Stoll, Raphael and Lodermeyer, Sibylla and Bosserhoff, Anja-Katrin (2006) Detailed analysis of MIA protein by mutagenesis. BIOLOGICAL CHEMISTRY, 387 (12). pp. 1601-1606. ISSN 1431-6730,
Full text not available from this repository. (Request a copy)Abstract
MIA (melanoma inhibitory activity) has been identified as a small protein secreted by malignant melanoma cells that interacts with extracellular matrix proteins including fibronectin. These findings suggest that MIA may play a role in tumor progression and the spread of malignant melanomas by mediating detachment of cells from extracellular matrix molecules. Here, we present a detailed study on functionally important MIA domains. Using site-directed mutagenesis, amino acids important for MIA structure and/or function were determined. Amino acids conserved in SH3 domains were shown to be important for structural integrity. In addition, amino acid residues necessary for MIA function were identified. Interestingly, not all of them are conserved with respect to other members of the MIA protein family. In summary, our results lead to a better understanding of MIA function. Regulating MIA functions in vivo may provide a novel therapeutic strategy for metastatic melanoma disease.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MELANOMA INHIBITORY-ACTIVITY; MALIGNANT-MELANOMA; SH3 DOMAINS; CELLS; NMR; METASTASIS; RELAXATION; DYNAMICS; INVASION; |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Pathologie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 15 Jan 2021 13:25 |
| Last Modified: | 15 Jan 2021 13:25 |
| URI: | https://pred.uni-regensburg.de/id/eprint/33671 |
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