Comprehensive two‐dimensional gel protein databases offer a global approach to the analysis of human cells: The transformed amnion cells (AMA) master database and its link to genome DNA sequence data
- 1 January 1990
- journal article
- research article
- Published by Wiley in Electrophoresis
- Vol. 11 (12), 989-1071
- https://doi.org/10.1002/elps.1150111202
Abstract
A total of 3430 polypeptides (2592 cellular; 838 secreted) from transformed human amnion cells (AMA) labeled with [35S]methionine were separated and recorded using computer-aided two-dimensional (2-D) gel electrophoresis. A master 2-D gel database of cellular protein information that includes both qualitative and quantitative annotations has been established. The protein numbers in this database differ from those reported in an earlier version (Celis et al. Leukemia 1988,2, 561–602) as a result of changes in the scanning hardware. The reported information includes: percentage of total radioactivity recovered from the gels (based on quantitations of polypeptides labeled with a mixture of 16 14C-amino acids), protein name (including credit to investigators that aided identification), antibody against protein, cellular localization, (nuclear, 40S hnRNP, 20S snRNP U5, proteasomes, endoplasmic reticulum, mitochondria, Golgi, ribosomes, intermediate filaments, microfilaments and microtubules), levels in fetal human tissues, partial protein sequences (containing information on 48 human proteins microsequenced so far), cell cycle-regulated proteins, proteins sensitive to interferons α, β, and γ, heat shock proteins, annexins and phosphorylated proteins. The results presented should be considered as the initial phase of a joint effort between our laboratories to undertake a general and systematic analysis of human proteins. Using this integrated approach it will be possible to identify phenotype-specific proteins, to microsequence them and store the information in the database, to identify the corresponding genes, to search for homology with previously characterized proteins and to study the function of groups of proteins (pathways, organelles, etc.) that exhibit interesting regulatory properties. In particular, the 2-D gel protein database may become increasingly important in view of the concerted effort to map and sequence the entire human genome.Keywords
This publication has 84 references indexed in Scilit:
- Isolation and characterization of a molecular cDNA clone of a human mRNA from interferon-treated cells encoding nucleolar protein B23, numatrinBiochemical and Biophysical Research Communications, 1989
- Comprehensive, human cellular protein databases and their implication for the study of genome organization and functionFEBS Letters, 1989
- Cell cycle-associated change in the expression of the proliferation-sensitive and heat-shock protein hs × 70 (IEF14): Increased synthesis during mitosisExperimental Cell Research, 1988
- Molecular cloning of cDNA coding for human PGP 9.5 proteinFEBS Letters, 1987
- Enhancer-facilitated expression of prokaryotic and eukaryotic genes using human histone gene 5′ regulatory sequencesBiochemistry and Cell Biology, 1986
- Amino acid sequence of equine platelet tropomyosinFEBS Letters, 1983
- Human leukemias: A preliminary 2‐D electrophoretic analysisElectrophoresis, 1982
- Coexistence of three major isoactins in a single sarcoma 180 cellCell, 1981
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970