PDCD6 Human

PDCD6 was first identified in the context of apoptosis, where it was found to be upregulated in cells undergoing programmed cell death. The protein contains five EF-hand motifs, which are helix-loop-helix structural domains capable of binding calcium ions. This calcium-binding ability is critical for its function in apoptosis .

PDCD6 interacts with various proteins involved in the apoptotic pathway. One of its key interactions is with Death-Associated Protein Kinase 1 (DAPk1). This interaction enhances the apoptotic signals through a caspase-3 dependent pathway, leading to cell death . The protein’s role in apoptosis is not limited to this interaction; it also binds to other apoptotic proteins, thereby modulating the cell death process.

Recent studies have highlighted the significance of PDCD6 in cancer biology. In epithelial ovarian cancer, PDCD6 has been identified as an independent predictor of progression-free survival. High levels of PDCD6 expression correlate with increased cell migration and invasion, suggesting that PDCD6 may play a role in cancer metastasis . This makes PDCD6 a potential target for therapeutic interventions in cancer treatment.

Recombinant PDCD6 refers to the protein produced through recombinant DNA technology, which allows for the expression of the human PDCD6 gene in a host organism, such as bacteria or yeast. This technology enables the production of large quantities of PDCD6 for research and therapeutic purposes. Recombinant PDCD6 is used in various studies to understand its function and to develop potential therapeutic strategies targeting its activity.

The role of PDCD6 in apoptosis and cancer progression makes it a significant molecule for clinical research. Understanding the mechanisms by which PDCD6 regulates cell death and survival pathways can lead to the development of novel cancer therapies. Additionally, PDCD6’s involvement in other diseases related to apoptosis, such as neurodegenerative disorders, is an area of active research.