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1.
Cells ; 9(9)2020 09 09.
Article in English | MEDLINE | ID: mdl-32917016

ABSTRACT

Annexin A2 (AnxA2) is a calcium- and lipid-binding protein involved in neuroendocrine secretion where it participates in the formation and/or stabilization of lipid micro-domains required for structural and spatial organization of the exocytotic machinery. We have recently described that phosphorylation of AnxA2 on Tyr23 is critical for exocytosis. Considering that Tyr23 phosphorylation is known to promote AnxA2 externalization to the outer face of the plasma membrane in different cell types, we examined whether this phenomenon occurred in neurosecretory chromaffin cells. Using immunolabeling and biochemical approaches, we observed that nicotine stimulation triggered the egress of AnxA2 to the external leaflets of the plasma membrane in the vicinity of exocytotic sites. AnxA2 was found co-localized with tissue plasminogen activator, previously described on the surface of chromaffin cells following secretory granule release. We propose that AnxA2 might be a cell surface tissue plasminogen activator receptor for chromaffin cells, thus playing a role in autocrine or paracrine regulation of exocytosis.


Subject(s)
Annexin A2/metabolism , Calcium/metabolism , Exocytosis/physiology , Neuroendocrine Cells/metabolism , Humans
2.
Endocr Relat Cancer ; 23(4): 281-93, 2016 Apr.
Article in English | MEDLINE | ID: mdl-26911374

ABSTRACT

Among small GTPases from the Rho family, Cdc42, RAC, and Rho are well known to mediate a large variety of cellular processes linked with cancer biology through their ability to cycle between an inactive (GDP-bound) and an active (GTP-bound) state. Guanine nucleotide exchange factors (GEFs) stimulate the exchange of GDP for GTP to generate the activated form, whereas the GTPase-activating proteins (GAPs) catalyze GTP hydrolysis, leading to the inactivated form. Modulation of Rho GTPase activity following altered expression of RHO-GEFs and/or RHO-GAPs has already been reported in various human tumors. However, nothing is known about the Rho GTPase activity or the expression of their regulators in human pheochromocytomas, a neuroendocrine tumor (NET) arising from chromaffin cells of the adrenal medulla. In this study, we demonstrate, through an ELISA-based activity assay, that Rac1 and Cdc42 activities decrease in human pheochromocytomas (PCCs) compared with the matched adjacent non-tumor tissue. Furthermore, through quantitative mass spectrometry (MS) approaches, we show that the expression of two RHO-GEF proteins, namely ARHGEF1 and FARP1, is significantly reduced in tumors compared with matched non-tumor tissue, whereas ARHGAP36 expression is increased. Moreover, siRNA-based knockdown of ARHGEF1 and FARP1 in PC12 cells leads to a significant inhibition of Rac1 and Cdc42 activities, respectively. Finally, a principal component analysis (PCA) of our dataset was able to discriminate PCC from non-tumor tissue and indicates a close correlation between Cdc42/Rac1 activity and FARP1/ARHGEF1 expression. Altogether, our findings reveal for the first time the importance of modulation of Rho GTPase activities and expression of their regulators in human PCCs.


Subject(s)
Adrenal Gland Neoplasms/metabolism , Pheochromocytoma/metabolism , Rho Guanine Nucleotide Exchange Factors/metabolism , cdc42 GTP-Binding Protein/metabolism , rac1 GTP-Binding Protein/metabolism , Animals , Humans , PC12 Cells , RNA, Small Interfering/genetics , Rats , Rho Guanine Nucleotide Exchange Factors/genetics
3.
J Neurosci ; 35(31): 11045-55, 2015 Aug 05.
Article in English | MEDLINE | ID: mdl-26245966

