TY - JOUR
T1 - Chapter 18 The Role of Phosphorylation in Phagocyte Activation
AU - Tauber, Alfred I.
AU - Karnad, Anand B.
AU - Ginis, Irene
N1 - Funding Information:
The authors gratefully thank Drs. J. Curnutte and B. Babior for their critical review, and Ann Marie Happnie for hcr expert secretarial assistance in the preparation of this manuscript. This work was supported in part by National Institutes of Health grants A120064, HLB33565 and training grant HLO7501.
PY - 1990/1/1
Y1 - 1990/1/1
N2 - There is active phosphorylation–dephosphorylation when phagocytes are stimulated by a variety of agonists, but the actual assignment of a particular kinase/phosphatase protein substrate pair in the mapping of an activation cascade has not been satisfactorily accomplished. This chapter discusses the rapid progress that has been made in this area of phagocyte cell biology and examines the most compelling evidence for phosphorylation control that has been established in the human neutrophil for the activation of the nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase, the enzymatic activity of the respiratory burst. Of the various soluble and particulate agonists that stimulate oxidase, phorbol ester, phorbol myristate acetate (PMA), is of most relevance, for its receptor, protein kinase C (PKC) represents an important phosphorylating activity that has offered a functional assessment of oxidase activation in intact cells.
AB - There is active phosphorylation–dephosphorylation when phagocytes are stimulated by a variety of agonists, but the actual assignment of a particular kinase/phosphatase protein substrate pair in the mapping of an activation cascade has not been satisfactorily accomplished. This chapter discusses the rapid progress that has been made in this area of phagocyte cell biology and examines the most compelling evidence for phosphorylation control that has been established in the human neutrophil for the activation of the nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase, the enzymatic activity of the respiratory burst. Of the various soluble and particulate agonists that stimulate oxidase, phorbol ester, phorbol myristate acetate (PMA), is of most relevance, for its receptor, protein kinase C (PKC) represents an important phosphorylating activity that has offered a functional assessment of oxidase activation in intact cells.
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U2 - 10.1016/S0070-2161(08)60090-8
DO - 10.1016/S0070-2161(08)60090-8
M3 - Article
AN - SCOPUS:0000203475
VL - 35
SP - 469
EP - 494
JO - Current Topics in Membranes
JF - Current Topics in Membranes
SN - 1063-5823
IS - C
ER -