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Human Leukocyte Migration Inhibitory Factor (LIF)
Author(s) -
BENDTZEN K.
Publication year - 1977
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1977.tb00378.x
Subject(s) - inhibitory postsynaptic potential , leukemia inhibitory factor , factor (programming language) , immunology , macrophage migration inhibitory factor , biology , endocrinology , interleukin 6 , computer science , inflammation , cytokine , programming language
Recently reported experiments suggest that human leukocyte migration inhibitory factor (LIF) has properties of an esterase and a protease with substrate specificities directed against arginine esters and amides. Also reported previously, the synthetic phosphodiester bis‐ p ‐nitrophenyl phosphate (BNPP) but not various phosphomonoesters preserve LIF activity in the presence of the serine esterase inhibitor phenylmethylsulfonyl fluoride (PMSF). In this paper I demonstrate that guanosine 3′,5′‐cyclic monophosphoric acid (3′,5′‐cGMP), a naturally occurring phosphodiester, at concentrations in excess of 10 −5 M also protects LIF against PMSF inactivation. The effect seems specific for the diester bond, its position in the nucleotide, and the guanine base. The possibility that LIF may be a multifunctional or an allosteric enzyme regulated by 3′,5′‐cGMP is discussed.