measurements only immunoreactive profile by visual inspection and kept constant . All images analysis was performed such that the experimenter was blind to the stage.…”

Section: Methodsmentioning

confidence: 99%

“…The quantitative analysis revealed the relationship between GAP- 43 Figure 6A). At 14 DIV, however, the percentage of puncta having strong GAP-43 and weak synapsin immunoreactivity decreased to 56.6%, and vice versa the percentage of puncta having weak GAP-43 and strong synapsin immunoreactivity increased to 43.4% from 4.1%, respectively ( Figure 6B).…”

Section: Correlation Between Gap-43 and Synaptic Vesicle-associated Pmentioning

confidence: 99%

See 1 more Smart Citation

Synaptic localization of growth‐associated protein 43 in cultured hippocampal neurons during synaptogenesis

Morita

Miyata

2012

Cell Biochemistry & Function

View full text Add to dashboard Cite

Growth-associated protein 43 (GAP-43), a novel axonal phosphoprotein, is originally identified as a growth-cone-specific protein of developing neurons in vitro. The expression of GAP-43 is also shown to be up-regulated concomitant with increased synaptic plasticity in the brains in vivo, but how GAP-43 is concerned with synaptic plasticity is not well understood. In the present study, therefore, we aimed to elucidate subcellular localization of GAP-43 as culture development of rat hippocampal neurons. Western blotting showed that the expression of GAP-43 in the cerebral and hippocampal tissues was prominently high at postnatal days 14 and 21 or the active period of synaptogenesis. Double-labelling immunohistochemistry with an axonal marker Tau revealed that the immunoreactivity of GAP-43 was seen throughout axons of cultured hippocampal neurons but stronger at axonal puncta of developing neurons than axonal processes. Double-labelling immunohistochemistry with presynaptic terminal markers of synapsin and synaptotagmin revealed that the immunoreactivity of GAP-43 was observed mostly at weak synapsin- and synaptotagmin-positive puncta rather than strong ones. The quantitative analysis of immunofluorescent intensity showed a clear inverse correlation between GAP-43 and either synapsin or synaptotagmin expression. These data indicate that GAP-43 is highly expressed at immature growing axonal terminals and its expression is decreased along with the maturation of synaptogenesis.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Correlation Between Gap-43 and Synaptic Vesicle-associated Pmentioning

confidence: 99%

Synaptic localization of growth‐associated protein 43 in cultured hippocampal neurons during synaptogenesis

Morita

Miyata

2012

Cell Biochemistry & Function

View full text Add to dashboard Cite

show abstract

“…PTN is a phosphacan ligand and its binding is influenced by the sulfation pattern of the GAG side chains of phosphacan (Maeda et al 2003). Signaling of pleiotrophin through RPTP-f is involved in the activation of oligodendrocyte progenitor cells (Kuboyama et al 2016) and oligodendrocyte differentiation (Asai et al 2009) and regulates the morphogenesis of Purkinje cell dendrites in the developing cerebellum and hippocampus (Asai et al 2009). Contactin-1 binds CS-E and this promotes axonal outgrowth (Mikami et al 2009;Nakanishi et al 2012).…”

Section: Retinofugal Axonal Extension Provides Regulatory Clues Over mentioning

confidence: 99%

Keratan sulfate (KS)‐proteoglycans and neuronal regulation in health and disease: the importance ofKS‐glycodynamics and interactive capability with neuroregulatory ligands

