P56

Ranvier, Gustavo G. Fernandez; Weng, Julie; Yeh, Ru-Fang; Shibru, Daniel; Duh, Quan Yang; Clark, Orlo H.; Kebebew, Electron

doi:10.1016/j.jss.2006.12.285

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2011

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“…Moreover, a positive correlation of expression of chemerin mRNA with tumor size of adrenocortical carcinoma has been reported (27). Similar to the human glioma cell line DBTRG-05MG (28), we also detected expression of chemerin receptors including CMKLR1, CCRL2, and GPR1 in human GBM U-87 MG cells at the mRNA level, and flow cytometry showed that U-87 MG cells expressed chemerin receptors.…”

Section: Discussionsupporting

confidence: 79%

Proteolytic Cleavage of Chemerin Protein Is Necessary for Activation to the Active Form, Chem157S, Which Functions as a Signaling Molecule in Glioblastoma

Yamaguchi

Zhao

et al. 2011

Journal of Biological Chemistry

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Background: Chemerin (chem163S) is proteolytically cleaved to generate active isoforms. Results: Chem157S has the highest activity in stimulating calcium transients and chemotaxis, chem158K and chem163S have much lower activity, and chem155A is not an agonist. Chem157S stimulates signaling in glioblastoma cells. Conclusion: Chem163S proteolysis to chem157S is needed for its activity. Significance: Chemerin may play a role in glioblastoma.

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Section: Discussionsupporting

confidence: 79%