MIA Human

Recombinant Human MIA is produced in Escherichia coli and is a single, non-glycosylated polypeptide chain consisting of 108 amino acids, with a total molecular mass of approximately 12,237 Daltons . The protein contains an SH3 domain, which is crucial for its interaction with other proteins and its inhibitory functions.

MIA was initially identified as an inhibitor of the in vitro growth of malignant melanoma cells . It acts as a potent tumor cell growth inhibitor for malignant melanoma and other neuroectodermal tumors, including gliomas, in an autocrine fashion. This means that the cells producing MIA can also respond to it, creating a self-regulating loop that influences cell behavior.

MIA has been shown to be a very sensitive and specific serum marker for systemic malignant melanoma . This makes it useful for:

• Staging of primary melanomas: Determining the extent of the disease.
• Detection of progression: Monitoring the transition from localized to metastatic disease.
• Therapy monitoring: Assessing the effectiveness of treatments for advanced melanomas.

In addition to its role in melanoma, MIA has been found to increase the invasiveness of pancreatic cancer cells . This highlights its broader significance in cancer biology and its potential as a target for therapeutic interventions.

Research into MIA continues to uncover its various roles and mechanisms. For example, studies have shown that MIA mRNA expression is inversely correlated with pigmentation in melanoma cell lines . This suggests that MIA could be involved in the regulation of pigmentation and melanoma progression.

Moreover, MIA’s interaction with extracellular matrix proteins like fibronectin and laminin suggests that it could influence cell adhesion and migration . These properties make it a potential target for therapies aimed at preventing cancer metastasis.