Perforin-1 (PRF) is a pore-forming protein encoded in humans by the PRF1 gene. It is stored in the secretory granules of cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells, collectively known as cytotoxic lymphocytes (CLs). Upon activation, these cells release perforin to form pores in the membranes of target cells, enabling the entry of granzymes that trigger apoptosis. Perforin is therefore a central effector molecule of the immune system, essential for the elimination of virus-infected and transformed cells. Mutations in PRF1 that impair perforin expression or function are associa
Perforin-1 (PRF) is a pore-forming protein encoded in humans by the PRF1 gene. It is stored in the secretory granules of cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells, collectively known as cytotoxic lymphocytes (CLs). Upon activation, these cells release perforin to form pores in the membranes of target cells, enabling the entry of granzymes that trigger apoptosis. Perforin is therefore a central effector molecule of the immune system, essential for the elimination of virus-infected and transformed cells. Mutations in PRF1 that impair perforin expression or function are associated with familial hemophagocytic lymphohistiocytosis (FHL) and related immune dysregulation syndromes, a spectrum of conditions sometimes collectively referred to as perforinopathies.
== Discovery == Perforin was initially discovered in 1983 and subsequently cloned from an expression library in 1988 using anti-complement C9 antibody cross-reactivity. A sequence comparison showed a notable resemblance between the two proteins in a specific central region, termed the 'membrane attack complex/perforin' (MACPF) domain.
Discovered by embedding cosine similarity (sentence-transformers MiniLM, 384-dim).