Recombinant Human CHGA protein

Chromogranin A (CHGA), a member of the granin family of acidic secretory proteins, is a key component of neuroendocrine secretory granules. It is ubiquitously expressed in neurons, endocrine cells, and neuroendocrine tumors, where it co-stores and co-releases with hormones, neuropeptides, and neurotransmitters. CHGA serves multiple roles: it regulates the biogenesis and stability of secretory granules through its calcium-binding capacity, modulates hormone processing by acting as a prohormone, and exhibits bioactive peptide fragments with diverse physiological functions. These fragments, including vasostatin, pancreastatin, and catestatin, influence cardiovascular homeostasis, glucose metabolism, immune responses, and antimicrobial activity.

Recombinant CHGA proteins are engineered to study its structure-function relationships and therapeutic potential. Produced via heterologous expression systems (e.g., E. coli, mammalian cells), they retain post-translational modifications critical for bioactivity. Recombinant CHGA enables researchers to investigate its role in neuroendocrine disorders, such as hypertension, heart failure, and neuroendocrine tumors, where CHGA levels serve as diagnostic biomarkers. Additionally, it aids in exploring its involvement in neurodegenerative diseases like Alzheimer’s and Parkinson’s, linked to dysregulated secretory pathways.

The development of recombinant CHGA has advanced drug discovery, particularly for cardiovascular and metabolic diseases. For example, catestatin derivatives are being explored as antihypertensive agents. However, challenges remain in mimicking native protein folding and post-translational modifications. Ongoing research focuses on optimizing expression systems and engineering bioactive peptides to harness CHGA’s therapeutic potential while addressing its dual role in both physiological regulation and disease pathogenesis.