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Sequential processing of the transmembrane chemokines CX3CL1 and CXCL16 by alpha- and gamma-secretases

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Sequential processing of the transmembrane chemokines CX3CL1 and CXCL16 by alpha- and gamma-secretases. / Schulte, A; Schulz, B; Andrzejewski, M G; Hundhausen, C; Mletzko, S; Achilles, J; Reiss, K; Paliga, K; Weber, C; John, S Rose; Ludwig, A.

In: BIOCHEM BIOPH RES CO, Vol. 358, No. 1, 22.06.2007, p. 233-40.

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

Harvard

Schulte, A, Schulz, B, Andrzejewski, MG, Hundhausen, C, Mletzko, S, Achilles, J, Reiss, K, Paliga, K, Weber, C, John, SR & Ludwig, A 2007, 'Sequential processing of the transmembrane chemokines CX3CL1 and CXCL16 by alpha- and gamma-secretases', BIOCHEM BIOPH RES CO, vol. 358, no. 1, pp. 233-40. https://doi.org/10.1016/j.bbrc.2007.04.100

APA

Schulte, A., Schulz, B., Andrzejewski, M. G., Hundhausen, C., Mletzko, S., Achilles, J., Reiss, K., Paliga, K., Weber, C., John, S. R., & Ludwig, A. (2007). Sequential processing of the transmembrane chemokines CX3CL1 and CXCL16 by alpha- and gamma-secretases. BIOCHEM BIOPH RES CO, 358(1), 233-40. https://doi.org/10.1016/j.bbrc.2007.04.100

Vancouver

Schulte A, Schulz B, Andrzejewski MG, Hundhausen C, Mletzko S, Achilles J et al. Sequential processing of the transmembrane chemokines CX3CL1 and CXCL16 by alpha- and gamma-secretases. BIOCHEM BIOPH RES CO. 2007 Jun 22;358(1):233-40. https://doi.org/10.1016/j.bbrc.2007.04.100

Bibtex

@article{df48e37dd4ad42618ec809db82a4b5dd,
title = "Sequential processing of the transmembrane chemokines CX3CL1 and CXCL16 by alpha- and gamma-secretases",
abstract = "The chemokines CX3CL1/Fractalkine and CXCL16 are expressed as transmembrane molecules and can mediate cell-cell-adhesion. By proteolytic processing, CX3CL1 and CXCL16 are released from the cell surface by proteolytic shedding resulting in the generation of soluble chemoattractants. This ectodomain release is mediated by the alpha-secretase-like activity of the two disintegrins and metalloproteinases ADAM10 and ADAM17. Using CX3CL1 and CXCL16 constructs C-terminally fused to two Z-domains of Protein A (2Z-tag) we detect C-terminal fragments (CTFs) of both chemokines resulting from ADAM10-mediated cleavages at multiple sites as examined by inhibitor studies. Furthermore, inhibitor studies as well as genetic studies using presenilin 1/2-deficient cell lines suggest the involvement of gamma-secretase-but not beta-secretase-like activity in the processing of transmembrane chemokines. The combination of alpha- and gamma-secretase and proteasomal inhibitors points towards a sequential processing of transmembrane chemokines by first ADAM10 and then gamma-secretases and possible further degradation. This proteolytic processing cascade of transmembrane chemokines is similar to that described for Notch and E-cadherin where CTFs generated by gamma-secretase serve as intracellular signal transmitters.",
keywords = "ADAM Proteins, Amyloid Precursor Protein Secretases, Cell Line, Chemokine CX3CL1, Chemokines, CX3C, Chemokines, CXC, Cloning, Molecular, Humans, Membrane Proteins, Presenilin-1, Presenilin-2, Proteasome Endopeptidase Complex, Protein Structure, Tertiary, Receptors, Scavenger",
author = "A Schulte and B Schulz and Andrzejewski, {M G} and C Hundhausen and S Mletzko and J Achilles and K Reiss and K Paliga and C Weber and John, {S Rose} and A Ludwig",
year = "2007",
month = jun,
day = "22",
doi = "10.1016/j.bbrc.2007.04.100",
language = "English",
volume = "358",
pages = "233--40",
journal = "BIOCHEM BIOPH RES CO",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - Sequential processing of the transmembrane chemokines CX3CL1 and CXCL16 by alpha- and gamma-secretases

