Research ExplorerPublicationsSoluble T cell immunoglobulin and mucin domain (TIM)-1 and -...

Soluble T cell immunoglobulin and mucin domain (TIM)-1 and -4 generated by A Disintegrin And Metalloprotease (ADAM)-10 and -17 bind to phosphatidylserine

Standard

Soluble T cell immunoglobulin and mucin domain (TIM)-1 and -4 generated by A Disintegrin And Metalloprotease (ADAM)-10 and -17 bind to phosphatidylserine. / Schweigert, Olga; Dewitz, Christin; Möller-Hackbarth, Katja; Trad, Ahmad; Garbers, Christoph; Rose-John, Stefan; Scheller, Jürgen.

In: Biochim Biophys Acta, Vol. 1843, No. 2, 02.2014, p. 275-287.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Schweigert, O, Dewitz, C, Möller-Hackbarth, K, Trad, A, Garbers, C, Rose-John, S & Scheller, J 2014, 'Soluble T cell immunoglobulin and mucin domain (TIM)-1 and -4 generated by A Disintegrin And Metalloprotease (ADAM)-10 and -17 bind to phosphatidylserine', Biochim Biophys Acta, vol. 1843, no. 2, pp. 275-287. https://doi.org/10.1016/j.bbamcr.2013.11.014

APA

Schweigert, O., Dewitz, C., Möller-Hackbarth, K., Trad, A., Garbers, C., Rose-John, S., & Scheller, J. (2014). Soluble T cell immunoglobulin and mucin domain (TIM)-1 and -4 generated by A Disintegrin And Metalloprotease (ADAM)-10 and -17 bind to phosphatidylserine. Biochim Biophys Acta, 1843(2), 275-287. https://doi.org/10.1016/j.bbamcr.2013.11.014

Vancouver

Schweigert O, Dewitz C, Möller-Hackbarth K, Trad A, Garbers C, Rose-John S et al. Soluble T cell immunoglobulin and mucin domain (TIM)-1 and -4 generated by A Disintegrin And Metalloprotease (ADAM)-10 and -17 bind to phosphatidylserine. Biochim Biophys Acta. 2014 Feb;1843(2):275-287. https://doi.org/10.1016/j.bbamcr.2013.11.014

Bibtex

@article{8596cfa7d9064bfeb1083948f8b9e5bb,
title = "Soluble T cell immunoglobulin and mucin domain (TIM)-1 and -4 generated by A Disintegrin And Metalloprotease (ADAM)-10 and -17 bind to phosphatidylserine",
abstract = "T cell immunoglobulin and mucin domain 1 and 4 (TIM-1 and -4) proteins serve as phosphatidylserine receptors to engulf apoptotic cells. Here we show that human TIM-1 and TIM-4 proteins are targets of A Disintegrin And Metalloprotease (ADAM)-mediated ectodomain shedding resulting in soluble forms of TIM-1 and TIM-4. We identified ADAM10 and ADAM17 as major sheddases of TIM-1 and TIM-4 as shown by protease-specific inhibitors, the ADAM10 prodomain, siRNA and ADAM10/ADAM17 deficient murine embryonic fibroblasts (MEFs). TIM-1 and TIM-4 lacking the intracellular domain were efficiently cleaved after ionomycin- and PMA-treatment, indicating that the intracellular domain was not necessary for ectodomain shedding. Soluble TIM-1 and -4 were able to bind to phosphatidylserine, suggesting that soluble TIM-1 and -4 might act as negative regulators of cellular TIM-1 and -4. In summary, we describe TIM-1 and TIM-4 as novel targets for ADAM10- and ADAM17-mediated ectodomain shedding. ",
keywords = "ADAM Proteins/metabolism, ADAM10 Protein, ADAM17 Protein, Amino Acid Sequence, Amino Acids/metabolism, Amyloid Precursor Protein Secretases/metabolism, Animals, Cell Differentiation/drug effects, Cell Membrane/drug effects, HEK293 Cells, Hepatitis A Virus Cellular Receptor 1, Humans, Ionomycin/pharmacology, Membrane Glycoproteins/chemistry, Membrane Proteins/chemistry, Mice, Molecular Sequence Data, Phosphatidylserines/metabolism, Protein Binding/drug effects, Protein Structure, Tertiary, RNA, Small Interfering/metabolism, Receptors, Virus/chemistry, Sequence Deletion, Solubility/drug effects, Tetradecanoylphorbol Acetate/pharmacology",
author = "Olga Schweigert and Christin Dewitz and Katja M{\"o}ller-Hackbarth and Ahmad Trad and Christoph Garbers and Stefan Rose-John and J{\"u}rgen Scheller",
note = "Copyright {\textcopyright} 2013 Elsevier B.V. All rights reserved.",
year = "2014",
month = feb,
doi = "10.1016/j.bbamcr.2013.11.014",
language = "English",
volume = "1843",
pages = "275--287",
journal = "Biochim Biophys Acta",
issn = "0006-3002",
number = "2",

