High molecular weight tau: preferential localization in the peripheral nervous system

Using epitope mapping we have demonstrated that a high molecular weight protein (Mr approximately 115 × 10(3)) present in brain and spinal cord is a member of the tau family of microtubule-associated proteins. Antibodies directed against the amino-terminal, middle and carboxyl-terminal portions of tau recognize this protein. A limited survey of neuronal tissues has shown that this high molecular weight tau protein is present in brain, spinal cord, dorsal root ganglia, dorsal and ventral roots and peripheral nerves. High molecular weight tau protein is expressed at higher levels in spinal cord than in brain and is the only form of tau detected in the adult peripheral nervous system.

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Expression of high molecular weight tau in the central and peripheral nervous systems

Journal of Cell Science ◽

10.1242/jcs.105.3.729 ◽

1993 ◽

Vol 105 (3) ◽

pp. 729-737

Author(s):

I.S. Georgieff ◽

R.K. Liem ◽

D. Couchie ◽

C. Mavilia ◽

J. Nunez ◽

...

Keyword(s):

Spinal Cord ◽

Molecular Weight ◽

Nervous System ◽

High Molecular Weight ◽

Tumor Cells ◽

Apparent Molecular Weight ◽

In Vitro Transcription ◽

The Central Nervous System ◽

Immunohistochemical Studies

Using a novel PCR approach, we have cloned a cDNA encoding the entire high molecular weight tau molecule from rat dorsal root ganglia. The resulting 2080 bp cDNA differs from low molecular weight rat brain tau by the insertion of a novel 762 bp region (exon 4a) between exons 4 and 5. This cDNA clone is identical in sequence with a high molecular weight tau (HMW) cDNA from rat PC12 tumor cells and is closely related to a HMW tau cDNA from mouse N115 tumor cells. In vitro transcription/translation produces a protein that migrates on SDS-PAGE with the same apparent molecular weight as HMW tau purified from rat sciatic nerve. The HMW tau protein is generated from an 8 kb mRNA, which can be detected by northern blots in peripheral ganglia, but not in brain. A more sensitive assay using PCR and Southern blot analysis demonstrates the presence of exon 4a in spinal cord and in retina. In combination with immunohistochemical studies of spinal cord, these data suggest that HMW tau, though primarily in the peripheral nervous system, is also expressed in limited areas of the central nervous system, although its presence cannot be detected in the cerebral cortices.

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Interactions between neurofilaments and microtubule-associated proteins: a possible mechanism for intraorganellar bridging.

The Journal of Cell Biology ◽

10.1083/jcb.95.3.982 ◽

1982 ◽

Vol 95 (3) ◽

pp. 982-986 ◽

Cited By ~ 145

Author(s):

J F Leterrier ◽

R K Liem ◽

M L Shelanski

Keyword(s):

Spinal Cord ◽

Molecular Weight ◽

High Molecular Weight ◽

Microtubule Assembly ◽

Microtubule Associated Proteins ◽

Saturable Binding ◽

In Vitro Assembly ◽

Associated Proteins ◽

Brain And Spinal Cord

Mammalian neurofilaments prepared from brain and spinal cord by either of two methods partially inhibit the in vitro assembly of microtubules. This inhibition is shown to be due to the association of a complex of high molecular weight microtubule-associated proteins (MAP1 and MAP2) and tubulin with the neurofilament. Further analysis of the association reveals a saturable binding of purified brain MAPs to purified neurofilaments with a Kd of 10(-7) M. Purified astroglial filaments neither inhibit microtubule assembly nor show significant binding of MAPs. It is proposed that the MAPs might function as one element in a network of intraorganellar links in the cytoplasm.

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

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.89.10.4378 ◽

1992 ◽

Vol 89 (10) ◽

pp. 4378-4381 ◽

Cited By ~ 118

Author(s):

D. Couchie ◽

C. Mavilia ◽

I. S. Georgieff ◽

R. K. Liem ◽

M. L. Shelanski ◽

...

Keyword(s):

Molecular Weight ◽

Nervous System ◽

High Molecular Weight ◽

Peripheral Nervous System ◽

Primary Structure

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Microtubule motors and other maps

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010015753x ◽

1990 ◽

Vol 48 (3) ◽

pp. 1-1

Author(s):

Richard B. Vallee

Keyword(s):

