SILAC Quantitative Proteomics and Biochemical Analyses Reveal a Novel Molecular Mechanism by Which ADAM12S Promotes the Proliferation, Migration, and Invasion of Small Cell Lung Cancer Cells through Upregulating Hexokinase 1.

Small cell lung cancer (SCLC) accounts for ∼14% of total lung cancer, which is the worldwide leading cause of morbidity and mortality in cancer. Although SCLC can be treated with chemotherapy and radiotherapy, its 5 year survival rate is still below 7%. Therefore, it is essential to discover new molecules and elucidate the underlying mechanisms modulating the tumorigenesis and metastasis of SCLC for the unmet medical needs.

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

Unlabelled: 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.

Simultaneous enzymatic activity modulation and rapid determination of enzyme kinetics by highly crystalline graphite dots.

The research field in enzyme-based biotechnology urgently requires the discovery of new materials and methods with high-performance. Here we report that highly crystalline graphite dots (GDs) can modulate enzyme activities, and simultaneously allow for real-time measurements on enzyme kinetics in combination with mass spectrometry (MS). A well-defined modulation of lipolytic activities from inhibition to enhancement can be realized by selectively coupling lipase enzymes with GDs containing specific functional groups on the surface.

Quantitative proteomics identifies myoferlin as a novel regulator of A Disintegrin and Metalloproteinase 12 in HeLa cells.

Unlabelled: A Disintegrin and Metalloproteinase 12 (ADAM12) is expressed significantly higher in multiple tumors than in normal tissues and has been used as a prognostic marker for the evaluation of cancer progression. Although several ADAM12 substrates have been identified biochemically and its proteolytic function has been explored, the upstream regulators and the interacting proteins have not been systematically investigated. Here, we use immunoprecipitation and mass spectrometry (MS)-based quantitative proteomic approaches to identify 28 interacting partners for the long form of ADAM12 (ADAM12-L) in HeLa cells.