Proteomics

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Mining gastric cancer cellular quantitative phosphotyrosine proteomics data to analyse the signiling cascade regulated my CAMKK2 in gastric cancer


ABSTRACT: Gastric cancer is a global health concern. Tyrosine kinases (TKs) are important mediators of signaling cascades, which regulate diverse biological processes like growth, differentiation, metabolism, and apoptosis in response to external and internal stimuli. Molecular alterations in various signaling pathways have been implicated in the development and late-stage progression/metastasis of gastric cancer. Dysregulation of TK’s are reported to be involved in different malignancies.1 Tyrosine kinases represent a major portion of all oncoproteins that play a transforming role in a plethora of cancers.. This study aimed at analysing the phosphotyrosine proteome change upon inhibition of CAMKK2 in gastric cancer cells using LC-MS/MS based quantitative inhibition proteomic approach. A label free based quantitative approach was used to identify the significantly altered phosphorylations upon inhibition of CAMKK2. Gene Ontology (GO) analysis and pathway analysis was done for the significantly altered proteins and was later validated by immunoblotting.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Gastric Adenocarcinoma Cell, Diploid Cell

DISEASE(S): Gastric Adenocarcinoma

SUBMITTER: Aditi Chatterjee  

LAB HEAD: Aditi chatterjee

PROVIDER: PXD032001 | Pride | 2022-06-09

REPOSITORIES: Pride

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Publications

Tyrosine Phosphorylation Profiling Revealed the Signaling Network Characteristics of CAMKK2 in Gastric Adenocarcinoma.

Najar Mohd Altaf MA   Arefian Mohammad M   Sidransky David D   Gowda Harsha H   Prasad T S Keshava TSK   Modi Prashant Kumar PK   Chatterjee Aditi A  

Frontiers in genetics 20220513


Calcium/calmodulin-dependent protein kinase kinase 2 (CAMKK2) is a serine/threonine protein kinase which functions <i>via</i> the calcium-triggered signaling cascade with CAMK1, CAMK4, and AMPKα as the immediate downstream substrates. CAMKK2 is reported to be overexpressed in gastric cancer; however, its signaling mechanism is poorly understood. We carried out label-free quantitative tyrosine phosphoproteomics to investigate tyrosine-mediated molecular signaling associated with CAMKK2 in gastric  ...[more]

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