}

RIS

TY - JOUR

T1 - Soluble T cell immunoglobulin and mucin domain (TIM)-1 and -4 generated by A Disintegrin And Metalloprotease (ADAM)-10 and -17 bind to phosphatidylserine

AU - Schweigert, Olga

AU - Dewitz, Christin

AU - Möller-Hackbarth, Katja

AU - Trad, Ahmad

AU - Garbers, Christoph

AU - Rose-John, Stefan

AU - Scheller, Jürgen

N1 - Copyright © 2013 Elsevier B.V. All rights reserved.

PY - 2014/2

Y1 - 2014/2

N2 - T cell immunoglobulin and mucin domain 1 and 4 (TIM-1 and -4) proteins serve as phosphatidylserine receptors to engulf apoptotic cells. Here we show that human TIM-1 and TIM-4 proteins are targets of A Disintegrin And Metalloprotease (ADAM)-mediated ectodomain shedding resulting in soluble forms of TIM-1 and TIM-4. We identified ADAM10 and ADAM17 as major sheddases of TIM-1 and TIM-4 as shown by protease-specific inhibitors, the ADAM10 prodomain, siRNA and ADAM10/ADAM17 deficient murine embryonic fibroblasts (MEFs). TIM-1 and TIM-4 lacking the intracellular domain were efficiently cleaved after ionomycin- and PMA-treatment, indicating that the intracellular domain was not necessary for ectodomain shedding. Soluble TIM-1 and -4 were able to bind to phosphatidylserine, suggesting that soluble TIM-1 and -4 might act as negative regulators of cellular TIM-1 and -4. In summary, we describe TIM-1 and TIM-4 as novel targets for ADAM10- and ADAM17-mediated ectodomain shedding.

AB - T cell immunoglobulin and mucin domain 1 and 4 (TIM-1 and -4) proteins serve as phosphatidylserine receptors to engulf apoptotic cells. Here we show that human TIM-1 and TIM-4 proteins are targets of A Disintegrin And Metalloprotease (ADAM)-mediated ectodomain shedding resulting in soluble forms of TIM-1 and TIM-4. We identified ADAM10 and ADAM17 as major sheddases of TIM-1 and TIM-4 as shown by protease-specific inhibitors, the ADAM10 prodomain, siRNA and ADAM10/ADAM17 deficient murine embryonic fibroblasts (MEFs). TIM-1 and TIM-4 lacking the intracellular domain were efficiently cleaved after ionomycin- and PMA-treatment, indicating that the intracellular domain was not necessary for ectodomain shedding. Soluble TIM-1 and -4 were able to bind to phosphatidylserine, suggesting that soluble TIM-1 and -4 might act as negative regulators of cellular TIM-1 and -4. In summary, we describe TIM-1 and TIM-4 as novel targets for ADAM10- and ADAM17-mediated ectodomain shedding.

KW - ADAM Proteins/metabolism

KW - ADAM10 Protein

KW - ADAM17 Protein

KW - Amino Acid Sequence

KW - Amino Acids/metabolism

KW - Amyloid Precursor Protein Secretases/metabolism

KW - Animals

KW - Cell Differentiation/drug effects

KW - Cell Membrane/drug effects

KW - HEK293 Cells

KW - Hepatitis A Virus Cellular Receptor 1

KW - Humans

KW - Ionomycin/pharmacology

KW - Membrane Glycoproteins/chemistry

KW - Membrane Proteins/chemistry

KW - Mice

KW - Molecular Sequence Data

KW - Phosphatidylserines/metabolism

KW - Protein Binding/drug effects

KW - Protein Structure, Tertiary

KW - RNA, Small Interfering/metabolism

KW - Receptors, Virus/chemistry

KW - Sequence Deletion

KW - Solubility/drug effects

KW - Tetradecanoylphorbol Acetate/pharmacology

U2 - 10.1016/j.bbamcr.2013.11.014

DO - 10.1016/j.bbamcr.2013.11.014

M3 - SCORING: Journal article

C2 - 24286866

VL - 1843

SP - 275

EP - 287

JO - Biochim Biophys Acta

JF - Biochim Biophys Acta

SN - 0006-3002

IS - 2

ER -