Melrose

2019

Journal of Neurochemistry

View full text Add to dashboard Cite

Compared to the other classes of glycosaminoglycans (GAGs), that is, chondroitin/dermatan sulfate, heparin/heparan sulfate and hyaluronan, keratan sulfate (KS), have the least known of its interactive properties. In the human body, the cornea and the brain are the two most abundant tissue sources of KS. Embryonic KS is synthesized as a linear poly‐N‐acetyllactosamine chain of d‐galactose‐GlcNAc repeat disaccharides which become progressively sulfated with development, sulfation of GlcNAc is more predominant than galactose. KS contains multi‐sulfated high‐charge density, monosulfated and non‐sulfated poly‐N‐acetyllactosamine regions and thus is a heterogeneous molecule in terms of chain length and charge distribution. A recent proteomics study on corneal KS demonstrated its interactivity with members of the Slit‐Robbo and Ephrin‐Ephrin receptor families and proteins which regulate Rho GTPase signaling and actin polymerization/depolymerization in neural development and differentiation. KS decorates a number of peripheral nervous system/CNS proteoglycan (PG) core proteins. The astrocyte KS‐PG abakan defines functional margins of the brain and is up‐regulated following trauma. The chondroitin sulfate/KS PG aggrecan forms perineuronal nets which are dynamic neuroprotective structures with anti‐oxidant properties and roles in neural differentiation, development and synaptic plasticity. Brain phosphacan a chondroitin sulfate, KS, HNK‐1 PG have roles in neural development and repair. The intracellular microtubule and synaptic vesicle KS‐PGs MAP1B and SV2 have roles in metabolite transport, storage, and export of neurotransmitters and cytoskeletal assembly. MAP1B has binding sites for tubulin and actin through which it promotes cytoskeletal development in growth cones and is highly expressed during neurite extension. The interactive capability of KS with neuroregulatory ligands indicate varied roles for KS‐PGs in development and regenerative neural processes.

show abstract

“…They are functionally different, and the full‐length form appears to mediate the action of PTN in hippocampal neurons. PTN increases the density of hippocampal dendritic synapses, and overexpression of the full‐length form decreases the density (Asai et al ., ). This observation is consistent with the action mechanism of PTPζ described above.…”

Section: Mk Signallingmentioning

confidence: 97%

Structure and function of midkine as the basis of its pharmacological effects

Muramatsu

2014

British J Pharmacology

106

View full text Add to dashboard Cite

Midkine (MK) is a heparin-binding growth factor or cytokine and forms a small protein family, the other member of which is pleiotrophin. MK enhances survival, migration, cytokine expression, differentiation and other activities of target cells. MK is involved in various physiological processes, such as development, reproduction and repair, and also plays important roles in the pathogenesis of inflammatory and malignant diseases. MK is largely composed of two domains, namely a more N-terminally located N-domain and a more C-terminally located C-domain. Both domains are basically composed of three antiparallel β-sheets. In addition, there are short tails in the N-terminal and C-terminal sides and a hinge connecting the two domains. Several membrane proteins have been identified as MK receptors: receptor protein tyrosine phosphatase Z1 (PTPζ), low-density lipoprotein receptor-related protein, integrins, neuroglycan C, anaplastic lymphoma kinase and Notch-2. Among them, the most established one is PTPζ. It is a transmembrane tyrosine phophatase with chondroitin sulfate, which is essential for high-affinity binding with MK. PI3K and MAPK play important roles in the downstream signalling system of MK, while transcription factors affected by MK signalling include NF-κB, Hes-1 and STATs. Because of the involvement of MK in various physiological and pathological processes, MK itself as well as pharmaceuticals targeting MK and its signalling system are expected to be valuable for the treatment of numerous diseases. LINKED ARTICLESThis article is part of a themed section on Midkine. To view the other articles in this section visit http://dx.doi.org/10.1111/bph.2014.171.issue-4 Abbreviations ALK, anaplastic lymphoma kinase; Hes-1, hairy and enhancer of split-1; HIF, hypoxia-induced factor; LRP, low-density lipoprotein receptor-related protein; Mdka, Midkine-a; Mdkb, Midkine-b; MK, midkine; PTN, pleiotrophin; PTPζ, receptor protein tyrosine phosphatase Z1

show abstract

Functional difference of receptor-type protein tyrosine phosphatase ζ/β isoforms in neurogenesis of hippocampal neurons

Cited by 13 publications

References 47 publications

Synaptic localization of growth‐associated protein 43 in cultured hippocampal neurons during synaptogenesis

Synaptic localization of growth‐associated protein 43 in cultured hippocampal neurons during synaptogenesis

Keratan sulfate (KS)‐proteoglycans and neuronal regulation in health and disease: the importance ofKS‐glycodynamics and interactive capability with neuroregulatory ligands

Structure and function of midkine as the basis of its pharmacological effects

Contact Info

Product

Resources

About