Combined proteomic approach with SELDI-TOF-MS and peptide mass fingerprinting identified the rapid increase of monomeric transthyretin in rat cerebrospinal fluid after transient focal cerebral ischemia

Suzuyama, Kenji; Shiraishi, Tetsuya; Oishi, Tsuyoshi; Ueda, Shigeo; Okamoto, Hiroaki; Furuta, Makoto; Mineta, Toshihiro

doi:10.1016/j.molbrainres.2004.06.021

Cited by 27 publications

(19 citation statements)

References 35 publications

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“…Traumatic brain injury induces a 1.8-fold increase in hippocampal transthyretin expression (Long et al 2003). Proteomic analyses of rat cerebrospinal fluid after induction of transient cerebral ischemia also found increased presence of transthyretin during the acute phase of ischemia (Suzuyama et al 2004).…”

Section: Transthyretin In Naïve Pkc Mutantsmentioning

confidence: 92%

Microarray Analysis of the Effects of a γ-protein Kinase C Null Mutation on Gene Expression in Striatum: A Role for Transthyretin in Mutant Phenotypes

Smith

Bowers²,

Radcliffe

et al. 2006

Behav Genet

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A constitutive null mutation of the neural-specific isotype of protein kinase C (gamma-PKC) in mice produces alterations in behavioral traits and responses to ethanol suggesting that gamma-PKC-mediated phosphorylation is essential for regulation of some behaviors. However, it is possible that some of the effects of gamma-PKC gene deletion also may be due to altered gene expression. To examine alterations in gene expression, microarray analyses were performed on striatal tissue from wild types and mutants. A total of 143 genes and ESTs were identified as potential candidates related to differences between null mutants and wild types. Confirmation studies using qRT-PCR indicated that the expression of transthyretin was increased about 8-fold in striatum of naïve mutants compared to wild types. The effect of chronic ethanol treatment on transthyretin expression was analyzed because gamma-PKC mutants do not develop tolerance to chronic ethanol treatment. Ethanol treatment of mutants reversed the dramatic increase in transthyretin expression seen in naïve and control-diet treated mutants, but did not affect transthyretin expression in wild types.

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Section: Transthyretin In Naïve Pkc Mutantsmentioning

confidence: 92%

Microarray Analysis of the Effects of a γ-protein Kinase C Null Mutation on Gene Expression in Striatum: A Role for Transthyretin in Mutant Phenotypes

Smith

Bowers²,

Radcliffe

et al. 2006

Behav Genet

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“…TTR was identified as being differentially expressed in fluids or tissues after ischemia (97)(98)(99)) and a mice model of permanent middle cerebral artery occlusion (pMCAO) showed TTR as a neuroprotective molecule. TTR null mice heterozygous for heatshock transcription factor 1 (HSF1) (TTR -/-/HSF1/ +/-) presented increased infarct area, cerebral edema and microglial-leukocyte response when compared with TTR wild-type animals (TTR +/+ /HSF +/-), 24h after pMCAO.…”

Section: Cerebral Ischemiamentioning

confidence: 99%

Transthyretin: a multifaceted protein

Vieira¹,

Saraiva²

2014

BioMolecular Concepts

148

120

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Transthyretin is a highly conserved homotetrameric protein, mainly synthetized by the liver and the choroid plexus of brain. The carrier role of TTR is well-known; however, many other functions have emerged, namely in the nervous system. Behavior, cognition, neuropeptide amidation, neurogenesis, nerve regeneration, axonal growth and 14-3-3ζ metabolism are some of the processes where TTR has an important role. TTR aggregates are responsible for many amyloidosis such as familial amyloidotic polyneuropathy and cardiomyopathy. Normal TTR can also aggregate and deposit in the heart of old people and in preeclampsia placental tissue. Differences in TTR levels have been found in several neuropathologies, but its neuroprotective role, until now, was described in ischemia and Alzheimer's disease. The aim of this review is to stress the relevance of TTR, besides its well-known role on transport of thyroxine and retinol-binding protein.

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“…Surface enhanced laser desorption/ ionization-time of flight mass spectrometry (SELDI-TOF-MS) is an analytical technology for proteomic analysis that combines chromatography and mass spectrometry. Suzuyama et al [7] found an ischemia-induced marker monometric transthyretin in cerebrospinal fluid using SELDI-TOF-MS. This technology has also been utilized in brain tissue, but never in the ischemic core and penumbra of focal ischemia model.…”

Section: Introductionmentioning

confidence: 99%

Regional and Temporal Changes in Proteomic Profile after Middle Cerebral Artery Occlusion with or without Reperfusion in Rats

et al. 2009

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Although DNA microarray studies showed up-regulation of various genes, failures of translation of many genes are expected to occur under ischemic conditions even in the penumbra with mild reduction in cerebral blood flow. We applied surface enhanced laser desorption/ionization-time of flight mass spectrometry (SELDI-TOF-MS) technology to study proteomic profile at 6, 12, and 24 h after photothrombotic middle cerebral artery (MCA) occlusion with or without YAG laser-induced reperfusion in adult male spontaneously hypertensive rats. Of the 43 protein peaks that differed from the sham-operation group with a criterion (no overlap of peak intensities between the two groups), 36 peaks (84%) were down-regulated, and seven were up-regulated. All increased peaks showed greater than twofold increases (up to 8.1 fold) compared with those in the sham-operation group. Effects of reperfusion were observed mainly at 24 h after 1 h of MCA occlusion only in the penumbra, where 23 of 32 peaks returned toward the control values, whereas none of 33 peaks showed such attenuation in the ischemic core. Major ischemia-induced changes in protein peaks detected with SELDI-TOF-MS were down-regulations. The present study showed that dynamic changes of protein profile were associated with progression and recovery of the ischemic core and penumbra.

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Combined proteomic approach with SELDI-TOF-MS and peptide mass fingerprinting identified the rapid increase of monomeric transthyretin in rat cerebrospinal fluid after transient focal cerebral ischemia

Cited by 27 publications

References 35 publications

Microarray Analysis of the Effects of a γ-protein Kinase C Null Mutation on Gene Expression in Striatum: A Role for Transthyretin in Mutant Phenotypes

Microarray Analysis of the Effects of a γ-protein Kinase C Null Mutation on Gene Expression in Striatum: A Role for Transthyretin in Mutant Phenotypes

Transthyretin: a multifaceted protein

Regional and Temporal Changes in Proteomic Profile after Middle Cerebral Artery Occlusion with or without Reperfusion in Rats

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