Structure and Dynamics of Human Chemokine CCL16-Implications for Biological Activity.

Tytuł:: Structure and Dynamics of Human Chemokine CCL16-Implications for Biological Activity.
Autorzy:: Weiergräber OH; Institute of Biological Information Processing, IBI-7: Structural Biochemistry, Forschungszentrum Jülich, 52425 Jülich, Germany.
Petrović D; Institute of Biological Information Processing, IBI-7: Structural Biochemistry, Forschungszentrum Jülich, 52425 Jülich, Germany.
Kislat A; Klinik für Dermatologie, Universitätsklinikum Düsseldorf, 40225 Düsseldorf, Germany.
Pattky M; Zentralinstitut für Engineering, Elektronik und Analytik, ZEA-3: Analytik, Forschungszentrum Jülich, 52425 Jülich, Germany.
Fabig J; Institute of Biological Information Processing, IBI-7: Structural Biochemistry, Forschungszentrum Jülich, 52425 Jülich, Germany.
Batra-Safferling R; Institute of Biological Information Processing, IBI-7: Structural Biochemistry, Forschungszentrum Jülich, 52425 Jülich, Germany.
Schulte Am Esch J; Klinik für Allgemein-, Viszeral- und Kinderchirurgie, Universitätsklinikum Düsseldorf, 40225 Düsseldorf, Germany.
Hänel K; Institute of Biological Information Processing, IBI-7: Structural Biochemistry, Forschungszentrum Jülich, 52425 Jülich, Germany.
Huhn C; Zentralinstitut für Engineering, Elektronik und Analytik, ZEA-3: Analytik, Forschungszentrum Jülich, 52425 Jülich, Germany.
Strodel B; Institute of Biological Information Processing, IBI-7: Structural Biochemistry, Forschungszentrum Jülich, 52425 Jülich, Germany.; Institute of Theoretical and Computational Chemistry, Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany.
Homey B; Klinik für Dermatologie, Universitätsklinikum Düsseldorf, 40225 Düsseldorf, Germany.
Willbold D; Institute of Biological Information Processing, IBI-7: Structural Biochemistry, Forschungszentrum Jülich, 52425 Jülich, Germany.; Institut für Physikalische Biologie und BMFZ, Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany.
Źródło:: Biomolecules [Biomolecules] 2022 Oct 28; Vol. 12 (11). Date of Electronic Publication: 2022 Oct 28.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Original Publication: Basel, Switzerland : MDPI, 2011-
MeSH Terms:: Chemokines, CC*/metabolism
Chemokines*
Humans ; Ligands ; Glycosaminoglycans
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Contributed Indexing:: Keywords: CCL16; chemokine; glycosaminoglycan; haptotaxis; limited proteolysis
Substance Nomenclature:: 0 (Chemokines, CC)
0 (Chemokines)
0 (Ligands)
0 (Glycosaminoglycans)
Entry Date(s):: Date Created: 20221111 Date Completed: 20221114 Latest Revision: 20221201
Update Code:: 20240104
PubMed Central ID:: PMC9687583
DOI:: 10.3390/biom12111588
PMID:: 36358937
: Czasopismo naukowe

Pełny tekst

Human C-C motif ligand 16 (CCL16) is a chemokine that is distinguished by a large cleavable C-terminal extension of unknown significance. Conflicting data have been reported concerning its tissue distribution and modulation of expression, rendering the biological function of CCL16 enigmatic. Here, we report an integrated approach to the characterisation of this chemokine, including a re-assessment of its expression characteristics as well as a biophysical investigation with respect to its structure and dynamics. Our data indicate that CCL16 is chiefly synthesised by hepatocytes, without an appreciable response to mediators of inflammation, and circulates in the blood as a full-length protein. While the crystal structure of CCL16 confirms the presence of a canonical chemokine domain, molecular dynamics simulations support the view that the C-terminal extension impairs the accessibility of the glycosaminoglycan binding sites and may thus serve as an intrinsic modulator of biological activity.

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