NOGO is increased and binds to BACE1 in sporadic inclusion-body myositis and in AβPP-overexpressing cultured human muscle fibers

Wójcik, Sławomir; Engel, W. King; Yan, Riqiang; McFerrin, Janis; Askanas, Valerie

doi:10.1007/s00401-007-0281-y

Cited by 35 publications

(24 citation statements)

References 42 publications

(113 reference statements)

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“…A BLAST search of the epitope recognized by Ab-2 reveals little else in the human proteome that Ab-2 would likely react with. The monomer for Nogo-A is 130 kDa but is known to migrate at 180 kDa [20], and can be seen in lanes 1 and 3 for Ab-2 (fig. 2).…”

Section: Resultsmentioning

confidence: 99%

Expression of Nogo-A Is Decreased with Increasing Gestational Age in the Human Fetal Brain

et al. 2012

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Nogo is a member of the reticulon family. Our understanding of the physiological functions of the Nogo-A protein has grown over the last few years, and this molecule is now recognized as one of the most important axonal regrowth inhibitors present in central nervous system (CNS) myelin. Nogo-A plays other important roles in nervous system development, epilepsy, vascular physiology, muscle pathology, stroke, inflammation, and CNS tumors. Since the exact role of Nogo-A protein in human brain development is still poorly understood, we studied its cellular and regional distribution by immunohistochemistry in the frontal lobe of 30 human fetal brains. Nogo-A was expressed in the following cortical zones: ependyma, ventricular zone, subventricular zone, intermediate zone, subplate, cortical plate, and marginal zone. The number of positive cells decreased significantly with increasing gestational age in the subplate and marginal zone. Using different antibodies, changes in isoform expression and dimerization states could be shown between various cortical zones. The results demonstrate a significant change in the expression of Nogo-A during the development of the human brain. The effects of its time- and region-specific regulation have to be further studied in detail.

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Section: Resultsmentioning

confidence: 99%

Expression of Nogo-A Is Decreased with Increasing Gestational Age in the Human Fetal Brain

et al. 2012

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“…These include aBC, a stress-related heat shock protein that recognizes and stabilizes proteins with a propensity to form aggregates and precipitate [39,40], and NOGO-B [41], an integral membrane protein that binds to BACE-1 and blocks its activity by blocking access to APP. APP overexpression in cultured muscle stimulated expression of both proteins [40,41]. The effect of aBC is unclear.…”

Section: Aberrant Protein Accumulation and The Stress Responsementioning

confidence: 99%

Inclusion body myositis: new insights into pathogenesis

Garlepp

Mastaglia²

2008

Current Opinion in Rheumatology

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Understanding the paradoxes in sporadic inclusion body myositis is important in determining rational therapy for the disease. Amyloid precursor protein is expressed in muscle in other inflammatory muscle diseases but the cellular distribution differs and inclusions do not form so that other metabolic defects seem to be important. Intramuscular immune cells influence muscle function and viability in inclusion body myositis but immunotherapy is ineffective. A useful target for therapy may be restoration of muscle regenerating capacity.

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“…Although the fi rst study of this protein in myositis reported an IBM-disease specifi c role [31], the recent study and a prior one [54] found the protein to be nonspecifi cally overexpressed among infl ammatory myopathies. Nogo-B has also been reported as increased in IBM [55]. A 2.5-fold increase was found in whole muscle lysates through immunoblots compared with seven control specimens; however, the diagnoses of the control specimens were not reported (they all could have been normal samples).…”

Section: Protein Studiesmentioning

confidence: 84%

Inclusion body myositis: Review of recent literature

Greenberg

2008

Curr Neurol Neurosci Rep

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Inclusion body myositis (IBM) is a progressive inflammatory skeletal muscle disease of unknown cause and without effective treatment. This article discusses existing literature, emphasizing disease mechanisms and models. In particular, it addresses limitations in the beta-amyloid-mediated theory of IBM myofiber injury, flawed rationales of animal models of this disease, and recent reports regarding treatment.

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NOGO is increased and binds to BACE1 in sporadic inclusion-body myositis and in AβPP-overexpressing cultured human muscle fibers

Cited by 35 publications

References 42 publications

Expression of Nogo-A Is Decreased with Increasing Gestational Age in the Human Fetal Brain

Expression of Nogo-A Is Decreased with Increasing Gestational Age in the Human Fetal Brain

Inclusion body myositis: new insights into pathogenesis

Inclusion body myositis: Review of recent literature

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