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Record W2413403500 · doi:10.1007/978-1-60327-003-8_8

Cell-Based Identification of Natural Substrates and Cleavage Sites for Extracellular Proteases by SILAC Proteomics

2009· article· en· W2413403500 on OpenAlexaff
Magda Gioia, Leonard J. Foster, Christopher M. Overall

Bibliographic record

VenueMethods in molecular biology · 2009
Typearticle
Languageen
FieldChemistry
TopicAdvanced Proteomics Techniques and Applications
Canadian institutionsUniversity of British Columbia
Fundersnot available
KeywordsStable isotope labeling by amino acids in cell cultureProteolysisProteaseProteasesBiochemistryProteomeBiologyProteomicsExtracellularChemistryCell biologyEnzyme

Abstract

fetched live from OpenAlex

Proteolysis is one of the most important post-translational modifications of the proteome with every protein undergoing proteolysis during its synthesis and maturation and then upon inactivation and degradation. Extracellular proteolysis can either activate or inactivate bioactive molecules regulating physiological and pathological processes. Therefore, it is important to develop non-biased high-content screens capable of identifying the substrates for a specific protease. This characterization can also be useful for identifying the nodes of intersection between a protease and cellular pathways and so aid in the detection of drug targets. Classically, biochemical methods for protease substrate screening only discover what can be cleaved but this is often not what is actually cleaved in vivo. We suggest that biologically relevant protease substrates can be best found by analysis of proteolysis in a living cellular context, starting with a proteome that has never been exposed to the activity of the examined protease. Therefore, protease knockout cells form a convenient and powerful system for these screens. We describe a method for identification and quantification of shed and secreted cleaved substrates in cell cultures utilizing the cell metabolism as a labelling system. SILAC (stable isotope labelling by amino acids) utilises metabolic incorporation of stable isotope-labelled amino acids into living cells. As a model system to develop this approach, we chose the well-characterised matrix metalloproteinase, MMP-2, because of its importance in tumour metastasis and a large database of MMP substrates with which to benchmark this new approach. However, the concepts can be applied to any extracellular or cell membrane protease. Generating differential metabolically labelled proteomes is one key to the approach; the other is the use of a negative peptide selection procedure to select for cleaved N-termini in the N-terminome. Using proteomes exposed or not to a particular protease enables biologically relevant substrates and their cleavage sites to be identified and quantified by tandem mass spectrometry proteomics and database searching.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Methods · Consensus signal: Methods
Teacher disagreement score0.131
Threshold uncertainty score0.569

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.014
GPT teacher head0.366
Teacher spread0.352 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreMethods

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations19
Published2009
Admission routes1
Has abstractyes

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