In vitro assay of neurofilament light chain self-assembly using truncated mutants

Kim, Sungkuk; Cho, Sang-Min; Lee, In-Bum; Lee, Young Han; Kang, Jung Hoon; Choi, Jang Hyun; Suh, Pann‐Ghill; Chang, Jong-Soo

doi:10.1016/j.jneumeth.2006.10.022

Cited by 6 publications

(8 citation statements)

References 30 publications

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“…We found the middle subunit of neurofilament (NEFM) to be a function of the age of patients alone, and not depending on the group. Similarly, this finding is in contrast to other reports that did not include additional parameters into the analysis [41,42].…”

Section: Discussioncontrasting

confidence: 99%

Disease State, Age, Sex, and Post-Mortem Time-Dependent Expression of Proteins in AD vs. Control Frontal Cortex Brain Samples

Müller¹,

Jung

Ullrich³

et al. 2008

CAR

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Human post-mortem brain samples are excellent source material for the analysis of age-related disorders such as Alzheimer's disease (AD). Moreover, data obtained from cell culture- or mouse model-related experiments often need to be validated by using human tissue. In a variety of studies over the last few years, a huge list of genes or proteins with differential expression or abundance between AD-related and control tissue has been reported. However, highly important issues such as changes in post-mortem time, sex, age etc. of the patients have been rarely included in the analysis. In our study we examined human frontal brain samples of 10 AD patients vs. 10 unaffected controls using state-of-the-art two dimensional DIGE proteomics in order to analyze protein expression of up to 10,000 proteins in parallel. Data were analyzed using well established DIGE-software tool as well as an analysis of covariance model including the factor effects of group and sex and the covariable effects of age and post-mortem time. Within this study we report protein expression changes in AD vs. control human frontal brain samples without any influence of other parameters as well as expression changes depending on the parameters mentioned above. In fact, some proteins previously suggested a state of being dysregulated in AD vs. controls revealed age or sex-dependent regulation. Our analysis suggests the necessity of integrating additionally available covariables in comparative proteome studies of two different sets of human tissue.

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Section: Discussioncontrasting

confidence: 99%

Disease State, Age, Sex, and Post-Mortem Time-Dependent Expression of Proteins in AD vs. Control Frontal Cortex Brain Samples

Müller¹,

Jung

Ullrich³

et al. 2008

CAR

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“…One of the roles of the increased NGF could be the increase in the expression of neurofilaments, proteins that play a key role in the maintenance and remodeling of the neuronal cytoskeleton (Vaucher et al, 2001). Neurofilaments are heteropolymers composed of light (NF-L), middle (NF-M), and heavy (NF-H) subunits, present in most neurons (Kim et al, 2007). NF-L promoter activity is first detected at embryonic day 8.5 in neuroepithelial cells (Yaworsky et al, 1997) and its gene expression is induced by NGF (Marek et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

Effect of 1α,25‐dihydroxyvitamin D3 in embryonic hippocampal cells

et al. 2009

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Although the role of 1alpha,25-dihydroxyvitamin D3 in calcium homeostasis of bone tissue is clear, evidence of the involvement of vitamin D3 in the central nervous system functions is increasing. In fact, vitamin D3 regulates vitamin D receptor and nerve growth factor expression, modulates brain development, and reverses experimental autoimmune encephalomyelitis. Only few studies, however, address vitamin D3 effect on embryonic hippocampal cell differentiation. In this investigation, the HN9.10e cell line was used as experimental model; these cells, that are a somatic fusion product of hippocampal cells from embryonic day-18 C57BL/6 mice and N18TG2 neuroblastoma cells, show morphological and cytoskeletal features similar to their neuronal precursors. By this model, we have studied the time course of vitamin D3 localization in the nucleus and its effect on proteins involved in proliferation and/or differentiation. We found that the translocation of vitamin D3 from cytoplasm to the nucleus is transient, as the maximal nuclear concentration is reached after 10 h of incubation with (3)H-vitamin D3 and decreases to control values by 12 h. The appearance of differentiation markers such as Bcl2, NGF, STAT3, and the decrease of proliferation markers such as cyclin-1 and PCNA are late events. Moreover, physiological concentrations of vitamin D3 delay cell proliferation and induce cell differentiation of embryonic cells characterized by modification of soma lengthening and formation of axons and dendrites.

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“…The following plasmids were used: pEGFP (enhanced green fluorescent protein)‐N1 (Clontech, Heidelberg, Germany), EGFP‐TRIM2 (Reymond et al. 2001), EGFP‐NF‐L (Kim et al. 2007), Myc‐TRIM2, Myc‐ΔRBCC‐TRIM2 (both Balastik et al.…”

Section: Methodsmentioning

confidence: 99%

The E3‐ubiquitin ligase TRIM2 regulates neuronal polarization

Khazaei

Bunk

Hillje

et al. 2010

Journal of Neurochemistry

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Abbreviations used: DIV, days in vitro; EGFP, enhanced green fluorescent protein; MAP2, microtubule-associated protein 2; MN, motor neuron; MT, microtubule; NF-L, neurofilament light chain; RNAi, RNA interference; shRNAs, small hairpin RNAs; TRIM, tripartite motif; UPS, ubiquitin proteasome system. AbstractThe establishment of a polarized morphology with a single axon and multiple dendrites is an essential step during neuronal differentiation. This cellular polarization is largely depending on changes in the dynamics of the neuronal cytoskeleton. Here, we show that the tripartite motif (TRIM)-NHL protein TRIM2 is regulating axon specification in cultured mouse hippocampal neurons, where one of several initially indistinguishable neurites is selected to become the axon.Suppression of TRIM2 by RNA interference results in the loss of neuronal polarity while over-expression of TRIM2 induces the specification of multiple axons. TRIM2 conducts its function during neuronal polarization by ubiquitination of the neurofilament light chain. Together, our results imply an important function of TRIM2 for axon outgrowth during development.

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In vitro assay of neurofilament light chain self-assembly using truncated mutants

Cited by 6 publications

References 30 publications

Disease State, Age, Sex, and Post-Mortem Time-Dependent Expression of Proteins in AD vs. Control Frontal Cortex Brain Samples

Disease State, Age, Sex, and Post-Mortem Time-Dependent Expression of Proteins in AD vs. Control Frontal Cortex Brain Samples

Effect of 1α,25‐dihydroxyvitamin D3 in embryonic hippocampal cells

The E3‐ubiquitin ligase TRIM2 regulates neuronal polarization

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