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TY - JOUR AU - Segal, Anthony W. AU - Heyworth, Paul G. AU - Cockcroft, Shamshad AU - Barrowman, Margaret M. PY - 1985 DA - 1985/08/01 TI - Stimulated neutrophils from patients with autosomal recessive chronic granulomatous disease fail to phosphorylate a Mr-44,000 protein JO - Nature SP - 547 EP - 549 VL - 316 IS - 6028 AB - Phagocytosing neutrophils, monocytes, macrophages and eosino-phils produce a burst of non-mitochondrial respiration that is important for the killing and digestion of microbes. Much of the information about the oxidase system involved comes from studies on patients with chronic granulomatous disease (CGD), a syndrome in which an undue predisposition to infection results from complete absence of this burst of stimulated respiratory activity1. The basis of the oxidase activity is an electron transport chain, the only established component of which is a very unusual b-type cyto-chrome (b−245) (ref. 2). The molecular defect in the X-linked subgroup of CGD is the absence of this cytochrome b−245, which, however, appears to be normal in those subjects with the autosomal recessive mode of inheritance3. In an attempt to identify an abnormality of activation, or an absence or malfunction of a proximal component of the electron transport chain in this latter group, we examined protein phosphorylation in neutrophils after activation of the oxidase with phorbol myristate acetate. All four of the patients studied demonstrated a selective lack of the enhanced phosphorylation of a protein of relative molecular mass (Mr) 44,000 (44K) that was observed in normal subjects and in two CGD patients with an X-linked inheritance. This molecule, therefore, could be an important functional component of the oxidase. SN - 1476-4687 UR - https://doi.org/10.1038/316547a0 DO - 10.1038/316547a0 ID - Segal1985 ER -