Detailed analysis of MIA protein by mutagenesis

Biological Chemistry
Raphael StollAnja-Katrin Bosserhoff

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.

References

Jan 5, 1996·The Journal of Biological Chemistry·A K BosserhoffR Buettner
Jan 1, 1997·Biopolymers·D C DalgarnoR J Rickles
Jan 29, 1999·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·L E Kay
May 2, 2001·Proceedings of the National Academy of Sciences of the United States of America·J C LougheedT M Handel
Feb 20, 2003·Protein Science : a Publication of the Protein Society·Raphael StollT A Holak
Nov 15, 2003·Laboratory Investigation; a Journal of Technical Methods and Pathology·Anja-Katrin BosserhoffT A Holak

Citations

May 7, 2016·Scientific Reports·King Tuo YipRaphael Stoll
Aug 28, 2012·International Journal of Molecular Medicine·Thomas SchubertAnja K Bosserhoff

Related Concepts

MIA protein, human
Enzyme-Linked Immunosorbent Assay
Neoplasm Proteins
Western Blot
Mutagenesis, Site-Directed
Extracellular Matrix Proteins
Homologous Sequences, Amino Acid
Oligonucleotide Primers
Cell Line, Tumor

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