Development of sandwich ELISA for detection and quantification of human and murine a disintegrin and metalloproteinase17

Trad, Ahmad; Hedemann, Nina; Shomali, Mohammad; Pawlak, Verena; Grötzinger, Joachim; Lorenzen, Inken

doi:10.1016/j.jim.2011.06.015

Cited by 26 publications

(38 citation statements)

References 17 publications

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“…9820) was obtained from Cell Signaling. Antibodies against human ADAM17 were described previously (21, 22). Monoclonal antibody (mAb) A300E was used to immunoprecipitate ADAM17, and mAb A300D was used for ADAM17 detection via Western blotting.…”

Section: Methodsmentioning

confidence: 99%

Senescence‐associated release of transmembrane proteins involves proteolytic processing by ADAM17 and microvesicle shedding

et al. 2014

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Cellular senescence, a state of persistent cell cycle arrest, has emerged as a potent tumor suppressor mechanism by restricting proliferation of cells at risk for neoplastic transformation. Senescent cells secrete various growth factors, cytokines, and other proteins that can either elicit the clearance of tumor cells or potentially promote tumor progression. In addition, this senescence-associated secretory phenotype (SASP) includes various factors that are synthesized as transmembrane precursors and subsequently converted into their soluble counterparts. Despite the importance of the SASP to tumor biology, it is virtually unknown how transmembrane proteins are released from senescent cancer cells. Here we show in different models of senescence that the metalloprotease A disintegrin and metalloproteinase 17 (ADAM17) is activated and releases the epidermal growth factor receptor ligand amphiregulin and tumor necrosis factor receptor I (TNFRI) from the surface of senescent cells by ectodomain shedding. ADAM17 activation involves phosphorylation of its cytoplasmic tail by mitogen-activated protein kinase (MAPK) p38. Interestingly, unlike amphiregulin and TNFRI, full-length intercellular adhesion molecule 1 (ICAM1) is released from senescent cells by microvesicles independently of ADAM17. Thus, our results suggest that transmembrane proteins can be released by two distinct mechanisms and point to a crucial role for ADAM17 in shaping the secretory profile of senescent cells.

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Section: Methodsmentioning

confidence: 99%

Senescence‐associated release of transmembrane proteins involves proteolytic processing by ADAM17 and microvesicle shedding

et al. 2014

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“…The anti-ADAM17 mAb (clone A300E) was generated within the antibody facility (Z3 unit) of the CRC877 [28]. It recognizes a membrane proximal cysteine-rich extension of the ADAM17 protein and was extensively tested in comparison to commercially available antibodies for the use in flow cytometry.…”

Section: Methodsmentioning

confidence: 99%

Differential Surface Expression of ADAM10 and ADAM17 on Human T Lymphocytes and Tumor Cells

et al. 2013

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A disintegrin and metalloproteases (ADAMs) have been implicated in many processes controlling organismic development and integrity. Important substrates of ADAM proteases include growth factors, cytokines and their receptors and adhesion proteins. The inducible but irreversible cleavage of their substrates alters cell-cell communication and signaling. The crucial role of ADAM proteases (e.g. ADAM10 and 17) for mammalian development became evident from respective knockout mice, that displayed pre- or perinatal lethality with severe defects in many organs and tissues. Although many substrates for these two ADAM proteases were identified over the last decade, the regulation of their surface appearance, their enzymatic activity and their substrate specificity are still not well understood. We therefore analyzed the constitutive and inducible surface expression of ADAM10 and ADAM17 on a variety of human T cell and tumor cell lines. We demonstrate that ADAM10 is constitutively present at comparably high levels on the majority of the tested cell types. Stimulation with phorbol ester and calcium ionophore does not significantly alter the amount of surface ADAM10, except for a slight down-regulation from T cell blasts. Using FasL shedding as a readout for ADAM10 activity, we show that PKC activation and calcium mobilization are both prerequisite for activation of ADAM10 resulting in a production of soluble FasL. In contrast to ADAM10, the close relative ADAM17 is detected at only low levels on unstimulated cells. ADAM17 surface expression on T cell blasts is rapidly induced by stimulation. Since this inducible mobilization of ADAM17 is sensitive to inhibitors of actin filament formation, we propose that ADAM17 but not ADAM10 is prestored in a subcellular compartment that is transported to the cell surface in an activation- and actin-dependent manner.

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“…The following antibodies were used: TACE (Ab39162, Abcam); TACE Ab318 (monoclonal anti-TACE antibody (Trad et al, 2011) was used for the detection of mouse TACE; alpha-Tubulin (sc-8035, Santa Cruz), alpha-Tubulin (Clone YL1/2, Ana Regaldo, IGC), p97 (Thermo, MA1-21412), HA-HRP (clone 3F10, Roche), HA (clone HA.11, 901501, Biolegend) V5-HRP (R961-25, Life Technologies), Frmd8 (157H00083786-B01P, Abnova), Transferrin Receptor (13-6800, Life Technologies), Flag-HRP (A8592, Sigma), GAPDH (2118, CST), Actin (abcam ab8227). Anti-iRhom2 polyclonal antibodies specific to the mouse iRhom2 N-terminus (amino acids 1-373) or raised against the iRhom homology domain, were previously described (Adrain et al, 2012).…”

Section: Antibodiesmentioning

confidence: 99%

iTAP, a novel iRhom interactor, controls TNF secretion by policing the stability of iRhom/TACE

Oikonomidi

Burbridge

Cavadas

et al. 2018

Preprint

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Abstract. (150 words max)The apical inflammatory cytokine TNF regulates numerous important biological processes including inflammation and cell death, and drives inflammatory diseases. TNF secretion requires ADAM17/TACE, which cleaves TNF from its transmembrane tether, releasing it for signalling. The trafficking of ADAM17/TACE to the cell surface, and stimulation of its proteolytic activity, depends on membrane proteins, called iRhoms. To delineate how the TNF/TACE/iRhom axis is regulated, we performed an immunoprecipitation/mass spectrometry screen to identify iRhom-binding proteins. Here we report a novel protein, that we name iTAP (iRhom tail-associated protein) that binds to iRhoms, enhancing the stability of iRhoms and TACE, preventing their degradation in lysosomes. iTAP-null primary human macrophages, or tissues from iTAP KO mice, are dramatically depleted in the levels of iRhom2 and active TACE, and are, consequently, profoundly impaired in TNF production. Our work illustrates iTAP as a physiological rheostat controlling TNF signalling and a novel target for the control of inflammation.

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Development of sandwich ELISA for detection and quantification of human and murine a disintegrin and metalloproteinase17

Cited by 26 publications

References 17 publications

Senescence‐associated release of transmembrane proteins involves proteolytic processing by ADAM17 and microvesicle shedding

Senescence‐associated release of transmembrane proteins involves proteolytic processing by ADAM17 and microvesicle shedding

Differential Surface Expression of ADAM10 and ADAM17 on Human T Lymphocytes and Tumor Cells

iTAP, a novel iRhom interactor, controls TNF secretion by policing the stability of iRhom/TACE

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