Developmental changes of synapsin I subcellular localization in rat cerebellar neurons.

Harada, Akira; Sobue, Kenji; Hirokawa, Nobutaka

doi:10.1247/csf.15.329

Cited by 28 publications

(25 citation statements)

References 39 publications

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“…These findings suggest that the intracellular localization of synapsin III is an important determinant of its function, which might also be the case for the other two synapsins. For example, early in neuronal development, synapsin I (like synapsin III) is distributed throughout the soma of neurons, but, once synaptic contacts are initiated, synapsin I sequesters to the presynaptic compartment (Fletcher et al, 1991;Harada et al, 1990;Mason, 1986). A similar scenario may occur for synapsin II, which is known to bind to synapsin I or III (Hosaka and Sü dhof, 1999).…”

Section: Discussionmentioning

confidence: 99%

Early involvement of synapsin III in neural progenitor cell development in the adult hippocampus

Kao

Chao

et al. 2008

J of Comparative Neurology

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Synapsin III is a synaptic vesicle-associated protein that is expressed in cells of the subgranular layer of the hippocampal dentate gyrus, a brain region known to sustain substantial levels of neurogenesis into adulthood. Here we tested the hypothesis that synapsin III plays a role in adult neurogenesis with synapsin III knockout and wild-type mice. Immunocytochemistry of the adult hippocampal dentate gyrus revealed that synapsin III colocalizes with markers of neural progenitor cell development (nestin, PSA-NCAM, NeuN, and Tuj1) but did not colocalize with markers of mitosis (Ki67 and PCNA). Because neurogenesis consists of a number of stages, the proliferation, survival, and differentiation of neural progenitor cells were systematically quantitated in the hippocampal dentate gyrus of adult synapsin III knockout and wild-type mice. We found a 30% decrease in proliferation and a 55% increase in survival of neural progenitor cells in synapsin III knockout mice. We also observed a 6% increase in the number of neural progenitor cells that differentiated into neurons. No difference in the volume of the dentate gyrus was observed between synapsin III knockout and wild-type mice. Collectively, our results demonstrate a novel role for synapsin III in regulating the proliferation of neural progenitor cells in the adult hippocampal dentate gyrus. These findings suggest a distinct function for this synaptic vesicle protein, in addition to its role in neurotransmission.

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Section: Discussionmentioning

confidence: 99%

Early involvement of synapsin III in neural progenitor cell development in the adult hippocampus

Kao

Chao

et al. 2008

J of Comparative Neurology

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“…The sections were washed with 50 mMglycine in PBS for 15 min and blocked with 5% normal goat serum in PBS for 20 min. The sections were incubated for 1 h at 37°C with either diluted anti-synapsin I antibody or anti-synaptophysin antibody, whose characterization was perfomed elsewhere (9,14,(27)(28)(29). Antibodies were diluted in \% bovine serum albumin in PBS.…”

Section: Methodsmentioning

confidence: 99%

Redistribution of Synapsin I and Synaptophysin in Response to Electrical Stimulation in the Rat Neurohypophysial Nerve Endings.

Hayashi

Soulie

Nakata

et al. 1994

Cell Struct. Funct.

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ABSTRACT. To understand the dynamics of synaptic vesicles and synapsin I, we have studied the localization of synapsin I and synaptophysin in resting and stimulated nerve endings by ultracryomicrotomy and colloidal gold-immunocytochemistry. First, we characterized microvesicles in resting nerve endings of the rat neurohypophysis, which was chosen as the model of nerve ending in this study. Synaptophysin was localized in microvesicles that were clustered beneath the plasma membrane. Quick-freeze deep-etching electron microscopy showed that short strands cross-linked microvesicles to each other, which highly resembly the structures observed in our studies of the presynaptic nerve terminals of central and peripheral nervous system and in vitro reconstitution of synapsin I and synaptic vesicles. Immunocytochemistry showed that synapsin I was localized to the region of cluster of microvesicles. Second, using this system, we examined localization of synapsin I and synaptophysin in nerve endings after electrical stimulation. Besides release of neurosecretory granules, clusters of microvesicles disappeared and both microvesicles and synaptophysin were scattered over nerve endings. These changes were also confirmed by quick-freeze, freeze-substitution.Immunocytochemistry of the stimulated sample revealed that synapsin I was also scattered. The results show that microvesicles in neurohypophysis have similar characteristics of typical synaptic vesicles and synapsin I has a role as a scaffold to cross-link microvesicles to be clustered in resting nerve endings. This scaffold of synapsin I was disengaged after stimulation to redistribute microvesicles and synapsin I itself, which may be the mechanism of synapsin I to regulate the availability of synaptic vesicles for release.

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“…Samples were fixed using perfusion with 4% (w/v) PFA in 0.1 M phosphate buffer (pH 7.4) and processed as previously described (Harada et al, 1990, Sato et al, 2011. We performed hematoxylin-eosin staining using standard histological procedures.…”

Section: Histology and Western Blot Analysesmentioning

confidence: 99%

“…Tissues were dissected and further fixed for 2 hours at RT and treated with 1% OsO4 in 0.1 M cacodylate buffer followed by 0.5% uranyl acetate in water. The samples were dehydrated and embedded in Epon, and thin sections were post-stained with uranyl acetate and lead citrate as described previously (Harada et al, 1990). Sections were then studied under an electron microscope (model 1010; JEOL, Tokyo, Japan) at 80 kV.…”

Section: Electron Microscopymentioning

confidence: 99%

Rab8a and Rab8b are essential for several apical transport pathways but insufficient for ciliogenesis

Satō¹,

Iwano²,

Kunii³

et al. 2014

Development

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The small GTP-binding protein Rab8 is known to play an essential role in intracellular transport and cilia formation. We have previously demonstrated that Rab8a is required for localising apical markers in various organisms. Rab8a has a closely related isoform, Rab8b. To determine whether Rab8b can compensate for Rab8a, we generated Rab8b-knockout mice. Although the Rab8b-knockout mice did not display an overt phenotype, Rab8a and Rab8b double-knockout mice exhibited mislocalisation of apical markers and died earlier than Rab8a-knockout mice. The apical markers accumulated in three intracellular patterns in the double-knockout mice. However, the localisation of basolateral and/or dendritic markers of the double-knockout mice seemed normal. The morphology and the length of various primary and/or motile cilia, and the frequency of ciliated cells appeared to be identical in control and double-knockout mice. However, an additional knockdown of Rab10 in double-knockout cells greatly reduced the percentage of ciliated cells. Our results highlight the compensatory effect of Rab8a and Rab8b in apical transport, and the complexity of the apical transport process. In addition, neither Rab8a nor Rab8b are required for basolateral and/or dendritic transport. However, simultaneous loss of Rab8a and Rab8b has little effect on ciliogenesis, whereas additional loss of Rab10 greatly affects ciliogenesis.

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Developmental changes of synapsin I subcellular localization in rat cerebellar neurons.

Cited by 28 publications

References 39 publications

Early involvement of synapsin III in neural progenitor cell development in the adult hippocampus

Early involvement of synapsin III in neural progenitor cell development in the adult hippocampus

Redistribution of Synapsin I and Synaptophysin in Response to Electrical Stimulation in the Rat Neurohypophysial Nerve Endings.

Rab8a and Rab8b are essential for several apical transport pathways but insufficient for ciliogenesis

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