Tau gene expression in rat sensory neurons during development and regeneration

Oblinger, Monica M.; Argasinski, A; Wong, Johnson; Kosik, KS

doi:10.1523/jneurosci.11-08-02453.1991

Cited by 91 publications

(79 citation statements)

References 36 publications

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“…Previous results suggested that HMW-tau may play a role in the specialization of the adult peripheral nervous system (27,28). For instance, HMW-tau and LMW-tau variants are expressed during development in the dorsal root ganglia, whereas only HMW-tau is present in the adult (28).…”

Section: Discussionmentioning

confidence: 98%

“…For instance, HMW-tau and LMW-tau variants are expressed during development in the dorsal root ganglia, whereas only HMW-tau is present in the adult (28). Since the mRNA in young and adult dorsal root ganglia migrates at 8-9 kb (27) and no 6-kb message is seen, LMW-tau and HMW-tau must be encoded by mRNAs larger than those in brain. Northern blots of rodent dorsal root ganglia using a probe for the nonhomologous region show hybridization to the 8-to 9-kb mRNA, indicating that exon 4a is expressed in normal When assayed with brain poly(A)+ RNA (5 jLg), the N-terminal fragment detected the tau transcript of 6 kb (lane 1), which is expressed in the central nervous system (14).…”

Section: Discussionmentioning

confidence: 99%

“…In addition to the tau variants of Mr 48,000-65,000 apparent molecular weight expressed in the immature and adult brain, other proteins ofhigher molecular weight ( (25)(26)(27). By epitope mapping of tau using antibodies directed against its N-terminal, middle, and C-terminal portions we have demonstrated that this high molecular weight protein (HMW-tau) is a member of the tau family (28).…”

mentioning

confidence: 99%

“…By epitope mapping of tau using antibodies directed against its N-terminal, middle, and C-terminal portions we have demonstrated that this high molecular weight protein (HMW-tau) is a member of the tau family (28). A limited survey of neuronal tissues has shown that this HMW-tau variant is present in very low amounts in the central nervous system and is the only form of tau detected in the adult peripheral nervous system (27,28). An abnormal tau variant of Mr 120,000-130,000 has been also identified in extracts of paired helical filaments, the abnormal structures characteristic of Alzheimer dementia (29 (N115) by the procedure of Chirgwin et al (33).…”

mentioning

confidence: 99%

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Primary structure of high molecular weight tau present in the peripheral nervous system.

Couchie

Mavilia

Georgieff

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

219

167

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The tau proteins are a family of brain microtubule binding proteins that are required during axonal outgrowth and are found in neurofibrillary tangles in AMzeimer disease. A protein of higher molecular weight, immunologically related to tan, is expressed in the adult peripheral system and in cultured neuronal cell lines of neural crest origin. The predicted amino acid sequence ofthe high molecular weight tau from N115 cells has been determined from the sequence of its 2340-base-pair cDNA. High molecular weight tau contains an open reading frame encoding 733 amino acid residues. It contains sequences homologous to those present in the N-, middle, and C-terminal domains of adult brain tau proteins, incinding four homologous repeats, which are the tubulin binding sites, and an amino acid stretch, which is present only in the N-terminal domain of the mature brain variants. The middle region contains a previously unidentified nonhomol gous stretch of 237 amino acid residues as well as a domain of 66 residues homologous to exon 6 of the bovine gene that is absent in all bovine, rat, and mouse tau cDNAs sequenced so far. A cDNA probe specific to the nonhomologous tau insert hybridizes to the 8-to 9-kilobase tau mRNA in N115 cells but not to the 6-kilobase tan mRNA in brain. Probes for the domains common to brain tau isoforms hybridize to both messages. The sequence of hig molecular weight tan protein also suggests that it, like low molecular weight tan, is an elongated hydrophilic molecule. This cDNA should allow us to study the role of the do specific to these tau forms in the specialization of the peripheral nervous system and for study of their expression in normal and pathological states.Tau and MAP2 proteins are microtubule-associated proteins (MAPs) that are able to promote polymerization of tubulin into microtubules in vitro (1-3). Although the microtubules formed in the presence of these two MAPs are similar (4), several lines of evidence suggest that MAP2 and tau proteins play an essential role in the establishment of neuronal polarity. MAP2 is preferentially localized in dendrites, whereas tau is almost exclusively targeted to the axons and its expression is required during axonal outgrowth (5)(6)(7)(8). Additional interest in tau protein has stemmed from its identification as a major component of the paired helical filaments, the abnormal structures characteristic of the Alzheimer disease (9-12).

