Detection of the peripheral nervous system (PNS)-type glial fibrillary acidic protein (GFAP) and its mRNA in human lymphocytes

Riol, Hélène; Tardy, M.; Rolland, B.; Lévesque, Georges; Murthy, M.R.V.

doi:10.1002/(sici)1097-4547(19970401)48:1<53::aid-jnr5>3.0.co;2-d

Cited by 36 publications

(12 citation statements)

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“…Previous studies in aging rodent and human brains have pointed out that increased GFAP protein could result from either transcriptional or post-transcriptional regulation (8,(63)(64)(65). The results of the pGfa2luc experiment (Fig.…”

Section: Discussionmentioning

confidence: 81%

Intermediate filament transcription in astrocytes is repressed by proteasome inhibition

et al. 2009

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Increased expression of the astrocytic intermediate filament protein glial fibrillary acidic protein (GFAP) is a characteristic of astrogliosis. This process occurs in the brain during aging and neurodegeneration and coincides with impairment of the ubiquitin proteasome system. Inhibition of the proteasome impairs protein degradation; therefore, we hypothesized that the increase in GFAP may be the result of impaired proteasomal activity in astrocytes. We investigated the effect of proteasome inhibitors on GFAP expression and other intermediate filament proteins in human astrocytoma cells and in a rat brain model for astrogliosis. Extensive quantitative RT-PCR, immunocytochemistry, and Western blot analysis resulted unexpectedly in a strong decrease of GFAP mRNA to <4% of control levels [Control (DMSO) 100+/-19.2%; proteasome inhibitor (epoxomicin) 3.5+/-1.3%, n=8; P < or = 0.001] and a loss of GFAP protein in astrocytes in vitro. We show that the proteasome alters GFAP promoter activity, possibly mediated by transcription factors as demonstrated by a GFAP promoter-luciferase assay and RT(2) Profiler PCR array for human transcription factors. Most important, we demonstrate that proteasome inhibitors also reduce GFAP and vimentin expression in a rat model for induced astrogliosis in vivo. Therefore, proteasome inhibitors could serve as a potential therapy to modulate astrogliosis associated with CNS injuries and disease.

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Section: Discussionmentioning

confidence: 81%

Intermediate filament transcription in astrocytes is repressed by proteasome inhibition

et al. 2009

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“…Annealing temperatures (AT) and primer sequences are as follows: β2-actin (forward: 5′-CTCGCTGTCCACCTTCCA-3′; reverse: 5′-GCTGTCACCTTCACCGTTC-3′; size: 256 bp; AT: 56°C), S100B [27] (forward: 5′- CATTTCTTAGAGGAAATC-3′; reverse: 5′-ATGTTCAAAGAACTCGTG-3′; size: 147 bp; AT: 46°C), BDNF (forward: 5′-CAAACATCCGAGGACAAG-3′; reverse: 5′- GCCGTTACCCACTCACT-3′; size: 379 bp; AT: 56°C), and GDNF (forward: 5′- ACTTGGGTCTGGGCTATGAA-3′; reverse: 5′-TGTCACTCACCAGCCTTCTATT-3′; size: 132 bp; AT: 53°C). Amplification products were examined by electrophoresis on 1.5% agarose gel stained with ethidium bromide.…”

Section: Methodsmentioning

confidence: 99%

S100B Protein, Brain-Derived Neurotrophic Factor, and Glial Cell Line-Derived Neurotrophic Factor in Human Milk

