Glial fibrillary acidic protein: A marker of axonal Guillain–Barrè syndrome and outcome

Notturno, Francesca; Caporale, Christina M.; Lauretis, Angelo De; Uncini, Antonino

doi:10.1002/mus.20983

Cited by 21 publications

(13 citation statements)

References 31 publications

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“…Using an appropriate cutoff, GFAP determination may assess axonal damage with good sensitivity and specificity in chronic neuropathies. These findings confirm in chronic neuropathies the observation we made previously in GBS variants17 that GFAP is a marker, although indirect, of axonal damage. In the process of Wallerian degeneration the SCs lose contact with the axons, dedifferentiate, and reenter the cell proliferation cycle.…”

Section: Discussionsupporting

confidence: 92%

“…GFAP levels in serum were determined using a capture enzyme‐linked immunosorbent assay (ELISA) 17, 21. Briefly, microtiter plates were coated with the capturing antibody (rabbit polyclonal antibody anti‐GFAP) at 4°C overnight.…”

Section: Methodsmentioning

confidence: 99%

“…Recently we found that GFAP was increased in the cerebrospinal fluid and serum of patients with axonal Guillain–Barré syndrome (GBS) compared with patients who had acute inflammatory demyelinating polyneuropathy and controls. GFAP values correlated with the outcome at 6 months 17…”

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confidence: 89%

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Glial fibrillary acidic protein as a marker of axonal damage in chronic neuropathies

et al. 2009

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We evaluated serum glial fibrillary acidic protein (GFAP) levels by enzyme-linked immunosorbent assay (ELISA) in controls (n = 30) and in patients with chronic sensory-motor axonal neuropathy (CSMAN) (n = 30), chronic inflammatory demyelinating polyneuropathy (CIDP) (n = 30), multifocal motor neuropathy (MMN) (n = 30), and primary muscular spinal atrophy (PMSA) (n = 15). GFAP levels, expressed as optical density, were increased in CSMAN (median = 1.05) compared to controls (median = 0.41; P < 0.05) and CIDP (median = 0.53, P < 0.05). They were also increased in PMSA (median = 0.99) compared to controls (P < 0.05) and MMN (median = 0.66; P < 0.05). To differentiate CSMAN from CIDP and PMSA from MMN, we applied a cutoff of GFAP levels at 0.66, and we obtained good sensitivity and specificity. In neuropathies, serum GFAP correlated with summated sensory nerve action potential amplitudes (r = -0.57; P = 0.0006) and disease severity (r = 0.37; P = 0.0011). Thus, we propose serum GFAP as a marker of axonal damage and severity in chronic neuropathies.

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Section: Discussionsupporting

confidence: 92%

Section: Methodsmentioning

confidence: 99%

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Glial fibrillary acidic protein as a marker of axonal damage in chronic neuropathies

et al. 2009

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“…A recent report indicates that GFAP is elevated in serum (and CSF) of patients with both axonal and demyelinating forms of GuillainBarré syndrome (49), an adult-onset autoimmune disorder of the PNS of unknown etiology. It would be interesting to search for elevations of serum GFAP in other disorders where there are suspected abnormalities of peripheral GFAP-expressing cells, such as inflammatory bowel disease (50).…”

Section: Gfap and Potential Links To Gigaxonin?mentioning

confidence: 99%

Dysfunctions of neuronal and glial intermediate filaments in disease

Liem

Messing²

2009

J. Clin. Invest.

125

100

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Intermediate filaments (IFs) are abundant structures found in most eukaryotic cells, including those in the nervous system. In the CNS, the primary components of neuronal IFs are α-internexin and the neurofilament triplet proteins. In the peripheral nervous system, a fifth neuronal IF protein known as peripherin is also present. IFs in astrocytes are primarily composed of glial fibrillary acidic protein (GFAP), although vimentin is also expressed in immature astrocytes and some mature astrocytes. In this Review, we focus on the IFs of glial cells (primarily GFAP) and neurons as well as their relationship to different neurodegenerative diseases.

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“…GFAP is a monomeric intermediate filament protein expressed in the cytoskeleton of mature astrocytes and outside the CNS in mature non-myelin-forming Schwann cells (Notturno et al 2008). These proteins are not found, or only at a much lower level, in myelin-forming Schwann cells (Jessen et al 1990).…”

Section: Antibodiesmentioning

confidence: 99%

Neuroimmune connections in ovine pharyngeal tonsil: potential site for prion neuroinvasion

et al. 2012

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Recent studies have established the involvement of nasal-associated lymphoid tissues, mainly the pharyngeal tonsil, in prion pathogenesis. However, the mechanisms of the associated neuroinvasion are still debated. To determine potential sites for prion neuroinvasion inside the ovine pharyngeal tonsil, the topography of heavy (200 kDa) and light (70 kDa) neurofilaments and of glial fibrillar acidic protein has been semi-quantitatively analysed inside the various compartments of the tonsil. The results show that the most innervated areas are the interfollicular area and the connective tissue located beneath the respiratory epithelium. The existence of rare synapses between follicular dendritic cells and nerve fibres inside the germinal centre indicates that this mechanism of neuroinvasion is possible but, since germinal centres of lymphoid follicles are poorly innervated, other routes of neuroinvasion are likely. The host PRNP genotype does not influence the pattern of innervation in these various tonsil compartments, unlike ageing during which an increase of nerve endings occurs in a zone of high trafficking cells beneath the respiratory epithelium. A minimal age-related increase of innervation inside the lymphoid follicles has also been observed. An increase in nerve fibre density around the lymphoid follicles, in an area rich in mobile cells such as macrophages and dendritic cells capable of capturing and conveying pathogen prion protein (PrPd), might ensure more efficient infectivity, not in the early phase but in the advanced phase of lymphoinvasion after the amplification of PrPd; alternatively, this area might even act as a direct site of entry during neuroinvasion.

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Glial fibrillary acidic protein: A marker of axonal Guillain–Barrè syndrome and outcome

Cited by 21 publications

References 31 publications

Glial fibrillary acidic protein as a marker of axonal damage in chronic neuropathies

Glial fibrillary acidic protein as a marker of axonal damage in chronic neuropathies

Dysfunctions of neuronal and glial intermediate filaments in disease

Neuroimmune connections in ovine pharyngeal tonsil: potential site for prion neuroinvasion

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