ABSTRACT

Oligophrenin-1 (OPHN1) is a protein with multiple domains including a Rho family GTPase-activating (Rho-GAP) domain, and a Bin-Amphiphysin-Rvs (BAR) domain. Involved in X-linked intellectual disability, OPHN1 has been reported to control several synaptic functions, including synaptic plasticity, synaptic vesicle trafficking, and endocytosis. In neuroendocrine cells, hormones and neuropeptides stored in large dense core vesicles (secretory granules) are released through calcium-regulated exocytosis, a process that is tightly coupled to compensatory endocytosis, allowing secretory granule recycling. We show here that OPHN1 is expressed and mainly localized at the plasma membrane and in the cytosol in chromaffin cells from adrenal medulla. Using carbon fiber amperometry, we found that exocytosis is impaired at the late stage of membrane fusion in Ophn1 knock-out mice and OPHN1-silenced bovine chromaffin cells. Experiments performed with ectopically expressed OPHN1 mutants indicate that OPHN1 requires its Rho-GAP domain to control fusion pore dynamics. On the other hand, compensatory endocytosis assessed by measuring dopamine-ß-hydroxylase (secretory granule membrane) internalization is severely inhibited in Ophn1 knock-out chromaffin cells. This inhibitory effect is mimicked by the expression of a truncated OPHN1 mutant lacking the BAR domain, demonstrating that the BAR domain implicates OPHN1 in granule membrane recapture after exocytosis. These findings reveal for the first time that OPHN1 is a bifunctional protein that is able, through distinct mechanisms, to regulate and most likely link exocytosis to compensatory endocytosis in chromaffin cells.


Subject(s)
Chromaffin Cells/metabolism , Cytoskeletal Proteins/metabolism , Endocytosis/physiology , Exocytosis/physiology , GTPase-Activating Proteins/metabolism , Membrane Fusion/physiology , Nuclear Proteins/metabolism , Animals , Cattle , Cell Membrane/metabolism , Mice , Mice, Knockout , Synaptic Vesicles/metabolism
4.
PLoS One ; 8(8): e70638, 2013.
Article in English | MEDLINE | ID: mdl-23940613

ABSTRACT

Over the past years, dynamin has been implicated in tuning the amount and nature of transmitter released during exocytosis. However, the mechanism involved remains poorly understood. Here, using bovine adrenal chromaffin cells, we investigated whether this mechanism rely on dynamin's ability to remodel actin cytoskeleton. According to this idea, inhibition of dynamin GTPase activity suppressed the calcium-dependent de novo cortical actin and altered the cortical actin network. Similarly, expression of a small interfering RNA directed against dynamin-2, an isoform highly expressed in chromaffin cells, changed the cortical actin network pattern. Disruption of dynamin-2 function, as well as the pharmacological inhibition of actin polymerization with cytochalasine-D, slowed down fusion pore expansion and increased the quantal size of individual exocytotic events. The effects of cytochalasine-D and dynamin-2 disruption were not additive indicating that dynamin-2 and F-actin regulate the late steps of exocytosis by a common mechanism. Together our data support a model in which dynamin-2 directs actin polymerization at the exocytosis site where both, in concert, adjust the hormone quantal release to efficiently respond to physiological demands.


Subject(s)
Actin Cytoskeleton/metabolism , Actins/metabolism , Chromaffin Cells/metabolism , Dynamin II/physiology , Animals , Catecholamines/metabolism , Cattle , Cells, Cultured , Exocytosis , Gene Expression , Membrane Fusion , Protein Multimerization , Secretory Vesicles/metabolism
5.
J Neurosci ; 33(8): 3545-56, 2013 Feb 20.
Article in English | MEDLINE | ID: mdl-23426682

ABSTRACT

Calcium-regulated exocytosis in neuroendocrine cells and neurons is accompanied by the redistribution of phosphatidylserine (PS) to the extracellular space, leading to a disruption of plasma membrane asymmetry. How and why outward translocation of PS occurs during secretion are currently unknown. Immunogold labeling on plasma membrane sheets coupled with hierarchical clustering analysis demonstrate that PS translocation occurs at the vicinity of the secretory granule fusion sites. We found that altering the function of the phospholipid scramblase-1 (PLSCR-1) by expressing a PLSCR-1 calcium-insensitive mutant or by using chromaffin cells from PLSCR-1⁻/⁻ mice prevents outward translocation of PS in cells stimulated for exocytosis. Remarkably, whereas transmitter release was not affected, secretory granule membrane recapture after exocytosis was impaired, indicating that PLSCR-1 is required for compensatory endocytosis but not for exocytosis. Our results provide the first evidence for a role of specific lipid reorganization and calcium-dependent PLSCR-1 activity in neuroendocrine compensatory endocytosis.


