Deletion of Biliverdin Reductase A in Myeloid Cells Promotes Chemokine Expression and Chemotaxis in Part via a Complement C5a--C5aR1 Pathway.


Journal

Journal of immunology (Baltimore, Md. : 1950)
ISSN: 1550-6606
Titre abrégé: J Immunol
Pays: United States
ID NLM: 2985117R

Informations de publication

Date de publication:
15 05 2019
Historique:
received: 13 10 2017
accepted: 11 03 2019
pubmed: 7 4 2019
medline: 31 12 2019
entrez: 7 4 2019
Statut: ppublish

Résumé

Biliverdin reductase (BVR)-A is a pleotropic enzyme converting biliverdin to bilirubin and a signaling molecule that has cytoprotective and immunomodulatory effects. We recently showed that biliverdin inhibits the expression of complement activation fragment 5a receptor one (C5aR1) in RAW 264.7 macrophages. In this study, we investigated the role of BVR-A in determining macrophage inflammatory phenotype and function via regulation of C5aR1. We assessed expression of C5aR1, M1-like macrophage markers, including chemokines (RANTES, IP-10), as well as chemotaxis in response to LPS and C5a in bone marrow-derived macrophages from

Identifiants

pubmed: 30952817
pii: jimmunol.1701443
doi: 10.4049/jimmunol.1701443
pmc: PMC6504595
mid: NIHMS1524242
doi:

Substances chimiques

C5ar1 protein, mouse 0
Chemokines 0
Receptor, Anaphylatoxin C5a 0
Complement C5a 80295-54-1
Oxidoreductases Acting on CH-CH Group Donors EC 1.3.-
biliverdin reductase EC 1.3.1.24

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2982-2990

Subventions

Organisme : NIDDK NIH HHS
ID : R01 DK104714
Pays : United States
Organisme : NCI NIH HHS
ID : R21 CA169904
Pays : United States

Informations de copyright

Copyright © 2019 by The American Association of Immunologists, Inc.

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Auteurs

Kavita Bisht (K)

Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215.
Cancer Care and Biology Program, Mater Research Institute, The University of Queensland, Translational Research Institute, Woolloongabba, Queensland 4102, Australia.

Giacomo Canesin (G)

Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215.

Tasneem Cheytan (T)

Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215.

Mailin Li (M)

Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215.

Zsuzsanna Nemeth (Z)

Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215.

Eva Csizmadia (E)

Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215.

Trent M Woodruff (TM)

School of Biomedical Sciences, The University of Queensland, Queensland 4072, Australia.

David E Stec (DE)

Department of Physiology and Biophysics, The University of Mississippi Medical Center, Jackson, MS 39216; and.

Andrew C Bulmer (AC)

School of Medical Science, Griffith University, Queensland 4222, Australia.

Leo E Otterbein (LE)

Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215.

Barbara Wegiel (B)

Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215; bwegiel@bidmc.harvard.edu.

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