Biochemical and biophysical characterization of cytokine-like protein 1 (CYTL1)
Autor: | Apostolos G. Gittis, Philip M. Murphy, David N. Garboczi, Joohee Lee, Aurelie Tomczak, Kavita Singh |
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Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
CCR1 Receptors CCR2 Immunology CCR3 Biology CCL7 Biochemistry Article 03 medical and health sciences Chemokine receptor Chondrocytes Humans Immunology and Allergy CX3CL1 Molecular Biology 030102 biochemistry & molecular biology Circular Dichroism Blood Proteins Hematology CXCL2 030104 developmental biology Cytokines XCL2 Receptors Chemokine Chemokines Signal Transduction CCL21 |
Zdroj: | Cytokine. 96:238-246 |
ISSN: | 1043-4666 |
Popis: | Cytokine-like protein 1 (CYTL1) is a small widely expressed secreted protein lacking significant primary sequence homology to any other known protein. CYTL1 expression appears to be highest in the hematopoietic system and in chondrocytes; however, maintenance of cartilage in mouse models of arthritis is its only reported function in vivo. Despite lacking sequence homology to chemokines, CYTL1 is predicted by computational methods to fold like a chemokine, and has been reported to function as a chemotactic agonist at the chemokine receptor CCR2 in mouse monocyte/macrophages. Nevertheless, since chemokines are defined by structure and chemokine receptors are able to bind many non-chemokine ligands, direct determination of the CYTL1 tertiary structure will ultimately be required to know whether it actually folds as a chemokine and therefore is a chemokine. Towards this goal, we have developed a method for producing functional recombinant human CYTL1 in bacteria, and we provide new evidence about the biophysical and biochemical properties of recombinant CYTL1. Circular dichroism analysis showed that, like chemokines, CYTL1 has a higher content of beta-sheet than alpha-helix secondary structure. Furthermore, recombinant CYTL1 promoted calcium flux in chondrocytes. Nevertheless, unlike chemokines, CYTL1 had limited affinity to proteoglycans. Together, these properties further support cytokine-like properties for CYTL1 with some overlap with the chemokines. |
Databáze: | OpenAIRE |
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