Molecular Weight ◽

High Molecular Weight ◽

Cytoplasmic Dynein ◽

Organelle Transport ◽

Structural Components ◽

Microtubule Associated Proteins ◽

Microtubule Motors ◽

Associated Proteins ◽

The Subject ◽

Intracellular Motility

Microtubules are involved in a number of forms of intracellular motility, including mitosis and bidirectional organelle transport. Purified microtubules from brain and other sources contain tubulin and a diversity of microtubule associated proteins (MAPs). Some of the high molecular weight MAPs - MAP 1A, 1B, 2A, and 2B - are long, fibrous molecules that serve as structural components of the cytamatrix. Three MAPs have recently been identified that show microtubule activated ATPase activity and produce force in association with microtubules. These proteins - kinesin, cytoplasmic dynein, and dynamin - are referred to as cytoplasmic motors. The latter two will be the subject of this talk.Cytoplasmic dynein was first identified as one of the high molecular weight brain MAPs, MAP 1C. It was determined to be structurally equivalent to ciliary and flagellar dynein, and to produce force toward the minus ends of microtubules, opposite to kinesin.

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Karolinska Institutet 200-Year Anniversary Symposium on Injuries to the Spinal Cord and Peripheral Nervous System - An Update on Recent Advances in Regenerative Neuroscience

10.3389/978-2-88945-324-5 ◽

2017 ◽

Keyword(s):

Spinal Cord ◽

Nervous System ◽

Peripheral Nervous System ◽

Recent Advances

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Faculty Opinions recommendation of Combining an autologous peripheral nervous system "bridge" and matrix modification by chondroitinase allows robust, functional regeneration beyond a hemisection lesion of the adult rat spinal cord.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.14713.472229 ◽

2006 ◽

Author(s):

Robert Ruff

Keyword(s):

Spinal Cord ◽

Nervous System ◽

Peripheral Nervous System ◽

Rat Spinal Cord ◽

Adult Rat ◽

Matrix Modification ◽

Functional Regeneration ◽

Adult Rat Spinal Cord

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Interaction of the tail domain of high molecular weight subunits of neurofilaments with the COOH-terminal region of tubulin and its regulation by tau protein kinase II.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)41583-9 ◽

1993 ◽

Vol 268 (30) ◽

pp. 22695-22702

Author(s):

H Miyasaka ◽

S Okabe ◽

K Ishiguro ◽

T Uchida ◽

N Hirokawa

Keyword(s):

Molecular Weight ◽

Protein Kinase ◽

High Molecular Weight ◽

Tau Protein ◽

Terminal Region ◽

Tail Domain ◽

Protein Kinase Ii ◽

Tau Protein Kinase

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Identity and Origin of the ATPase activity associated with neuronal microtubules. I. The ATPase activity is associated with membrane vesicles.

The Journal of Cell Biology ◽

10.1083/jcb.96.5.1298 ◽

1983 ◽

Vol 96 (5) ◽

pp. 1298-1305 ◽

Cited By ~ 13

Author(s):

D B Murphy ◽

R R Hiebsch ◽

K T Wallis

Keyword(s):

Molecular Weight ◽

Atpase Activity ◽

High Molecular Weight ◽

Brain Tissue ◽

Membrane Vesicles ◽

Microtubule Associated Proteins ◽

In Vitro Assembly ◽

Microtubule Protein ◽

Associated Proteins

Microtubule protein purified from brain tissue by cycles of in vitro assembly-disassembly contains ATPase activity that has been postulated to be associated with microtubule-associated proteins (MAPs) and therefore significant for studies of microtubule-dependent motility. In this paper we demonstrate that greater than 90% of the ATPase activity is particulate in nature and may be derived from contaminating membrane vesicles. We also show that the MAPs (MAP-1, MAP-2, and tau factors) and other high molecular weight polypeptides do not contain significant amounts of ATPase activity. These findings do not support the concept of "brain dynein" or of MAPs with ATPase activity.

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The neuropathology of “typical” Friedreich's ataxia in Quebec

Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques ◽

10.1017/s0317167100035113 ◽

1984 ◽

Vol 11 (S4) ◽

pp. 592-600 ◽

Cited By ~ 60

Author(s):

J.B. Lamarche ◽

B. Lemieux ◽

H.B. Lieu

Keyword(s):

Spinal Cord ◽

Central Nervous System ◽

Nervous System ◽

Peripheral Nervous System ◽

Diagnostic Criteria ◽

Clinical Findings ◽

Spinal Ganglia ◽

Cooperative Study ◽

Segmental Demyelination ◽

Dying Back

AbstractWe present the pathological data from the autopsies performed on 6 Friedreich's disease patients since the start of the Quebec Cooperative Study. All patients met the strict diagnostic criteria of the QCSFA. The anatomical lesions found in the peripheral and central nervous system were similar in all 6 cases and do not differ from those described in the literature. The clinical findings correlate closely with the histological lesions found in the peripheral nervous system and spinal cord. The evidence of segmental demyelination and remyelination in the spinal ganglia and posterior roots further supports the dying-back axonopathy hypothesis.

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