Eosinophilic Leucocytes and Phospholipase B of Rat Tissues

Ottolenghi, Athos

doi:10.1111/j.1365-2184.1986.tb00737.x

Cited by 1 publication

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“…Although our initial evaluation of human eosinophil lysophospholipase activities was engendered by reports of heightened lysophospholipase (then known as phospholipase B or lysolecithinase) activities in rat eosinophils, 37 we focused on a single protein with lysophospholipase activities that was prominent in eosinophil cytoplasm‐rich fractions. Unanticipated by us at the time, CLCs had been identified previously as arising from the cytoplasm and not granules of human eosinophils 3 .…”

Section: Initial Studies Of the Lysophospholipase Activity Of Clc‐pmentioning

confidence: 99%

The Charcot–Leyden crystal protein revisited—A lysopalmitoylphospholipase and more

Weller

Wang

Melo

2020

Journal of Leukocyte Biology

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The Charcot–Leyden crystal protein (CLC‐P), a constituent of human and not mouse eosinophils, is one of the most abundant proteins within human eosinophils. It has a propensity to form crystalline structures, Charcot–Leyden crystals, which are hallmarks in their distinctive extracellular crystalline forms as markers of eosinophilic inflammation. The functions of CLC‐P within eosinophils have been uncertain. Although the action of CLC‐P as a lysophospholipase has been questioned, assays of chromatographically purified CLC‐P and crystal‐derived CLC‐P as well as studies of transfected recombinant CLC‐P have consistently documented that CLC‐P endogenously expresses lysophospholipase activity, releasing free palmitate from substrate lysopalmitoylphosphatidylcholine. Rather than acting solely as a hydrolytic enzyme to release palmitate from a lysolipid substrate, some other lysophospholipases function more dominantly as acyl‐protein thioesterases (APTs), enzymes that catalyze the removal of thioester‐linked, long chain fatty acids, such as palmitate, from cysteine residues of proteins. As such APTs participate in palmitoylation, a post‐translational modification that can affect membrane localization, vesicular transport, and secretion. CLC‐P has attributes of an APT. Thus, whereas CLC‐P expresses inherent lysophospholipase activity, like some other lysophospholipase enzymes, it likely also functions in regulating the dynamic palmitoylation cycle, including, given its dominant subplasmalemmal location, at the human eosinophil's plasma membrane.

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Section: Initial Studies Of the Lysophospholipase Activity Of Clc‐pmentioning

confidence: 99%