Subject(s)
Chromaffin Cells/metabolism , Endocytosis/physiology , Neuroendocrine Cells/metabolism , Phosphatidylserines/metabolism , Phospholipid Transfer Proteins/metabolism , Animals , Biological Transport, Active/physiology , Cattle , Cell Membrane/metabolism , Chromaffin Cells/enzymology , Exocytosis/physiology , Female , Lipid Metabolism/physiology , Male , Mice , Mice, Transgenic , Neuroendocrine Cells/enzymology , PC12 Cells , Rats
6.
J Neurochem ; 117(4): 623-31, 2011 May.
Article in English | MEDLINE | ID: mdl-21392006

ABSTRACT

Rho GTPases are small GTP binding proteins belonging to the Ras superfamily which act as molecular switches that regulate many cellular function including cell morphology, cell to cell interaction, cell migration and adhesion. In neuronal cells, Rho GTPases have been proposed to regulate neuronal development and synaptic plasticity. However, the role of Rho GTPases in neurosecretion is poorly documented. In this review, we discuss data that highlight the importance of Rho GTPases and their regulators into the control of neurotransmitter and hormone release in neurons and neuroendocrine cells, respectively.


Subject(s)
Neurosecretion/physiology , rho GTP-Binding Proteins/physiology , Animals , Chromaffin System/physiology , Humans , Neurotransmitter Agents/metabolism , Neurotransmitter Agents/physiology , PC12 Cells , Rats , Synaptic Transmission/physiology
7.
Traffic ; 12(1): 72-88, 2011 Jan.
Article in English | MEDLINE | ID: mdl-20880191

ABSTRACT

In secretory cells, calcium-regulated exocytosis is rapidly followed by compensatory endocytosis. Neuroendocrine cells secrete hormones and neuropeptides through various modes of exo-endocytosis, including kiss-and-run, cavicapture and full-collapse fusion. During kiss-and-run and cavicapture modes, the granule membrane is maintained in an omega shape, whereas it completely merges with the plasma membrane during full-collapse mode. As the composition of the granule membrane is very different from that of the plasma membrane, a precise sorting process of granular proteins must occur. However, the fate of secretory granule membrane after full fusion exocytosis remains uncertain. Here, we investigated the mechanisms governing endocytosis of collapsed granule membranes by following internalization of antibodies labeling the granule membrane protein, dopamine-ß-hydroxylase (DBH) in cultured chromaffin cells. Using immunofluorescence and electron microscopy, we observed that after full collapse, DBH remains clustered on the plasma membrane with other specific granule markers and is subsequently internalized through vesicular structures composed mainly of granule components. Moreover, the incorporation of this recaptured granule membrane into an early endosomal compartment is dependent on clathrin and actin. Altogether, these results suggest that after full collapse exocytosis, a selective sorting of granule membrane components is facilitated by the physical preservation of the granule membrane entity on the plasma membrane.


Subject(s)
Cell Membrane/metabolism , Chromaffin Cells/physiology , Exocytosis , Neuroendocrine Cells/metabolism , Secretory Vesicles , Actins/metabolism , Animals , Cattle , Clathrin/metabolism , Humans , Secretory Vesicles/physiology
8.
Traffic ; 11(7): 958-71, 2010 Jul 01.
Article in English | MEDLINE | ID: mdl-20374557

ABSTRACT

In neuroendocrine cells, annexin-A2 is implicated as a promoter of monosialotetrahexosylganglioside (GM1)-containing lipid microdomains that are required for calcium-regulated exocytosis. As soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) require a specific lipid environment to mediate granule docking and fusion, we investigated whether annexin-A2-induced lipid microdomains might be linked to the SNAREs present at the plasma membrane. Stimulation of adrenergic chromaffin cells induces the translocation of cytosolic annexin-A2 to the plasma membrane, where it colocalizes with SNAP-25 and S100A10. Cross-linking experiments performed in stimulated chromaffin cells indicate that annexin-A2 directly interacts with S100A10 to form a tetramer at the plasma membrane. Here, we demonstrate that S100A10 can interact with vesicle-associated membrane protein 2 (VAMP2) and show that VAMP2 is present at the plasma membrane in resting adrenergic chromaffin cells. Tetanus toxin that cleaves VAMP2 solubilizes S100A10 from the plasma membrane and inhibits the translocation of annexin-A2 to the plasma membrane. Immunogold labelling of plasma membrane sheets combined with spatial point pattern analysis confirmed that S100A10 is present in VAMP2 microdomains at the plasma membrane and that annexin-A2 is observed close to S100A10 and to syntaxin in stimulated chromaffin cells. In addition, these results showed that the formation of phosphatidylinositol (4,5)-bisphosphate (PIP(2)) microdomains colocalized with S100A10 in the vicinity of docked granules, suggesting a functional interplay between annexin-A2-mediated lipid microdomains and SNAREs during exocytosis.


