PXD000570

PXD000570 is an original dataset announced via ProteomeXchange.

Title	Substrate specificity divergence of granzyme tryptases.
Description	Elucidating the true physiological functions of granzymes has been challenging since the origin of the granzyme studied, the use of non-physiological granzyme concentrations and the interspecies use of granzymes, with extrapolation of all these data to orthologous granzymes has led to inconsistencies. This is highly relevant for granzymes A and K where a debate is ongoing concerning their involvement in either cytotoxic or inflammatory processes, or in both. In order to tackle such contradictions, detailed knowledge of the substrate repertoires and substrate specificities of granzymes as well as their cleavage efficiencies may add in unraveling the primary signaling pathways these granzymes are involved in. Therefore, a degradome analysis using N-terminal COFRADIC was performed to unravel the substrate repertoires and subsite determinants for the closely related homologous human tryptases. We furthermore also profiled the uncharacterized mouse granzyme K in a comparative analysis with its human ortholog. Despite the subtle differences observed in the primary specificity profiles of these granzymes, for each granzyme distinguishing substrate subsite features could be elucidated.
HostingRepository	PRIDE
AnnounceDate	2015-09-30
AnnouncementXML	Submission_2015-09-30_05:38:58.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD000570
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Pieter-Jan De Bock
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	L-methionine sulfoxide: 15.994915; 6x(13)C: 4x(15)N labeled L-arginine; 2-pyrrolidone-5-carboxylic acid (Gln): -17.026549; monohydroxylated residue: 15.994915; 6x(13)C labeled residue: 6.020129; iodoacetamide derivatized residue: 57.021464; N-acetylated residue: 42.010565; acetate labeling reagent (N-term) (heavy form: +3amu)
Instrument	LTQ Orbitrap; instrument model: LTQ-Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2013-11-06 05:19:26	ID requested
⏵ 1	2015-09-30 05:38:59	announced

Plasman K, Demol H, Bird PI, Gevaert K, Van Damme P, Substrate specificities of the granzyme tryptases A and K. J Proteome Res, 13(12):6067-77(2014) [pubmed]

curator keyword: Biological

submitter keyword: N-terminal COFRADIC, granzyme, protease, proteomics, specificity profile

Kris Gevaert
contact affiliation	Ghent University, VIB
contact email	kris.gevaert@vib-ugent.be
lab head
Pieter-Jan De Bock
contact affiliation	Biochemistry
contact email	pieter-jan.debock@cea.fr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD000570
     1. Label: PRIDE project
     2. Name: Substrate specificity divergence of granzyme tryptases.