Distribution of Rab3a in rat nervous system: comparison with other synaptic vesicle proteins and neuropeptides

Li, Jiayi; Jahn, Reinhard; Hou, Xie-E; Kling-Petersen, Anne; Dahlström, Annica

doi:10.1016/0006-8993(95)01202-8

Cited by 16 publications

(2 citation statements)

References 32 publications

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“…Our data suggests that Rab3A may be involved in the packaging of specific proteins into different vesicle subtypes that in turn may be moved by specific motor proteins. In this regard, it is remarkable that inhibition of Rab3A had no influence on the anterograde transport of synaptophysin, even though Rab3 colocalizes with synaptophysin at nerve terminals (Li et al, 1996a), and has been co-purified from synaptic vesicles in immunoisolation experiments (Fischer von Mollard et al, 1990; de Wit et al, 1999). The anti-Rab3 antibody used in these two studies does not allow differentiating between the Rab3 isoforms.…”

Section: Discussionmentioning

confidence: 99%

APP Anterograde Transport Requires Rab3A GTPase Activity for Assembly of the Transport Vesicle

Szodorai¹,

Kuan²,

Hunzelmann³

et al. 2009

J. Neurosci.

110

104

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The amyloid precursor protein (APP) is anterogradely transported by conventional kinesin in a distinct transport vesicle, but both the biochemical composition of such a vesicle and the specific kinesin-1 motor responsible for transport are poorly defined. APP may be sequentially cleaved by ␤-and ␥-secretases leading to accumulation of ␤-amyloid (A␤) peptides in brains of Alzheimer's disease patients, whereas cleavage of APP by ␣-secretases prevents A␤ generation. Here, we demonstrate by time-lapse analysis and immunoisolations that APP is a cargo of a vesicle containing the kinesin heavy chain isoform kinesin-1C, the small GTPase Rab3A, and a specific subset of presynaptic protein components. Moreover, we report that assembly of kinesin-1C and APP in this vesicle type requires Rab3A GTPase activity. Finally, we show cleavage of APP intransportvesiclesby␣-secretaseactivity,likelymediatedbyADAM10.Together,thesedataindicatethatmaturationofAPPtransportvesicles, including recruitment of conventional kinesin, requires Rab3 GTPase activity.

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Section: Discussionmentioning

confidence: 99%

APP Anterograde Transport Requires Rab3A GTPase Activity for Assembly of the Transport Vesicle

Szodorai¹,

Kuan²,

Hunzelmann³

et al. 2009

J. Neurosci.

110

104

View full text Add to dashboard Cite

show abstract

“…To investigate the rate of anterograde (proximal site to crush) and retrograde axonal transport (distal site to crush) of studied proteins, sciatic nerves were collected at 1, 3 and 6 h after the crush (Li et al ., ; Wang et al ., ), transferred immediately to 4% paraformaldehyde in 0.1 m phosphate‐buffered saline (PBS) and post‐fixed for 12 h at 4 °C. The following day, sections were rinsed in PBS, transferred to 20% sucrose and stored at −20 °C for further processing.…”

Section: Methodsmentioning

confidence: 99%

Impaired slow axonal transport in diabetic peripheral nerve is independent of RAGE

Juranek

Geddis

Rosario

et al. 2013

Eur J of Neuroscience

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Diabetic peripheral nerve dysfunction is a common complication occurring in 30-50% of long-term diabetic patients. The pathogenesis of this dysfunction remains unclear but growing evidence suggests that it might be attributed, in part, to alteration in axonal transport. Our previous studies demonstrated that RAGE (Receptor for Advanced Glycation Endproducts) contributes to the pathogenesis of diabetic peripheral neuropathy and impairs nerve regeneration consequent to sciatic nerve crush, particularly in diabetes. We hypothesize that RAGE plays a role in axonal transport impairment via the interaction of its cytoplasmic domain with mammalian Diaphanous 1 (mDia1) - actin interacting molecule. Studies showed that mDia1-RAGE interaction is necessary for RAGE-ligand-dependent cellular migration, AKT phosphorylation, macrophage inflammatory response and smooth muscle migration. Here, we studied RAGE, mDia1 and markers of axonal transport rates in the peripheral nerves of wild-type C57BL/6 and RAGE null control and streptozotocin-injected diabetic mice at 1, 3 and 6 h after sciatic nerve crush. The results show that in both control and diabetic nerves, the amount of RAGE accumulated at the proximal and distal side of the crush area is similar, indicating that the recycling rate for RAGE is very high and that it is evenly transported from and towards the neuronal cell body. Furthermore, we show that slow axonal transport of proteins such as Neurofilament is affected by diabetes in a RAGE-independent manner. Finally, our study demonstrates that mDia1 axonal transport is impaired in diabetes, suggesting that diabetes-related changes affecting actin binding proteins occur early in the course of the disease.

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Axonal transport and distribution of immunologically distinct kinesin heavy chains in rat neurons

Pfister

Brady

et al. 1999

J. Neurosci. Res.

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The functional significance of biochemical and immunochemical heterogeneity in neuronal kinesin remains uncertain. Confocal laser scanning microscopy, cytofluorimetric scanning, and immunoblots were used for quantitative analyses of axonal transport and cellular distribution of immunochemically distinct kinesin heavy chain isoforms (H1 and H2) in rat peripheral nerve and spinal cord. H1 and H2 immunoreactivities (IR) were observed in axons proximal to a crush as early as 1 hr after the crush operation and increased linearly with time, consistent with fast axonal transport of both. Only approximately 10% of the proximal accumulations of H1-IR and H2-IR accumulated distal to the crush, in contrast to synaptophysin-IR (approximately 70%). H2-IR was widely present in peripheral nervous system and virtually colocalized with synaptic vesicle proteins synaptophysin, synaptobrevin I, and SNAP-25 and two neuropeptides [calcitonin gene-related peptide (CGRP) and substance P (SP)], although H2-IR was weaker in spinal cord terminals. In contrast, H1-IR appeared preferentially enriched in large axons, probably motor and large sensory neurons, which contained synaptophysin-IR, synaptobrevin I-IR, SNAP-25-IR, and CGRP-IR. However, H1-IR was weak or absent from SP-containing thin and medium-sized axons. In addition, H1-IR appeared to be absent from spinal cord nerve terminals. H1- and H2-IR kinesins are both transported with fast axonal transport, and comparatively small amounts of kinesins are retrogradely transported. H2 was widely distributed in motor, sensory, and sympathetic neurons, whereas H1 was enriched in large motor and sensory neurons.

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Distribution of Rab3a in rat nervous system: comparison with other synaptic vesicle proteins and neuropeptides

Cited by 16 publications

References 32 publications

APP Anterograde Transport Requires Rab3A GTPase Activity for Assembly of the Transport Vesicle

APP Anterograde Transport Requires Rab3A GTPase Activity for Assembly of the Transport Vesicle

Impaired slow axonal transport in diabetic peripheral nerve is independent of RAGE

Axonal transport and distribution of immunologically distinct kinesin heavy chains in rat neurons

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