Metabolic · Chromogranin A-derived regulatory peptide
Pancreastatin
Also known as PST
A chromogranin A-derived peptide studied in islet secretion and cellular metabolic signalling, with an unresolved receptor.
- Length
- 52 amino acids in the commonly referenced human form
- Half-life
- Not well characterised
- Mechanism
- Pancreastatin modifies stimulus-coupled secretion and metabolic signalling in experimental systems, with Gq/11-associated phospholipase C and calcium pathways implicated in some models. Its molecular receptor identity remains unresolved, so it should not be assigned to a definitively established receptor target.
- Studied in
- Isolated pancreatic islets, hepatocytes, adipocytes and rodent metabolic models are used to investigate pancreastatin-dependent secretion and cellular substrate handling.
About Pancreastatin
Pancreastatin was first isolated from porcine pancreas in 1986 and subsequently recognised as a proteolytic product of chromogranin A, a secretory granule protein. The original porcine peptide contains 49 residues, whereas the commonly referenced human form contains 52. Its C-terminal region is relatively conserved and carries important functional determinants. Native pancreastatin is C-terminally amidated, making terminal chemistry an essential part of sequence identification when comparing research preparations.
Chromogranin A processing varies between tissues and experimental conditions, so pancreastatin-related material can comprise different molecular forms. Laboratory investigations examine glucose-stimulated secretion in islets, calcium mobilisation and phosphoinositide signalling, alongside glycogen and lipid-related endpoints in isolated cells. Although membrane binding and G protein-linked responses have been reported, the receptor has not been conclusively identified. Full-length peptides and active C-terminal fragments should therefore be treated as distinct experimental reagents.
Laboratory notes
- Specify species, residue boundaries and C-terminal amidation status on assay records and analytical certificates.
- Validate immunoassay recognition against chromogranin A and related fragments to distinguish pancreastatin from precursor-associated signal.
- In islet experiments, standardise glucose conditions, preparation viability and sampling times before comparing secretory responses.
Storage and reconstitution basics: storage guide.
Questions about Pancreastatin
Why are both 49- and 52-residue forms described?
The original porcine pancreastatin is 49 residues long, while the commonly referenced human sequence contains 52. Species and fragment boundaries must accompany the peptide name.
Is C-terminal amidation relevant to assay design?
Yes. Amidation changes terminal chemistry and can influence peptide recognition and activity. An amidated preparation should not automatically be treated as equivalent to its free-acid counterpart.
Can a pancreastatin response identify its receptor?
No. Calcium mobilisation or phospholipase C activation indicates a downstream response, not a unique receptor identity. Direct binding and molecular validation are needed for receptor assignment.
Is Pancreastatin for human use?
No. It is supplied strictly for in-vitro laboratory research and is not for human or animal consumption.
Related research peptides
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