Synemin isoforms during mouse development: Multiplicity of partners in vascular and neuronal systems

Izmiryan, Araksya; Franco, Cláudio A.; Paulin, Denise; Li, Zhenlin; Xue, Zhigang

doi:10.1016/j.yexcr.2008.12.009

Cited by 23 publications

(32 citation statements)

References 55 publications

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“…An exception is the protein synemin. First identified as a high-molecular-mass protein associated with desmin and vimentin filaments in muscle (Granger and Lazarides, 1980), synemin expression was later detected in different tissues and cell types, including the nervous system, endothelial cells, retinal cells and hepatic stellate cells (Hirako et al, 2003;Izmiryan et al, 2006;Izmiryan et al, 2009;Izmiryan et al, 2010;Schmitt-Graeff et al, 2006;Tawk et al, 2003;Uyama et al, 2006). Three synemin isoforms differing in their C-terminal tails -a-synemin (also known as synemin H, 180 kDa), b-synemin (also known as synemin M, 150 kDa) and synemin L (41 kDa) -are produced by alternative splicing and are differentially regulated during embryonic development (Titeux et al, 2001;Xue et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

“…Consequently, synemin filaments are unstable and delocalised in the cells of mice lacking desmin or vimentin (Carlsson et al, 2000;Izmiryan et al, 2006;Izmiryan et al, 2009;Jing et al, 2007;Xue et al, 2004). Synemin also interacts with a-actinin, plectin 1, zyxin, and three components of the dystrophin-associated protein complex, dystrophin, utrophin and a-dystrobrevin (Bellin et al, 1999;Bhosle et al, 2006;Hijikata et al, 2008;Mizuno et al, 2001;Sun et al, 2010a).…”

Section: Introductionmentioning

confidence: 99%

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Synemin acts as a regulator of signalling molecules in skeletal muscle hypertrophy

Li¹,

Parlakian²,

Coletti³

et al. 2014

Journal of Cell Science

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Synemin, a type IV intermediate filament (IF) protein, forms a bridge between IFs and cellular membranes. As an A-kinase-anchoring protein, it also provides temporal and spatial targeting of protein kinase A (PKA). However, little is known about its functional roles in either process. To better understand its functions in muscle tissue, we generated synemin-deficient (Synm 2/2 ) mice. Synm 2/2 mice displayed normal development and fertility but showed a mild degeneration and regeneration phenotype in myofibres and defects in sarcolemma membranes. Following mechanical overload, Synm 2/2 mice muscles showed a higher hypertrophic capacity with increased maximal force and fatigue resistance compared with control mice. At the molecular level, increased remodelling capacity was accompanied by decreased myostatin (also known as GDF8) and atrogin (also known as FBXO32) expression, and increased follistatin expression. Furthermore, the activity of muscle-mass control molecules (the PKA RIIa subunit, p70S6K and CREB1) was increased in mutant mice. Finally, analysis of muscle satellite cell behaviour suggested that the absence of synemin could affect the balance between self-renewal and differentiation of these cells. Taken together, our results show that synemin is necessary to maintain membrane integrity and regulates signalling molecules during muscle hypertrophy.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Synemin acts as a regulator of signalling molecules in skeletal muscle hypertrophy

Li¹,

Parlakian²,

Coletti³

et al. 2014

Journal of Cell Science

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“…Recently, we have showed that synemin is the one of the earliest markers during mouse embryo development [9]. Synemin M mRNA was present as early as E5 with vimentin and nestin.…”

Section: Introductionmentioning

confidence: 99%

“…All three isoforms, with molecular weights 180 (H), 150 (M), and 41 (L) kDa, have the same head and rod domains and differ in their tail domain sequences (Fig. 1, [11][12][13]), but each is expressed in a developmentally specific manner [9,12]. Synemin has also been found in a subpopulation of rat and mouse astrocytes that contains GFAP, vimentin and nestin [10,14], and in mouse lens and the retina [15].…”

Section: Introductionmentioning

confidence: 99%

Synemin Isoforms in Astroglial and Neuronal Cells from Human Central Nervous System

Izmiryan¹,

Peltekian²,

Paulin³

et al. 2009

Neurochem Res

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The intermediate filament (IF) synemin gene encodes three IF proteins (H 180, M 150, L 41 kDa) with overlapping distributions. Synemin M was present early with vimentin and nestin. Synemin H was found later in the nervous system and mesodermic derivatives concomitantly with angiogenesis and the migration of neural crest cells. Synemin L appeared later in neurons. A series of in vitro cell cultures were done to identify the linkage between synemin isoforms and specific cell types of the central nervous system (CNS). The neurons and glia from the brains of humans and rats were cultured and double immunostaining done with antibodies against the H/M or L synemin isoforms and neural cell types (betaIII-tubulin or NeuN) or astrocyte intermediate filaments (GFAP or vimentin). In neurons of the CNS, synemin H/M were co-expressed with GFAP, vimentin or nestin in glial cells, whereas synemin L was found in neurons.

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“…Syncoilin is unlike neuronal IF proteins peripherin and neurofilament, whose isoforms are expressed in the same cell types (Lee et al, 1993;McLean et al, 2008). Instead, the different expressions and potentially different functions of the syncoilin isoforms resemble those of the synemin isoforms, two of which are expressed in glial cells during development and one of which is expressed in mature neurons (Izmiryan et al, 2006;Izmiryan et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

Syncoilin modulates peripherin filament networks and is necessary for large-calibre motor neurons

Clarke

Edwards

McCullagh

et al. 2010

Journal of Cell Science

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SummarySyncoilin is an atypical type III intermediate filament (IF) protein, which is expressed in muscle and is associated with the dystrophinassociated protein complex. Here, we show that syncoilin is expressed in both the central and peripheral nervous systems. Isoform Sync1 is dominant in the brain, but isoform Sync2 is dominant in the spinal cord and sciatic nerve. Peripherin is a type III IF protein that has been shown to colocalise and interact with syncoilin. Our analyses suggest that syncoilin might function to modulate formation of peripherin filament networks through binding to peripherin isoforms. Peripherin is associated with the disease amyotrophic lateral sclerosis (ALS), thus establishing a link between syncoilin and ALS. A neuronal analysis of the syncoilin-null mouse (Sync -/-) revealed a reduced ability in accelerating treadmill and rotarod tests. This phenotype might be attributable to the impaired function of extensor digitorum longus muscle and type IIb fibres caused by a shift from large-to small-calibre motor axons in the ventral root.

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Synemin isoforms during mouse development: Multiplicity of partners in vascular and neuronal systems

Cited by 23 publications

References 55 publications

Synemin acts as a regulator of signalling molecules in skeletal muscle hypertrophy

Synemin acts as a regulator of signalling molecules in skeletal muscle hypertrophy

Synemin Isoforms in Astroglial and Neuronal Cells from Human Central Nervous System

Syncoilin modulates peripherin filament networks and is necessary for large-calibre motor neurons

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