Gelsolin Levels are Increased in the Brain as a Function of Age During Normal Development in Children That are Further Increased in Down Syndrome

Ji, Lina; Chauhan, Abha; Muthaiyah, Balu; Węgiel, Jerzy; Chauhan, Ved

doi:10.1097/wad.0b013e31819d494e

Cited by 11 publications

(9 citation statements)

References 23 publications

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“…TPMs are capable of annealing gelsolin-severed actin filaments and are efficient in converting gelsolin-actin complexes into long actin filaments (Nyakern-Meazza et al, 2002). TPM and gelsolin levels increase during stress conditions in vitro and during AD progression, suggesting that both TPM and gelsolin are involved in the disease progression (Ji et al, 2009;Owen et al, 2009). The current study showed an increase in WGA affinity for TPM1 and TPM2 and a decrease in WGA affinity for gelsolin.…”

Section: Cytoskeletal and Cytoskeletal Maintenance Proteinsmentioning

confidence: 97%

The wheat germ agglutinin‐fractionated proteome of subjects with Alzheimer's disease and mild cognitive impairment hippocampus and inferior parietal lobule: Implications for disease pathogenesis and progression

Domenico

Owen

Sultana

et al. 2010

J of Neuroscience Research

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Lectin affinity chromatography is a powerful separation technique that fractionates proteins by selectively binding to specific carbohydrate moieties characteristic of protein glycosylation type. Wheat germ agglutinin (WGA) selectively binds terminal N-acetylglucosamine (O-GlcNAc) and sialic acid moieties characteristic of O-linked glycosylation. The current study utilizes WGA affinity chromatography to fractionate proteins from hippocampus and inferior parietal lobule (IPL) from subjects with Alzheimer's disease (AD) and arguably its earliest form, mild cognitive impairment (MCI). Proteins identified by proteomics that were fractionated from MCI and AD hippocampus by WGA affinity chromatography with altered levels compared with age-matched controls included GP96, γ-enolase, glutamate dehydrogenase, glucosidase IIα, 14-3-3ϵ, 14-3-3γ, 14-3-3ζ, tropomyosin-2, calmodulin 2, gelsolin, β-synuclein, α1-antichymotrypsin, and dimethylguanosine tRNA methyltransferase. Proteins identified by proteomics that were fractionated from MCI and AD IPL by WGA affinity chromatography showing altered levels compared with age-matched controls included protein disulfide isomerase, calreticulin, and GP96. The proteins described in this study are involved in diverse processes, including glucose metabolism, endoplasmic reticulum (ER) functions, chaperoning, cytoskeletal assembly, and proteolysis, all of which are affected in AD. This study, the first to use proteomics to identify WGA-fractionated proteins isolated from brains from subjects with MCI and AD, provides additional information about the active proteome of the brain throughout AD progression.

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Section: Cytoskeletal and Cytoskeletal Maintenance Proteinsmentioning

confidence: 97%

The wheat germ agglutinin‐fractionated proteome of subjects with Alzheimer's disease and mild cognitive impairment hippocampus and inferior parietal lobule: Implications for disease pathogenesis and progression

Domenico

Owen

Sultana

et al. 2010

J of Neuroscience Research

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“…Gelsolin mutations are also linked to Alzheimer’s and Parkinson’s diseases [347]. In addition, subjects with Down syndrome exhibited an increase in gelsolin levels in developing frontal cortex, and levels of gelsolin were shown to rise with aging in control subjects [348]. The ability of gelsolin to bind and sever F-actin and to cap fast-growing barbed ends, as well as to nucleate filament polymerization, supports its role in mediating actin remodeling in dendritic spines.…”

Section: Proteins Regulating Actin Dynamics In Dendritic Spinesmentioning

confidence: 99%

Accelerators, Brakes, and Gears of Actin Dynamics in Dendritic Spines

Pontrello

Ethell

2009

TONEURJ

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Dendritic spines are actin-rich structures that accommodate the postsynaptic sites of most excitatory synapses in the brain. Although dendritic spines form and mature as synaptic connections develop, they remain plastic even in the adult brain, where they can rapidly grow, change, or collapse in response to normal physiological changes in synaptic activity that underlie learning and memory. Pathological stimuli can adversely affect dendritic spine shape and number, and this is seen in neurodegenerative disorders and some forms of mental retardation and autism as well. Many of the molecular signals that control these changes in dendritic spines act through the regulation of filamentous actin (F-actin), some through direct interaction with actin, and others via downstream effectors. For example, cortactin, cofilin, and gelsolin are actin-binding proteins that directly regulate actin dynamics in dendritic spines. Activities of these proteins are precisely regulated by intracellular signaling events that control their phosphorylation state and localization. In this review, we discuss how actin-regulating proteins maintain the balance between F-actin assembly and disassembly that is needed to stabilize mature dendritic spines, and how changes in their activities may lead to rapid remodeling of dendritic spines.

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“…In contrast, plasma gelsolin was significantly decreased in the mesenteric lymph following hemorrhagic shock (Jordan et al, 2007) and sepsis (Lee et al, 2008). It was noteworthy that gelsolin level was elevated in various neurodegenerative diseases, such as Down's syndrome (Ji et al, 2009a), whereas it was decreased in the blood and cerebrospinal fluid of multiple sclerosis subjects, strongly suggesting its role in the development of neurodegeneration associated with chronic inflammation (Kulakowska et al, 2010).…”

Section: Introductionmentioning

confidence: 92%