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STRL22 is a receptor for the CC chemokine MIP-3alpha
F Liao1, R Alderson, J Su
1Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
Biochemical and Biophysical Research Communications
|July 9, 1997
Summary
STRL22, a novel seven transmembrane domain orphan receptor, specifically binds MIP-3alpha. This interaction triggers a calcium flux in lymphocytes, identifying STRL22 as the CC chemokine receptor 6 (CCR6).
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Background:
- Seven transmembrane domain orphan receptors play crucial roles in cellular signaling.
- Chemokines and their receptors are vital in immune cell trafficking and function.
- STRL22 is a receptor expressed in lymphocytes and lymphoid tissues.
Purpose of the Study:
- To investigate the ligand-binding properties of the STRL22 receptor.
- To determine the functional response of STRL22 to chemokines.
- To characterize the role of STRL22 in immune cell signaling.
Main Methods:
- Transfection of human embryonic kidney 293 cells with STRL22.
- Specific binding assays using MIP-3alpha and other chemokines.
- Calcium flux measurements in transfected cells and primary lymphocytes.
Main Results:
- STRL22-transfected cells demonstrated specific binding to MIP-3alpha.
- MIP-3alpha induced a calcium flux in STRL22-transfected cells, but not other chemokines.
- MIP-3alpha also induced a calcium flux in peripheral blood lymphocytes and tumor-infiltrating lymphocytes expressing STRL22.
Conclusions:
- STRL22 functions as a specific receptor for the CC chemokine MIP-3alpha.
- The identification of STRL22 as a functional CC chemokine receptor leads to its re-naming as CCR6.
- CCR6 plays a role in mediating MIP-3alpha-induced signaling in lymphocytes.