Growth Factors
Product List
MIA Human
Melanoma Inhibitory Activity Human Recombinant
The MIA is purified by proprietary chromatographic techniques.
MIA Human, His
Melanoma Inhibitory Activity Protein Human Recombinant, His Tag
MIA2 Human
Melanoma Inhibitory Activity 2 Human Recombinant
The MIA2 is purified by proprietary chromatographic techniques.
Introduction
Melanoma Inhibitory Activity (MIA) is a small secreted protein primarily associated with malignant melanoma, a type of skin cancer. MIA was initially identified as a factor secreted by melanoma cells that inhibits the attachment of these cells to the extracellular matrix, thereby promoting their metastatic potential . MIA belongs to a family of proteins that includes MIA, OTOR (also known as MIAL), MIA2, and TANGO .
Key Biological Properties: MIA is a small protein with a molecular weight of approximately 11 kDa. It is secreted by cells and interacts with components of the extracellular matrix, such as fibronectin and laminin .
Expression Patterns: MIA is highly expressed in malignant melanoma cells and to a lesser extent in other types of cancer cells, such as those from breast, colon, and pancreatic cancers . In non-neoplastic tissues, MIA expression is primarily found in cartilage .
Tissue Distribution: MIA is predominantly localized in malignant cells within tumors. In pancreatic tissues, for example, MIA is found in malignant cells and tubular complexes of cancer specimens, but not in normal ductal cells, acinar cells, or islets .
Primary Biological Functions: MIA plays a crucial role in the progression and metastasis of malignant melanomas. It promotes the metastatic behavior of melanoma cells by interacting with extracellular matrix components and inhibiting cell attachment .
Role in Immune Responses and Pathogen Recognition: While the primary function of MIA is related to tumor progression, it also has implications in immune responses. MIA can modulate the tumor microenvironment, potentially influencing immune cell infiltration and activity .
Mechanisms with Other Molecules and Cells: MIA interacts with extracellular matrix proteins, such as fibronectin and laminin, through specific binding motifs. This interaction inhibits the attachment of melanoma cells to the extracellular matrix, promoting their metastatic potential .
Binding Partners and Downstream Signaling Cascades: MIA binds to integrins and other cell surface receptors, influencing downstream signaling pathways that regulate cell adhesion, migration, and invasion .
Transcriptional Regulation: The expression of MIA is regulated at the transcriptional level by specific transcription factors. These factors control the mRNA transcription of MIA in melanoma cells and chondrocytes .
Post-Translational Modifications: MIA undergoes post-translational modifications that can influence its activity and stability. These modifications include glycosylation and phosphorylation, which may affect its interactions with other proteins and its function in tumor progression .
Biomedical Research: MIA is used as a biomarker in biomedical research to study the progression and metastasis of melanoma and other cancers .
Diagnostic Tools: MIA levels in serum can serve as a diagnostic marker for detecting metastatic melanoma and monitoring therapy responses. A commercially available MIA-ELISA is routinely used in clinical settings for this purpose .
Therapeutic Strategies: Targeting MIA and its interactions with the extracellular matrix is a potential therapeutic strategy for inhibiting melanoma metastasis. Inhibitors that prevent MIA dimerization have shown promise in reducing cell migration and metastasis in preclinical studies .
Development to Aging and Disease: MIA plays a significant role throughout the life cycle of melanoma cells. From the early stages of tumor development, MIA promotes cell detachment and migration, facilitating metastasis. As the tumor progresses, MIA continues to influence the tumor microenvironment and immune responses, contributing to disease progression and resistance to therapy .
