Clinical Information

Tryptase, a neutral protease, is a dominant protein component of the secretory granules of human mast cells. There are 2 forms of tryptase, designated as alpha and beta, which are encoded by 2 separate genes.(1) Both are expressed as inactive proenzymes. Alpha-protryptase and beta-protryptase are spontaneously released from resting mast cells. The levels of the protrypases reflect the total number of mass cells within the body but are not an indication of mast cell activation. Beta-protryptase is processed to a mature form, which is stored in granules and released as an active tetramer that is bound to heparan or chondroitin sulfate proteoglycans. In contrast, an amino acid change in alpha-protryptase prevents processing to a mature form. Upon mast cell activation, degranulation releases mature tryptase, which is almost exclusively in the form of beta-tryptase.

During an anaphylactic episode, mast cell granules release tryptase; measurable amounts are found in blood, generally within 30 to 60 minutes.(2) The levels decline under first-order kinetics with half-life of approximately 2 hours. Measurement of tryptase 1 to 6 hours and at least 24 hours after the anaphylactic episode may be useful in demonstrating a return to baseline concentrations and evaluating the kinetics of the response. Tryptase concentrations may also be increased for a period of time following allergen challenge.

Mastocytosis occurs when there is clonal mast-cell proliferation, which leads to tissue accumulation.(3) Mastocytosis can be categorized as cutaneous and systemic. Cutaneous mastocytosis is generally associated with normal or slightly elevated (11.5-20.0 ng/mL) concentrations of tryptase. In systemic mastocytosis, high concentrations may be observed, with greater than 20 ng/mL being a minor criterion for the diagnosis of this condition.