MIA ("melanoma inhibitory activity"). Biological functions and clinical relevance in malignant melanoma

Der Hautarzt; Zeitschrift für Dermatologie, Venerologie, und verwandte Gebiete
A K BosserhoffR Hein

Abstract

The protein MIA was identified and isolated from the tissue culture supernatant of melanoma cells in vitro by its ability to inhibit thymidine incorporation by melanoma cell lines. After purification and partial sequencing of the peptide, a fragment of the MIA cDNA was cloned by RT-PCR. This cDNA fragment was used to screen phage libraries and subsequently fully encoding human and murine MIA cDNA and genomic DNA clones were obtained. The MIA gene spans a region of approximately 2 kb and is divided into 4 exons. Mapping the MIA gene revealed that the human gene is located on chromosome 19 and the murine gene on chromosome 7. The MIA open reading frame spans 131 (human) or 130 (murine) amino acids. The first 24 (human) or 23 (murine) amino acids represent a signal sequence directing the secretion of MIA into the extracellular compartment. The mature, secreted MIA consists of 107 amino acids and its MW is approximately 11 kDa. Preliminary structural data suggests that MIA is a small globular protein stabilized by two intramolecular disulfide bonds. Expression studies of protein und mRNA levels indicate that MIA is expressed specifically by malignant melanoma cells and chondrocytes. This points to a highly restricted expression pat...Continue Reading

References

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Related Concepts

Malignant Neoplasm of Skin
Gene Expression Regulation, Neoplastic
Exons
Extracellular
Thymidine
Cell Motility
Amino Acids, I.V. solution additive
Murine
Metastatic Melanoma
Extracellular Matrix

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