PTMA Human

Prothymosin Alpha is characterized by its extreme acidity (pI 3.5) and lack of a defined structure . It is primarily localized in the nucleus of living cells, where it plays a crucial role in controlling the cell cycle and promoting cell proliferation . However, PTMA also exhibits functional dualism, as it can be released from dead cells and acquire immunomodulatory properties in the extracellular environment .

Research has highlighted the clinical significance of PTMA, particularly in its potential medical applications . For instance, PTMA has been implicated in the immune response, where it may confer resistance to certain opportunistic infections . Additionally, PTMA has been associated with various pathological conditions, including cancer, ischemic stroke, and immunomodulation .

Recombinant human PTMA is produced by expressing the protein in E. coli and purifying it using conventional chromatography techniques . This recombinant form of PTMA is often fused to a His-tag at the N-terminus to facilitate purification and detection .

Recent studies have explored the role of PTMA in different tissues and cell types. For example, immunohistochemical and western blot analyses have been used to investigate the subcellular localization of PTMA under normal physiological conditions . These studies have revealed differential localization patterns of PTMA in the nucleus and cytoplasm, suggesting distinct functions in different cellular contexts .

Moreover, PTMA has been identified as a novel contributor to the immunopathogenesis of rheumatic heart valve disease (RHVD) . Proteomics and network analysis have shown that PTMA is associated with CD8+ T-cell pathogenic responses and recognition of type 1 collagen in RHVD . This discovery underscores the potential of PTMA as a target for therapeutic interventions in autoimmune and inflammatory diseases.