Variations on the theme of genomics

Woolf, Tod M.; Taylor, Margaret

doi:10.1016/s0168-9525(98)01502-9

Cited by 3 publications

(2 citation statements)

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“…For the reasons described above, we have the initiation of the (eventually) complete profile of the rat liver mitochondrial proteome using the techniques of high-throughput proteomics coupled with a novel affinity fractionation technique using minispin columns. To date, there are only two published reports of mitochondrial protein profiling using proteomic techniques [49,50]. It is estimated (from genomic data) that the complete mitochondrial proteome may consist of approximately 1500 distinct proteins, many of which may exist in multiple isoforms due to post-translational modifications.…”

Section: Introductionmentioning

confidence: 99%

High-throughput profiling of the mitochondrial proteome using affinity fractionation and automation

Lopez¹,

et al. 2000

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Recent studies have demonstrated the need for complementing cellular genomic information with specific information on expressed proteins, or proteomics, since the correlation between the two is poor. Typically, proteomic information is gathered by analyzing samples on two-dimensional gels with the subsequent identification of specific proteins of interest by using trypsin digestion and mass spectrometry in a process termed peptide mass fingerprinting. These procedures have, as a rule, been labor-intensive and manual, and therefore of low throughput. The development of automated proteomic technology for processing large numbers of samples simultaneously has made the concept of profiling entire proteomes feasible at last. In this study, we report the initiation of the (eventual) complete profile of the rat mitochondrial proteome by using high-throughput automated equipment in combination with a novel fractionation technique using minispin affinity columns. Using these technologies, approximately one hundred proteins could be identified in several days. In addition, separate profiles of calcium binding proteins, glycoproteins, and hydrophobic or membrane proteins could be generated. Because mitochondrial dysfunction has been implicated in numerous diseases, such as cancer, Alzheimer's disease and diabetes, it is probable that the identification of the majority of mitochondrial proteins will be a beneficial tool for developing drug and diagnostic targets for associated diseases.

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Section: Introductionmentioning

confidence: 99%

High-throughput profiling of the mitochondrial proteome using affinity fractionation and automation

Lopez¹,

et al. 2000

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“…Electrophoresis 2000, 21, 1082±1093 Optimizing proteome analysis through automation 1083 [50], endosomes [51,52], rough endoplasmic reticulum (ER), plasma and mitochondrial membrane [53], mitochondrialribosomes [54],centrosomes [55],andcyanobacterialthylakoidmembranes [56].…”

Section: Automation As An Approach To Increasing Throughputmentioning

confidence: 99%

Better approaches to finding the needle in a haystack: Optimizing proteome analysis through automation

Lopez¹

2000

Electrophoresis

112

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Applied Proteomics

Lopez

Melov

2002

Circulation Research

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Abstract-The identification of a majority of the polypeptides in mitochondria would be invaluable because they play crucial and diverse roles in many cellular processes and diseases. The endogenous production of reactive oxygen species (ROS) is a major limiter of life as illustrated by studies in which the transgenic overexpression in invertebrates of catalytic antioxidant enzymes results in increased lifespans. Mitochondria have received considerable attention as a principal source-and target-of ROS. Mitochondrial oxidative stress has been implicated in heart disease including myocardial preconditioning, ischemia/reperfusion, and other pathologies. In addition, oxidative stress in the mitochondria is associated with the pathogenesis of Alzheimer's disease, Parkinson's disease, prion diseases, and amyotrophic lateral sclerosis (ALS) as well as aging itself. The rapidly emerging field of proteomics can provide powerful strategies for the characterization of mitochondrial proteins. Current approaches to mitochondrial proteomics include the creation of detailed catalogues of the protein components in a single sample or the identification of differentially expressed proteins in diseased or physiologically altered samples versus a reference control. It is clear that for any proteomics approach prefractionation of complex protein mixtures is essential to facilitate the identification of low-abundance proteins because the dynamic range of protein abundance within cells has been estimated to be as high as 10 7 . The opportunities for identification of proteins directly involved in diseases associated with or caused by mitochondrial dysfunction are compelling. Future efforts will focus on linking genomic array information to actual protein levels in mitochondria. (Circ Res. 2002;90:380-389.)

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Variations on the theme of genomics

Cited by 3 publications

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High-throughput profiling of the mitochondrial proteome using affinity fractionation and automation

High-throughput profiling of the mitochondrial proteome using affinity fractionation and automation

Better approaches to finding the needle in a haystack: Optimizing proteome analysis through automation

Applied Proteomics

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