Proteomics

Dataset Information

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Identification of ADAM12S-interacting proteins in HeLa cells


ABSTRACT: ADAM12 is an A Disintegrin And Metalloproteinases (ADAMs). It is composed of signaling sequence, prodomain, metalloproteinase, disintegrin, cysteine-rich, EGF-like, transmembrane domains, and a cytoplasmic tail. ADAM12 is highly expressed in multiple cancers and is a diagnostic and prognostic biomarker for the proliferation, migration, and invasion of cancer cells. ADAM12 has several isoforms resulted from splicing variants with different subcellular localization and biological functions. Two most important isoforms are the prototype membrane-anchored long isoform ADAM12L and the secreted short isoform ADAM12S. Both of them contain the N-terminal 704 amino acids while their C-termini are different with each other. ADAM12S has extra 34 amino acids at its C-terminus, which replace the 171-amino acid transmembrane and cytoplasmic tail in ADAM12L. In this work, we use immunoprecipitation and quantitative proteomics to identify the interacting proteins of the short form of ADAM12 (ADAM12S).

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Early Embryonic Cell, Hela Cell

DISEASE(S): Cervix Carcinoma

SUBMITTER: lipeng xiong  

LAB HEAD: Guoqiang Xu

PROVIDER: PXD009078 | Pride | 2022-02-28

REPOSITORIES: Pride

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Publications

Quantitative proteomics and biochemical analyses reveal the role of endoplasmin in the regulation of the expression and secretion of A Disintegrin And Metalloproteinase 12.

Xiong Lipeng L   Yan Wenwen W   Zubia Emmanuel E   Zhou Yanqing Y   Zhang Yang Y   Duan Qianqian Q   Narayan Mahesh M   Xu Guoqiang G  

Journal of proteomics 20180502


A Disintegrin And Metalloproteinase 12 (ADAM12) is highly expressed in multiple cancers such as breast and cervical cancers and its high expression reduces the overall patient survival rate. ADAM12 has two major splicing variants, the long membrane-anchored form ADAM12L and the short secreted form ADAM12S. However, how they are regulated and whether they are modulated similarly or differently in cells are not clear. Here, we use affinity purification and mass spectrometry to identify the ADAM12S  ...[more]

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