Subject(s)
Annexin A2/physiology , Chromaffin Cells/metabolism , Exocytosis/physiology , SNARE Proteins/metabolism , Adrenergic Agents/metabolism , Annexin A2/metabolism , Annexin A2/ultrastructure , Cell Membrane/metabolism , Cell Membrane/ultrastructure , Cytoplasmic Granules/metabolism , Humans , Protein Transport , Qa-SNARE Proteins/metabolism , Qa-SNARE Proteins/ultrastructure , S100 Proteins/metabolism , S100 Proteins/ultrastructure , Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins/metabolism , Vesicle-Associated Membrane Protein 2/metabolism , Vesicle-Associated Membrane Protein 2/ultrastructure
9.
J Cell Sci ; 122(Pt 6): 798-806, 2009 Mar 15.
Article in English | MEDLINE | ID: mdl-19261846

ABSTRACT

Rho GTPases are crucial regulators of actin cytoskeletal rearrangements and play important roles in many cell functions linked to membrane trafficking processes. In neuroendocrine cells, we have previously demonstrated that RhoA and Cdc42 mediate part of the actin remodelling and vesicular trafficking events that are required for the release of hormones by exocytosis. Here, we investigate the functional importance of Rac1 for the exocytotic reaction and dissect the downstream and upstream molecular events that might integrate it to the exocytotic machinery. Using PC12 cells, we found that Rac1 is associated with the plasma membrane and is activated during exocytosis. Silencing of Rac1 by siRNA inhibits hormone release, prevents secretagogue (high K(+))-evoked phospholipase D1 (PLD1) activation and blocks the formation of phosphatidic acid at the plasma membrane. We identify betaPix as the guanine nucleotide-exchange factor integrating Rac1 activation to PLD1 and the exocytotic process. Finally, we show that the presence of the scaffolding protein Scrib at the plasma membrane is essential for betaPix/Rac1-mediated PLD1 activation and exocytosis. As PLD1 has recently emerged as a promoter of membrane fusion in various exocytotic events, our results define a novel molecular pathway linking a Rho GTPase, Rac1, to the final stages of Ca(2+)-regulated exocytosis in neuroendocrine cells.


Subject(s)
Exocytosis , Guanine Nucleotide Exchange Factors/metabolism , Neuroendocrine Cells/cytology , Neuroendocrine Cells/enzymology , Phospholipase D/metabolism , rac1 GTP-Binding Protein/metabolism , Animals , Biocatalysis/drug effects , Calcium/pharmacology , Cell Membrane/drug effects , Cell Membrane/enzymology , Enzyme Activation/drug effects , Exocytosis/drug effects , Growth Hormone/metabolism , Humans , Intracellular Signaling Peptides and Proteins/metabolism , Neuroendocrine Cells/drug effects , PC12 Cells , Phosphatidic Acids/metabolism , Protein Transport/drug effects , RNA Interference/drug effects , RNA, Small Interfering/metabolism , Rats , Rho Guanine Nucleotide Exchange Factors
10.
Ann N Y Acad Sci ; 1152: 209-14, 2009 Jan.
Article in English | MEDLINE | ID: mdl-19161392

ABSTRACT

Actin cytoskeleton remodeling is a critical step of regulated exocytosis in many secretory cell types, including neuroendocrine cells. While the classical model considers the cortical actin network as a physical barrier preventing the uncontrolled recruitment of secretory granules to the plasma membrane docking sites, recent evidence supports the idea that actin polymerization also plays a more active role in the late stages of exocytosis. However, the molecular machinery underlying this positive function of actin in the course of exocytosis remains largely unknown. Here, we propose that the neuronal guanine nucleotide exchange factor, intersectin-1L, activates the GTPase Cdc42, which in turn provides de novo actin filaments that are important for calcium-regulated exocytosis in PC12 cells.


