Human Leukocyte Migration Inhibitory Factor (LIF)

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Abstract
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 10−5M 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.

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