Cathepsin H overexpression 293T lysate (whole cell)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Cathepsin H also known as CPSH is a lysosomal cysteine protease that plays a role in intracellular protein degradation. It has a molecular mass of approximately 28 kilodaltons. This enzyme is expressed across various tissues with high expression levels in liver kidney and spleen. The enzyme primarily functions at acidic pH levels within lysosomes where it acts to break down peptides into amino acids by removing terminal residues.

Biological function summary

As a member of the cathepsin family Cathepsin H contributes to the regulation of protein turnover and homeostasis. It performs a dual role as both an aminopeptidase and endopeptidase. In addition to its function in protein degradation the enzyme involves itself in antigen processing during immune responses. Reactivity of Cathepsin H in immune complexes shows its importance in shaping immune tolerance and responses.

Pathways

Cathepsin H interacts with the lysosomal degradation pathway and plays a role in the MHC class II-mediated antigen presentation. This pathway is pivotal for the regulation of immune responses. Relation to other proteins like Cathepsin L and Cathepsin B highlights Cathepsin H's complementary function in proteolytic processing within lysosomes. Its role and expression play an integral part in balancing protein synthesis and degradation cycles.

Cathepsin H associates closely with cancer and neurodegenerative diseases. Its activity can influence tumor progression and metastasis due to its role in extracellular matrix remodeling and cell migration. In neurodegenerative disorders such as Alzheimer's disease its dysregulated activity may contribute to neuronal cell death. Cathepsin H’s connection to proteins like amyloid precursor protein (APP) in Alzheimer's highlights the complex interplay between protease activity and disease mechanisms.