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Primary structure of high molecular weight tau present in the peripheral nervous system.

Couchie

Mavilia

Georgieff

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

219

167

View full text Add to dashboard Cite

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“…Thus, a shift in the balance of various tubulins and MAPS during regeneration may either increase or decrease the plasticity of the microtubule network during different phases of regeneration. Recent observations of downregulation of tau mRNA and protein levels in DRG neurons during regeneration provide support to this argument (Oblinger et al, 1991). Clearly, additional information will be required to sort out the mechanisms by which augmented or decreased levels of various tubulins and MAPS produce alterations in the functional properties of microtubule networks.…”

Section: Axotomy-induced Changes In And-tubandn Content In Drg Neuronsmentioning

confidence: 96%

Sensory neurons selectively upregulate synthesis and transport of the beta III-tubulin protein during axonal regeneration

Moskowitz

Oblinger

1995

J. Neurosci.

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The effects of peripheral nerve injury on the content, synthesis, and axonal transport of the class Ill 6-tubulin protein in adult rat dorsal root ganglion (DRG) neurons were examined.Recent reports of selective increases in the steady-state levels of the j$,,-tubulin mRNA during axonal regeneration (Moskowitz et al., 1993) led to the hypothesis that upregulated levels of expression of the j3,,,-tubulin isotype that alter the composition of neuronal microtubules is important for effective axonal regrowth. If this is the case, the increases in ml?NA levels must be translated into increased j3,,,-tubulin protein levels and subsequently modify the axonal cytoskeleton via axonal transport mechanisms. The present study assessed whether or not this occurs by examining fI,,,-tubulin protein content in adult rat lumbar DRG neurons at different times (1-14 d) after a distal sciatic nerve crush (-55 mm from the DRG) by Western blotting and immunocytochemistry with a 6,,,-tubulin specific monoclonal antibody. These studies showed substantial increases in 6,,,-tubulin content in DRG neurons, as well as in proximal regions of peripheral sensory axons (O-6 mm from the DRG), from l-2 weeks after a distal nerve injury. Pulse labeling of DRG neurons with %-methionine and 35S-cysteine and immunoprecipitation of labeled f3,,,-tubulin indicated that the synthesis of j$,,-tubulin was increased in the DRG after axotomy.Studies of axonal transport, wherein L5 DRG proteins were labeled with %-methionine and %-cysteine by microinjection, revealed that slow component b (SCb) of axonal transport conveyed more labeled tubulin moving at apparently faster rates through the intact regions of sciatic nerve axons in response to crush injury of the distal sciatic nerve. lmmunoprecipitation experiments using proximal peripheral nerve segments showed that SCb in distally injured DRG neurons was enriched in the p,,,-tubulin isotype. These findings demonstrate that the augmented synthesis of p,,,-tubulin after axotomy alters the composition of the axonally transported cytoskeleton that moves with SCb. The increased amounts and rate of delivery of 6,,,-tubulin in axons of regenerating DRG neurons suggest that the altered pattern of tubulin gene expression that is initiated by axotomy impacts on the composition

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MAP1B expression and microtubule stability in growing and regenerating axons

Gordon‐Weeks

Fischer

2000

Microsc. Res. Tech.

113

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MAP1B is a microtubule‐associated phosphoprotein that is particularly highly expressed in developing neurons. There is experimental evidence that it plays an important role in neuronal differentiation, especially the extension of axons and dendrites, but exactly what role is unclear. Recent experiments have shed light on the gene structure of MAP1B and identified some of the kinases that phosphorylate the protein. Implicit in these findings is the idea that MAP1B regulates the organisation of microtubules in neurites and is itself regulated in a complex way and at a number of levels. Microsc. Res. Tech. 48:63–74, 2000. © 2000 Wiley‐Liss, Inc.

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Tau gene expression in rat sensory neurons during development and regeneration

Cited by 91 publications

References 36 publications

Primary structure of high molecular weight tau present in the peripheral nervous system.

Primary structure of high molecular weight tau present in the peripheral nervous system.

Sensory neurons selectively upregulate synthesis and transport of the beta III-tubulin protein during axonal regeneration

MAP1B expression and microtubule stability in growing and regenerating axons

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