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Membrane‐type frizzled‐related protein regulates lipidome and transcription for photoreceptor function
Author(s) -
Kautzmann MarieAudrey I.,
Gordon William C.,
Jun Bokkyoo,
Do Khanh V.,
Matherne Blake J.,
Fang Zhide,
Bazan Nicolas G.
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.201902359r
Subject(s) - lipidome , frizzled , microbiology and biotechnology , biology , transmembrane protein , membrane protein , retinal , gene , docosahexaenoic acid , wnt signaling pathway , integral membrane protein , signal transduction , biochemistry , receptor , polyunsaturated fatty acid , fatty acid , lipidomics , membrane
Molecular decision‐makers of photoreceptor (PRC) membrane organization and gene regulation are critical to understanding sight and retinal degenerations that lead to blindness. Using Mfrp rd6 mice, which develop PRC degeneration, we uncovered that membrane‐type frizzled‐related protein (MFRP) participates in docosahexaenoic acid (DHA, 22:6) enrichment in a manner similar to adiponectin receptor 1 (AdipoR1). Untargeted imaging mass spectrometry demonstrates cell‐specific reduction of phospholipids containing 22:6 and very long‐chain polyunsaturated fatty acids (VLC‐PUFAs) in Adipor1 −/− and Mfrp rd6 retinas. Gene expression of pro‐inflammatory signaling pathways is increased and gene‐encoding proteins for PRC function decrease in both mutants. Thus, we propose that both proteins are necessary for retinal lipidome membrane organization, visual function, and to the understanding of the early pathology of retinal degenerative diseases.