2011

PLoS ONE

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BackgroundHuman milk contains a wide variety of nutrients that contribute to the fulfillment of its functions, which include the regulation of newborn development. However, few studies have investigated the concentrations of S100B protein, brain-derived neurotrophic factor (BDNF), and glial cell line-derived neurotrophic factor (GDNF) in human milk. The associations of the concentrations of S100B protein, BDNF, and GDNF with maternal factors are not well explored.Methodology/Principal FindingsTo investigate the concentrations of S100B protein, BDNF, and GDNF in human milk and characterize the maternal factors associated with their levels in human milk, human milk samples were collected at days 3, 10, 30, and 90 after parturition. Levels of S100B protein, BDNF, and GDNF, and their mRNAs in the samples were detected. Then, these concentrations were compared with lactation and other maternal factors. S100B protein levels in human milk samples collected at 3, 10, 30, and 90 d after parturition were 1249.79±398.10, 1345.05±539.16, 1481.83±573.30, and 1414.39±621.31 ng/L, respectively. On the other hand, the BDNF concentrations in human milk samples were 10.99±4.55, 13.01±5.88, 13.35±6.43, and 2.83±5.47 µg/L, while those of GDNF were 10.90±1.65, 11.38±1., 11.29±3.10, and 11.40±2.21 g/L for the same time periods. Maternal post-pregnancy body mass index was positively associated with S100B levels in human milk (r = 0.335, P = 0.030<0.05). In addition, there was a significant correlation between the levels of S100B protein and BDNF (z = 2.09, P = 0.037<0.05). Delivery modes were negatively associated with the concentration of GDNF in human milk.ConclusionsS100B protein, BDNF, and GDNF are present in all samples of human milk, and they may be responsible for the long term effects of breast feeding.

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“…GFAP is a member of the family of intermediate filament structural proteins, which, in the mature nervous system, is found predominantly in protoplasmic and specialized astrocytes of the central nervous system (CNS) as well as in satellite cells, non-myelinating Schwann cells, and enteric glia in the peripheral nervous system (PNS; Jessen et al, 1984; Eng, 1985; Kato et al, 1990). Outside the nervous system, GFAP has also been detected in some rare non-glial cells of the salivary glands (Achstatter et al, 1986; Gustafsson et al, 1989), fibroblasts (Hainfellner et al, 2001), myoepithelial cells (Viale et al, 1991), liver stellate cells (Gard et al, 1985), and lymphocytes (Riol et al, 1997). This protein is one of the key elements of the cytoskeleton that contributes to the morphology and motility of astrocyte processes (Fuchs and Weber, 1994; Pekny and Pekna, 2004; Gomi et al, 2010; Middeldorp and Hol, 2011) and is upregulated in reactive astrocytes (astrogliosis) in essentially any CNS pathology (Eng and Ghirnikar, 1994; Eng et al, 2000; Pekny and Nilsson, 2005; Sofroniew, 2009; Sosunov et al, 2013).…”

Section: Studying Astrocyte Function Through Gene Disruptionmentioning

confidence: 99%

Recent molecular approaches to understanding astrocyte function in vivo

Davila

Thibault

Fiacco

et al. 2013

Front. Cell. Neurosci.

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Astrocytes are a predominant glial cell type in the nervous systems, and are becoming recognized as important mediators of normal brain function as well as neurodevelopmental, neurological, and neurodegenerative brain diseases. Although numerous potential mechanisms have been proposed to explain the role of astrocytes in the normal and diseased brain, research into the physiological relevance of these mechanisms in vivo is just beginning. In this review, we will summarize recent developments in innovative and powerful molecular approaches, including knockout mouse models, transgenic mouse models, and astrocyte-targeted gene transfer/expression, which have led to advances in understanding astrocyte biology in vivo that were heretofore inaccessible to experimentation. We will examine the recently improved understanding of the roles of astrocytes – with an emphasis on astrocyte signaling – in the context of both the healthy and diseased brain, discuss areas where the role of astrocytes remains debated, and suggest new research directions.

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Detection of the peripheral nervous system (PNS)-type glial fibrillary acidic protein (GFAP) and its mRNA in human lymphocytes

Cited by 36 publications

References 43 publications

Intermediate filament transcription in astrocytes is repressed by proteasome inhibition

Intermediate filament transcription in astrocytes is repressed by proteasome inhibition

S100B Protein, Brain-Derived Neurotrophic Factor, and Glial Cell Line-Derived Neurotrophic Factor in Human Milk

Recent molecular approaches to understanding astrocyte function in vivo

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