Cloning of a cDNA encoding the rat high molecular weight neurofilament peptide (NF-H): developmental and tissue expression in the rat, and mapping of its human homologue to chromosomes 1 and 22.

Lieberburg, Ivan; Spinner, Nancy B.; Snyder, Susan E.; Anderson, John P.; Goldgaber, D; Smulowitz, M; Carroll, Zev; Emanuel, Beverly S.; Breitner, John C.S.; Rubin, Lee L.

doi:10.1073/pnas.86.7.2463

Cited by 50 publications

(25 citation statements)

References 32 publications

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“…It has been re ported that NF-H protein [7] and the respective mRNAs [8] accumulate to a significant extent only in the postna tal brain; other works reported a possibility of embry onal expression of NF-H immuno-reactivity at embry onal stages [24], The use of a 1.7-kb-long specific NF-H cDNA probe largely circumvents these problems. The pNF-Hl probe hybridizes with a single 4.3-kb mRNA band, in agreement with previous values of 4.5 kb de scribed for the mouse [9] and rat [14] brain. The present results show that specific mRNA could also be detected at 17 days of embryonic development, mainly in the neurons expressing high amounts of mRNA at the adult stage, which is in accordance with previous findings [24].…”

Section: Discussionsupporting

confidence: 74%

In situ Localization of NF-H Neurofilament Subunit mRNAs in Rat Brain

Roussel

Felix²,

Pham-Dinh³

et al. 1991

Dev Neurosci

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The expression of NF-H neurofilament subunit mRNAs was investigated in the rat brain at different ontogenic stages. The levels of NF-H mRNAs vary 15-fold among brain regions with the highest level in the brainstem. In situ localization studies revealed that the NF-H mRNAs are mainly concentrated in the brainstem motoneuron nuclei. By increasing the sensitivity of the hybridization method, NF-H mRNAs could also be localized in neurons present in the cortex, thalamus and hippocampus areas. Minor amounts of NF-H mRNAs were already detected at 17-day embryonic stages.

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Section: Discussionsupporting

confidence: 74%

In situ Localization of NF-H Neurofilament Subunit mRNAs in Rat Brain

Roussel

Felix²,

Pham-Dinh³

et al. 1991

Dev Neurosci

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“…4,5 The major phosphorylation sites correspond to the serine amino acids of Lys-Ser-Pro (KSP) repeat motifs, 4 where serine phosphorylation changes the charge of the KSP motif from + 1e to − 1e. These phosphorylation sites are particularly found in NF-H and NF-M sidearms that have varying numbers of KSP repeat motifs (43-52 repeats in rodent and human NF-H; [6][7][8][9] 12 repeats in human NF-M). 10 The phosphorylation of these KSP repeats alters the charge density of the protrusions and is considered to increase the lateral extension of sidearms 11,12 (through repulsive interactions of negatively charged sites).…”

Section: Introductionmentioning

confidence: 99%

Structural Properties of Neurofilament Sidearms: Sequence-Based Modeling of Neurofilament Architecture

Chang

Kwak

Gebremichael

2009

Journal of Molecular Biology

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“…Three vertebrate neurofilament (NF) proteins [low (NF-L), medium (NF-M), and high (NF-H)], classified as type IV IF proteins (1), are expressed exclusively in cells of neuronal lineage (6)(7)(8)(9)(10). NF-M and NF-H contain long carboxylterminal tail domains, which are highly phosphorylated at repeated Lys-Ser-Pro (KSP) motifs (11) by specific kinases (12,13).…”

mentioning

confidence: 99%

A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain with Lys-Ser-Pro repeats.

Way

Hellmich

Jaffe

et al. 1992

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

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Previous studies have shown that two low molecular-weight neurofilament (NF) proteins (NF-60 and NF-70) from the squid Loligo pealei are translated from mRNAs that are splice variants of a single squid NF gene. In this study, we report the isolation and characterization of cDNA clones encoding a high-molecular-weight squid NF protein (NF-220), the mRNA of which derives from the same squid NF gene. All three proteins are identical in their amino-terminal and lamin-like rod domains but differ in their carboxyl-terminal tail regions. In contrast to the short tail domains of NF-60 and NF-70, the NF-220 protein has a longer tail domain containing an acidic cluster of amino acids immediately followed by repeated copies of the sequence motif Lys-Ser-Pro. The Lys-Ser-Pro domain is similar to that of mammalian medium NF (NF-M) and high NF (NF-H) proteins, where the serines are highly phosphorylated. Except for these Lys-Ser-Pro motifs, there is surprisingly little structural similarity between the squid NF-220 protein and mammalian NF-M and NF-H proteins. Furthermore, the location of introns in squid NF-220 protein shows that it is more closely related to nuclear lamins and type III intermediate-filament proteins than to vertebrate NF proteins.

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Cloning of a cDNA encoding the rat high molecular weight neurofilament peptide (NF-H): developmental and tissue expression in the rat, and mapping of its human homologue to chromosomes 1 and 22.

Abstract: Neurofflaments (NFs) are the intermediate

Cited by 50 publications

References 32 publications

In situ Localization of NF-H Neurofilament Subunit mRNAs in Rat Brain

In situ Localization of NF-H Neurofilament Subunit mRNAs in Rat Brain

Structural Properties of Neurofilament Sidearms: Sequence-Based Modeling of Neurofilament Architecture

A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain with Lys-Ser-Pro repeats.

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