Proteomics

Dataset Information

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Proteomic identification of cysteine cathepsin substrates shed from the surface of cancer cells


ABSTRACT: Extracellular cysteine cathepsins are known to drive cancer progression, but besides degradation of extracellular matrix proteins little is known about their physiological substrates and thus the molecular mechanisms they deploy. One of the major mechanisms used by other extracellular proteases to facilitate cancer progression is proteolytic release of the extracellular domains of transmembrane proteins or ectodomain shedding. Here we show using a mass spectrometry-based approach that cathepsins L and S act as sheddases and cleave extracellular domains of CAM adhesion proteins and transmembrane receptors from the surface of cancer cells.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Marko Fonovic  

LAB HEAD: Marko Fonovic

PROVIDER: PXD002192 | Pride | 2015-06-23

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
5XnizjiCatB1.raw Raw
5XnizjiCatB2.raw Raw
5XnizjiCatB3.raw Raw
5XnizjiCatB4.raw Raw
5XnizjiCatB5.raw Raw
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Publications

Proteomic Identification of Cysteine Cathepsin Substrates Shed from the Surface of Cancer Cells.

Sobotič Barbara B   Vizovišek Matej M   Vidmar Robert R   Van Damme Petra P   Gocheva Vasilena V   Joyce Johanna A JA   Gevaert Kris K   Turk Vito V   Turk Boris B   Fonović Marko M  

Molecular & cellular proteomics : MCP 20150616 8


Extracellular cysteine cathepsins are known to drive cancer progression, but besides degradation of extracellular matrix proteins little is known about their physiological substrates and thus the molecular mechanisms they deploy. One of the major mechanisms used by other extracellular proteases to facilitate cancer progression is proteolytic release of the extracellular domains of transmembrane proteins or ectodomain shedding. Here we show using a mass spectrometry-based approach that cathepsins  ...[more]

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