Subject(s)
Actins/metabolism , Adaptor Proteins, Vesicular Transport/metabolism , Calcium/metabolism , Exocytosis , Neuroendocrine Cells/metabolism , cdc42 GTP-Binding Protein/metabolism , Adaptor Proteins, Vesicular Transport/genetics , Animals , Enzyme Activation , PC12 Cells , Rats
11.
Mol Cell Neurosci ; 36(1): 71-85, 2007 Sep.
Article in English | MEDLINE | ID: mdl-17689979

ABSTRACT

A unique and unresolved property of the central nervous system is that its extracellular matrix lacks fibrillar elements. In the present report, we show that astrocytes secrete triple helices of fibrillar collagens type I, III and V in culture, while no astroglial collagen expression could be detected in vivo. We discovered two inhibitory mechanisms that could underlie this apparent discrepancy. Thus, we uncover a strong inhibitory effect of meningeal cells on astrocytic collagen expression in coculture assays. Furthermore, we present evidence that EGF-receptor activation downregulates collagen expression in astrocytes via an autocrine loop. These investigations provide a rational framework to explain why the brain is devoid of collagen fibers, which is a unique feature that characterizes the structure of the neural extracellular matrix. Moreover, fibrillar collagens were found transiently upregulated in a laser-induced cortical lesion, suggesting that these could contribute to the glial scar that inhibits axonal regeneration.


Subject(s)
Astrocytes/drug effects , Autocrine Communication/physiology , Epidermal Growth Factor/pharmacology , Fibrillar Collagens/metabolism , Gene Expression Regulation/drug effects , Meninges/cytology , Animals , Animals, Newborn , Astrocytes/metabolism , Astrocytes/radiation effects , Cells, Cultured , Cerebral Cortex/cytology , Coculture Techniques/methods , Culture Media, Conditioned/pharmacology , Cytokines/pharmacology , Gene Expression Regulation/physiology , Lasers/adverse effects , RNA, Messenger/biosynthesis , Rats , Reverse Transcriptase Polymerase Chain Reaction , Tyrphostins/pharmacology
12.
EMBO J ; 25(15): 3494-503, 2006 Aug 09.
Article in English | MEDLINE | ID: mdl-16874303

ABSTRACT

Rho GTPases are key regulators of the actin cytoskeleton in membrane trafficking events. We previously reported that Cdc42 facilitates exocytosis in neuroendocrine cells by stimulating actin assembly at docking sites for secretory granules. These findings raise the question of the mechanism activating Cdc42 in exocytosis. The neuronal guanine nucleotide exchange factor, intersectin-1L, which specifically activates Cdc42 and is at an interface between membrane trafficking and actin dynamics, appears as an ideal candidate to fulfill this function. Using PC12 and chromaffin cells, we now show the presence of intersectin-1 at exocytotic sites. Moreover, through an RNA interference strategy coupled with expression of various constructs encoding the guanine nucleotide exchange domain, we demonstrate that intersectin-1L is an essential component of the exocytotic machinery. Silencing of intersectin-1 prevents secretagogue-induced activation of Cdc42 revealing intersectin-1L as the factor integrating Cdc42 activation to the exocytotic pathway. Our results extend the current role of intersectin-1L in endocytosis to a function in exocytosis and support the idea that intersectin-1L is an adaptor that coordinates exo-endocytotic membrane trafficking in secretory cells.


Subject(s)
Adaptor Proteins, Vesicular Transport/metabolism , Exocytosis , Guanine Nucleotide Exchange Factors/metabolism , Secretory Vesicles/metabolism , cdc42 GTP-Binding Protein/metabolism , Actins/metabolism , Animals , Calcium/metabolism , Chromaffin Cells/cytology , Chromaffin Cells/metabolism , Exocytosis/physiology , Humans , Microscopy, Confocal , PC12 Cells , Rats , Signal Transduction/physiology , Transfection
13.
Eur J Neurosci ; 20(10): 2524-40, 2004 Nov.
Article in English | MEDLINE | ID: mdl-15548197

ABSTRACT

Analysis of Tenascin-C (TN-C) knockout mice revealed novel roles for this extracellular matrix (ECM) protein in regulation of the developmental programme of oligodendrocyte precursor cells (OPCs), their maturation into myelinating oligodendrocytes and sensitivity to growth factors. A major component of the ECM of developing nervous tissue, TN-C was expressed in zones of proliferation, migration and morphogenesis. Examination of TN-C knockout mice showed roles for TN-C in control of OPC proliferation and migration towards zones of myelination [E. Garcion et al. (2001) Development, 128, 2485-2496]. Extending our studies of TN-C effects on OPC development we found that OPCs can endogenously express TN-C protein. This expression covered the whole range of possible TN-C isoforms and could be strongly up-regulated by leukaemia inhibitory factor and ciliary neurotrophic factor, cytokines known to modulate OPC proliferation and survival. Comparative analysis of TN-C knockout OPCs with wild-type OPCs reveals an accelerated rate of maturation in the absence of TN-C, with earlier morphological differentiation and precocious expression of myelin basic protein. TN-C knockout OPCs plated on poly-lysine displayed higher levels of apoptosis than wild-type OPCs and there was also an earlier loss of responsiveness to the protective effects of platelet-derived growth factor (PDGF), indicating that TN-C has anti-apoptotic effects that may be associated with PDGF signalling. The existence of mechanisms to compensate for the absence of TN-C in the knockout is indicated by the development of oligodendrocytes derived from TN-C knockout neurospheres. These were present in equivalent proportions to those found in wild-type neurospheres but displayed enhanced myelin membrane formation.


