The rat brain hippocampus proteome

Fountoulakis, Michael; Tsangaris, George Th.; Maris, Antony; Lubec, Gert

doi:10.1016/j.jchromb.2005.01.037

Cited by 49 publications

(37 citation statements)

References 80 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Murine hippocampal protein profiling yielded in 450 spots displaying 157 different proteins at the most so far [12]. The recent analysis is thus complementing previous studies on the mouse [20,12], rat [15], and human [14] hippocampal proteome.…”

Section: Figuresupporting

confidence: 62%

“…In the search for the biochemical correlates to brain malfunction human samples [8][9][10] as well as samples from genetically engineered animal models for human mental disorders [11][12][13] have been investigated by means of proteomics. Protein profiles of the human [14] and rat [15] hippocampus have been established whereas currently the most comprehensive study on the murine hippocampus reports the identification of 157 different gene products [12]. This leads us to construct a more elaborate reference database of the mouse hippocampus giving consideration to the importance of the mouse as model organism.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

An integrated map of the murine hippocampal proteome based upon five mouse strains

et al. 2006

Self Cite

View full text Add to dashboard Cite

With the advent of proteomics technologies it is possible to simultaneously demonstrate the expression of hundreds of proteins. The information offered by proteomics provides context-based understanding of cellular protein networks and has been proven to be a valuable approach in neuroscience studies. The mouse hippocampus has been a major target of analysis in the search for molecular correlates to neuronal information storage. Although human and rat hippocampal samples have been successfully subjected to proteomic profiling, no elaborate analysis providing the fundamental experimental basis for protein-expression studies in the mouse hippocampus has been carried out as yet. This led us to construct a master map generated from the individual hippocampal proteomes of five different mouse strains. A proteomic approach, based upon 2-DE coupled to MS (MALDI-TOF/TOF) has been chosen in an attempt to establish a comprehensive reference database of proteins expressed in the mouse hippocampus. 469 individual proteins, represented by 1156 spots displaying various functional states of the respective gene products were identified. Proteomic profiling of the hippocampus, a brain region with a pivotal role for neuronal information processing and storage may provide insight into the characteristics of proteins serving this highly sophisticated function.

show abstract

Section: Figuresupporting

confidence: 62%

Section: Introductionmentioning

confidence: 99%

An integrated map of the murine hippocampal proteome based upon five mouse strains

et al. 2006

Self Cite

View full text Add to dashboard Cite

show abstract

“…Published CNS studies utilizing 2-DE reported the identification of nearly 500 proteins either from mouse or human brain [5,6]. In addition, 148, 165 and 38 proteins have been identified in rat hippocampus [7], human hippocampus [8] and pituitary [9], respectively. Although 2-DE has been effective for identifying new proteins and their PTMs, technical limitations confine its application to relatively abundant proteins.…”

mentioning

confidence: 99%

Optimized proteomic analysis of a mouse model of cerebellar dysfunction using amine-specific isobaric tags

Hu¹,

Qian²,

Borisov³

et al. 2006

Proteomics

View full text Add to dashboard Cite

Recent proteomic applications have demonstrated their potential for revealing the molecular mechanisms underlying neurodegeneration. The present study quantifies cerebellar protein changes in mice that are deficient in plasma membrane calcium ATPase 2 (PMCA2), an essential neuronal pump that extrudes calcium from cells and is abundantly expressed in Purkinje neurons. PMCA2-null mice display motor dyscoordination and unsteady gait deficits observed in neurological diseases such as multiple sclerosis and ataxia. We optimized an amine-specific isobaric tags (iTRAQ ™ )-based shotgun proteomics workflow for this study. This workflow took consideration of analytical variance as a function of ion signal intensity and employed biological repeats to aid noise reduction. Even with stringent protein identification criteria, we could reliably quantify nearly 1000 proteins, including many neuronal proteins that are important for synaptic function. We identified 21 proteins that were differentially expressed in PMCA2-null mice. These proteins are involved in calcium homeostasis, cell structure and chromosome organization. Our findings shed light on the molecular changes that underlie the neurological deficits observed in PMCA2-null mice. The optimized workflow presented here will be valuable for others who plan to implement the iTRAQ method.

show abstract

“…In another one-step-for-all extraction study, 30% of identified proteins were membrane and membrane organelle-related proteins (Fountoulakis et al, 2005). Compared to the fact that as high as 90% of proteins (enriched in the insoluble fraction C) belonged to this category in our study, the advantage of current strategy is really impressive.…”

Section: Discussionmentioning

confidence: 58%

Gel-based Proteomic Characterization of Soluble and Insoluble Fraction Proteins in Rat Spinal Cord

Yang¹,

Ding²,

Guo³

et al. 2010

J Proteomics Bioinform

View full text Add to dashboard Cite

Fractionation efficiency and protein characterization of neural soluble and insoluble proteins by sequential extraction was scrutinized by gel-based proteomic analysis. Spinal cord proteins of adult rats were first extracted with aqueous buffer (fraction A), followed by standard (fraction B) or modified (fraction C) enhanced solutions. Of the top 30 most abundant proteins in fractions A, B and C, the percentage of cytoplasmic proteins was 74% (28/38) , 37% (14/38) and 42% (15/36), respectively; membrane organellar proteins accounted for 8% (3/38), 45% (17/38), and 44% (16/36); membrane proteins accounted for 13% (5/38), 18% (7/38) and 14% (5/36). The number of hydrophobic domains was 5, 15 and 9. Shared proteins in three fractions were only 13%. When additional less abundant 30 spots enriched the insoluble fraction C were characterized, membrane proteins accounted for 31%, among which 83% were peripheral membrane proteins and 17% were integral membrane proteins. Functional analysis also revealed some difference between different fractions although all fractionated proteins are involved in energy metabolism, redox regulation, signal transduction and cellular architecture.

show abstract

The rat brain hippocampus proteome

Cited by 49 publications

References 80 publications

An integrated map of the murine hippocampal proteome based upon five mouse strains

An integrated map of the murine hippocampal proteome based upon five mouse strains

Optimized proteomic analysis of a mouse model of cerebellar dysfunction using amine-specific isobaric tags

Gel-based Proteomic Characterization of Soluble and Insoluble Fraction Proteins in Rat Spinal Cord

Contact Info

Product

Resources

About