AU - Schulte, A

AU - Schulz, B

AU - Andrzejewski, M G

AU - Hundhausen, C

AU - Mletzko, S

AU - Achilles, J

AU - Reiss, K

AU - Paliga, K

AU - Weber, C

AU - John, S Rose

AU - Ludwig, A

PY - 2007/6/22

Y1 - 2007/6/22

N2 - The chemokines CX3CL1/Fractalkine and CXCL16 are expressed as transmembrane molecules and can mediate cell-cell-adhesion. By proteolytic processing, CX3CL1 and CXCL16 are released from the cell surface by proteolytic shedding resulting in the generation of soluble chemoattractants. This ectodomain release is mediated by the alpha-secretase-like activity of the two disintegrins and metalloproteinases ADAM10 and ADAM17. Using CX3CL1 and CXCL16 constructs C-terminally fused to two Z-domains of Protein A (2Z-tag) we detect C-terminal fragments (CTFs) of both chemokines resulting from ADAM10-mediated cleavages at multiple sites as examined by inhibitor studies. Furthermore, inhibitor studies as well as genetic studies using presenilin 1/2-deficient cell lines suggest the involvement of gamma-secretase-but not beta-secretase-like activity in the processing of transmembrane chemokines. The combination of alpha- and gamma-secretase and proteasomal inhibitors points towards a sequential processing of transmembrane chemokines by first ADAM10 and then gamma-secretases and possible further degradation. This proteolytic processing cascade of transmembrane chemokines is similar to that described for Notch and E-cadherin where CTFs generated by gamma-secretase serve as intracellular signal transmitters.

AB - The chemokines CX3CL1/Fractalkine and CXCL16 are expressed as transmembrane molecules and can mediate cell-cell-adhesion. By proteolytic processing, CX3CL1 and CXCL16 are released from the cell surface by proteolytic shedding resulting in the generation of soluble chemoattractants. This ectodomain release is mediated by the alpha-secretase-like activity of the two disintegrins and metalloproteinases ADAM10 and ADAM17. Using CX3CL1 and CXCL16 constructs C-terminally fused to two Z-domains of Protein A (2Z-tag) we detect C-terminal fragments (CTFs) of both chemokines resulting from ADAM10-mediated cleavages at multiple sites as examined by inhibitor studies. Furthermore, inhibitor studies as well as genetic studies using presenilin 1/2-deficient cell lines suggest the involvement of gamma-secretase-but not beta-secretase-like activity in the processing of transmembrane chemokines. The combination of alpha- and gamma-secretase and proteasomal inhibitors points towards a sequential processing of transmembrane chemokines by first ADAM10 and then gamma-secretases and possible further degradation. This proteolytic processing cascade of transmembrane chemokines is similar to that described for Notch and E-cadherin where CTFs generated by gamma-secretase serve as intracellular signal transmitters.

KW - ADAM Proteins

KW - Amyloid Precursor Protein Secretases

KW - Cell Line

KW - Chemokine CX3CL1

KW - Chemokines, CX3C

KW - Chemokines, CXC

KW - Cloning, Molecular

KW - Humans

KW - Membrane Proteins

KW - Presenilin-1

KW - Presenilin-2

KW - Proteasome Endopeptidase Complex

KW - Protein Structure, Tertiary

KW - Receptors, Scavenger

U2 - 10.1016/j.bbrc.2007.04.100

DO - 10.1016/j.bbrc.2007.04.100

M3 - SCORING: Journal article

C2 - 17467666

VL - 358

SP - 233

EP - 240

JO - BIOCHEM BIOPH RES CO

JF - BIOCHEM BIOPH RES CO

SN - 0006-291X

IS - 1

ER -