iTRAQ-based quantitative analysis of hippocampal postsynaptic density-associated proteins in a rat chronic mild stress model of depression

Han, Xiaojian; Shao, Wei; Liu, Z.; Fan, ST; Yu, Jia; Chen, Jiayu; Qiao, Rui; Zhou, Jian; Xie, Peng

doi:10.1016/j.neuroscience.2015.04.006

Cited by 64 publications

(44 citation statements)

References 60 publications

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“…6b,c). This observation held true when the vPSD was obtained by comparing zebrafish PSD proteins with human53233, mouse383940 and rat34353637 PSD proteomes (median vPSD protein identity 66% and median mammalian-specific PSD protein identity 61.5%; significantly different, Mann–Whitney U -test, P <0.0001). Fifth, we asked whether the species-specific PSD (Zf-sPSD and Mm-sPSD) proteins also showed this high conservation, and found that they were significantly lower, even when compared with whole-brain proteomes (Fig.…”

Section: Resultsmentioning

confidence: 85%

Evolution of complexity in the zebrafish synapse proteome

et al. 2017

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The proteome of human brain synapses is highly complex and is mutated in over 130 diseases. This complexity arose from two whole-genome duplications early in the vertebrate lineage. Zebrafish are used in modelling human diseases; however, its synapse proteome is uncharacterized, and whether the teleost-specific genome duplication (TSGD) influenced complexity is unknown. We report the characterization of the proteomes and ultrastructure of central synapses in zebrafish and analyse the importance of the TSGD. While the TSGD increases overall synapse proteome complexity, the postsynaptic density (PSD) proteome of zebrafish has lower complexity than mammals. A highly conserved set of ∼1,000 proteins is shared across vertebrates. PSD ultrastructural features are also conserved. Lineage-specific proteome differences indicate that vertebrate species evolved distinct synapse types and functions. The data sets are a resource for a wide range of studies and have important implications for the use of zebrafish in modelling human synaptic diseases.

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Section: Resultsmentioning

confidence: 85%

Evolution of complexity in the zebrafish synapse proteome

et al. 2017

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“…Modifications of the GluN2A-containing NMDARs have been implicated in several pathological conditions including among others cerebral ischemia [148], depression [149][150][151][152][153][154][155][156], anxiety [149,157], schizophrenia [158][159][160][161], and Huntington's disease [162][163][164]. In this review we decided to focus our attention on selected brain disorders in which GluN2A disfunctions is strictly correlated to altered synaptic plasticity, such as epilepsy, Alzheimer's disease, Parkinson's disease, Fragile-X Syndrome, and autism.…”

Section: Role Of Glun2a In Pathological Plasticitymentioning

confidence: 99%

Synaptic GluN2A-Containing NMDA Receptors: From Physiology to Pathological Synaptic Plasticity

Franchini

Carrano

Luca

et al. 2020

IJMS

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N-Methyl-d-Aspartate Receptors (NMDARs) are ionotropic glutamate-gated receptors. NMDARs are tetramers composed by several homologous subunits of GluN1-, GluN2-, or GluN3-type, leading to the existence in the central nervous system of a high variety of receptor subtypes with different pharmacological and signaling properties. NMDAR subunit composition is strictly regulated during development and by activity-dependent synaptic plasticity. Given the differences between GluN2 regulatory subunits of NMDAR in several functions, here we will focus on the synaptic pool of NMDARs containing the GluN2A subunit, addressing its role in both physiology and pathological synaptic plasticity as well as the contribution in these events of different types of GluN2A-interacting proteins.

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“…After 2 h of incubation at room temperature, labeled samples were mixed at equal ratios. Subsequently, labeled peptides were combined and fractionated by strong cation exchange (SCX) chromatography (Han et al, 2015) and desalted on C18 Cartridges (66872-U; Sigma, St. Louis, MO, USA). The dried peptide mixture was reconstituted and acidified with 2 mL buffer A (10 mM KH 2 PO 4 in 25% of ACN, pH 3.0) and loaded onto a column (4.6 × 250 mm).…”

Section: Protein Extraction and Quantification Itraq Labeling And Smentioning

confidence: 99%

Proteomic analysis of the response of porcine adrenal gland to heat stress

Yong

Gong

et al. 2019

Research in Veterinary Science

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A B S T R A C THeat stress (HS) and its associated pathologies are major challenges facing the pig industry in southern China, and are responsible for large economic losses. However, the molecular mechanisms governing the abnormal secretion of HS-responsive hormones, such as glucocorticoids, are not fully understood. The goal of this study was to investigate differentially expressed proteins (DEPs) in the adrenal glands of pigs, and to elucidate changes in the immune neuroendocrine system in pigs following HS. Through a functional proteomics approach, we identified 1202 peptides, corresponding to 415 proteins. Of these, we found 226 DEPs between heat-stressed and control porcine adrenal gland tissue; 99 of these were up-regulated and 127 were down-regulated in response to HS. These DEPs included proteins involved in substrate transport, cytoskeletal changes, and stress responses. Ingenuity Pathway Analysis was used to identify the subcellular characterization, functional pathway involvement, regulatory networks, and upstream regulators of the identified proteins. Functional network and pathway analyses may provide insights into the complexity and dynamics of HS-host interactions, and may accelerate our understanding of the mechanisms of HS.

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iTRAQ-based quantitative analysis of hippocampal postsynaptic density-associated proteins in a rat chronic mild stress model of depression

Cited by 64 publications

References 60 publications

Evolution of complexity in the zebrafish synapse proteome

Evolution of complexity in the zebrafish synapse proteome

Synaptic GluN2A-Containing NMDA Receptors: From Physiology to Pathological Synaptic Plasticity

Proteomic analysis of the response of porcine adrenal gland to heat stress

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