Subject(s)
Gene Expression Regulation, Developmental/drug effects , Oligodendroglia/metabolism , Platelet-Derived Growth Factor/pharmacology , Stem Cells/metabolism , Tenascin/physiology , Animals , Animals, Newborn , Antigens/metabolism , Blotting, Western/methods , Brain/cytology , Brain/embryology , Brain/growth & development , Brain/metabolism , Bromodeoxyuridine/metabolism , Cell Count/methods , Cell Differentiation/drug effects , Cell Survival/drug effects , Cells, Cultured , Cerebral Cortex/cytology , Chondroitin Sulfates/metabolism , Cytokines/pharmacology , Embryo, Mammalian , Humans , Immunohistochemistry/methods , In Situ Hybridization/methods , In Situ Nick-End Labeling/methods , Mice , Mice, Inbred C57BL , Mice, Knockout , Models, Biological , Myelin Basic Protein/metabolism , Nerve Tissue Proteins/metabolism , Oligodendroglia/drug effects , Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/pharmacology , Protein Tyrosine Phosphatases/metabolism , Proteoglycans/metabolism , RNA, Messenger/biosynthesis , Rats , Rats, Sprague-Dawley , Receptor, Platelet-Derived Growth Factor alpha/genetics , Receptor, Platelet-Derived Growth Factor alpha/metabolism , Receptor-Like Protein Tyrosine Phosphatases, Class 5 , Reverse Transcriptase Polymerase Chain Reaction/methods , Stem Cells/drug effects , Tenascin/genetics , Time Factors
14.
J Neurosci ; 22(15): 6596-609, 2002 Aug 01.
Article in English | MEDLINE | ID: mdl-12151539

ABSTRACT

Tenascin-C is a multimodular glycoprotein that possesses neurite outgrowth-stimulating properties, and one functional site has been localized to the alternatively spliced fibronectin type III domain D. To identify the neuronal receptor that mediates this effect, neighboring pairs of fibronectin type III domains were expressed as hybrid proteins fused to the Fc fragment of human immunoglobulin. These IgFc fusions were tested for neurite outgrowth-promoting properties on embryonic day 18 rat hippocampal neurons, and both the combinations BD and D6 were shown to promote the elongation of the longest process, the prospective axon. Antibodies to the cell adhesion molecule F3/contactin of the Ig superfamily blocked the BD- but not the D6-dependent effect. Biochemical studies using F3/contactin-IgFc chimeric proteins confirmed that the adhesion molecule selectively reacts with the combination BD but not with other pairs of fibronectin type III repeats of tenascin-C. The alternatively spliced BD cassettes are prominently expressed in the developing hippocampus, as shown by reverse transcription PCR, and colocalize with F3 expression during perinatal periods when axon growth and the establishment of hippocampal connections take place. We conclude that F3/contactin regulates axon growth of hippocampal neurons in response to tenascin-C.


Subject(s)
Alternative Splicing/physiology , Cell Adhesion Molecules, Neuronal/metabolism , Hippocampus/drug effects , Neurons/drug effects , Tenascin/pharmacology , Amino Acid Motifs/physiology , Animals , Cells, Cultured , Contactins , Fibronectins/physiology , Hippocampus/cytology , Hippocampus/embryology , Humans , Immunoglobulin Fc Fragments/genetics , Immunoglobulin G/genetics , Immunohistochemistry , Mice , Neurites/drug effects , Neurites/physiology , Neurons/cytology , Neurons/metabolism , Protein Binding/physiology , Protein Structure, Tertiary/physiology , Rats , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Reverse Transcriptase Polymerase Chain Reaction
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