Written long, then trimmed
A peptide hormone is a protein, so the cell builds it the way it builds any protein: a gene is read and amino acids are linked into a chain. But the chain that comes off the ribosome is not the finished hormone. It is a longer draft called a preprohormone — the active hormone plus extra pieces front and back.
- The ribosome makes the [[preprohormone|preprohormone]] — the longest form. Its leading "pre" piece is a signal sequence that steers the chain into the endoplasmic reticulum.
- The signal sequence is clipped off, leaving the [[prohormone|prohormone]] — still not active, but closer.
- Inside secretory granules, enzymes make the final cuts, releasing the active hormone (and sometimes useful leftover fragments).
Insulin: the classic worked example
Insulin shows the trimming beautifully. Its prohormone, proinsulin, is a single folded chain. Enzymes snip out a middle segment — the C-peptide — leaving two chains joined by bridges: that is mature insulin. The C-peptide is released in equal amounts alongside insulin, which is why doctors can measure it to ask "how much insulin is this body making on its own?"
PREPRO-INSULIN [signal]---[B chain]---[ C-peptide ]---[A chain]
| clip signal in the ER
v
PRO-INSULIN [B chain]---[ C-peptide ]---[A chain] (one folded chain)
| enzymes excise C-peptide inside the granule
v
INSULIN [B chain]==bridges==[A chain] + free C-peptide
Secreted together, 1 : 1 -> measuring C-peptide estimates the body's own insulin output.Stored ahead, released in a flash
Because they are water-loving, peptide and protein hormones can be packed into membrane-wrapped secretory granules and stockpiled inside the cell. This is the great advantage of the family: the hormone is pre-made and waiting. When the right trigger arrives, granules fuse with the cell membrane and spill their contents into the blood within seconds — no time wasted on synthesis.