Structural commonality of C1q TNF‐related proteins and their potential to activate relaxin/insulin‐like family peptide receptor 1 signalling pathways in cancer cells | Zendy

Klonisch Thomas | Zendy; Glogowska Aleksandra | Zendy; Thanasupawat Thatchawan | Zendy; Burg Maxwell | Zendy; Krcek Jerry | Zendy; Pitz Marshall | Zendy; Jaggupilli Appalaraju | Zendy; Chelikani Prashen | Zendy; Wong G William | Zendy; HombachKlonisch Sabine | Zendy

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Structural commonality of C1q TNF‐related proteins and their potential to activate relaxin/insulin‐like family peptide receptor 1 signalling pathways in cancer cells

Author(s) -

Klonisch Thomas,

Glogowska Aleksandra,

Thanasupawat Thatchawan,

Burg Maxwell,

Krcek Jerry,

Pitz Marshall,

Jaggupilli Appalaraju,

Chelikani Prashen,

Wong G William,

HombachKlonisch Sabine

Publication year - 2017

Publication title -

british journal of pharmacology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.432

H-Index - 211

eISSN - 1476-5381

pISSN - 0007-1188

DOI - 10.1111/bph.13559

Subject(s) - relaxin , receptor , signal transduction , insulin , signalling , insulin receptor , microbiology and biotechnology , biology , signalling pathways , cancer research , chemistry , endocrinology , biochemistry , insulin resistance

We established the role of the GPCR relaxin/insulin-like family peptide receptor 1 (RXFP1 receptor) as a novel active receptor in human glioblastoma (GB), a fatal brain tumour. We identified C1q/TNF-related protein 8 (CTRP8) as a novel agonist of the RXFP1 receptor. CTRP8 enhanced the motility and matrix invasion of GB, and this involved PKC-mediated up-regulation of cathepsin B, a marker for poor prognosis in GB patients. We conclude that the absence of relaxin isoforms does not preclude the activation of the RXFP1 receptor, as the least known member of the CTRP family, CTRP8, can effectively target and activate RXFP1 receptors.

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