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Intracellular pH changes during neutrophil activation: Na+/H+ antiport. J Leukoc Biol 1987 Jan;41(1):25-32

Date

01/01/1987

Pubmed ID

3027217

DOI

10.1002/jlb.41.1.25

Abstract

Activation of the Na+/H+ antiport mechanism was studied in human neutrophils by monitoring intracellular pH with a carboxyfluorescein derivative. N-formyl-methionyl-leucyl-phenylalanine (FMLP) and phospholipase C (PLC) induced biphasic pH changes. Amiloride, which inhibits the antiport, completely blocked alkalinization but enhanced acidification. Polymyxin B, which inhibits protein kinase C, only blocked alkalinization. Activation with phorbol 12-myristate 13-acetate (PMA) led to alkalinization only; this was inhibited by amiloride or polymyxin B. Thus, during polymorphonuclear leukocyte (PMN) activation, intracellular alkalinization appears to be mediated by an amiloride-sensitive Na+/H+ antiport. Antiport activity can also be blocked indirectly by inhibition of protein kinase C activity. Early intracellular acidification does not appear to require kinase activity but is observed when phospholipids are remodeled with PLC. The antiport was also activatable by hypertonic buffered media. This response did not appear to be mediated by protein kinase C because it was unaffected by polymyxin B. Finally, superoxide generation was investigated. It is affected by, but not soley controlled by, either antiport or protein kinase C activity.

Author List

Weisman SJ, Punzo A, Ford C, Sha'afi RI

Author

Steven J. Weisman MD Professor in the Anesthesiology department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Amiloride
Humans
Hydrogen-Ion Concentration
Hypertonic Solutions
N-Formylmethionine Leucyl-Phenylalanine
Neutrophils
Polymyxin B
Protein Kinase C
Protons
Sodium
Superoxides
Tetradecanoylphorbol Acetate
Type C Phospholipases
jenkins-FCD Prod-484 8aa07fc50b7f6d102f3dda2f4c7056ff84294d1d