TY - JOUR
T1 - Effects of fibronectin on actin organization and respiratory burst activity in neutrophils, monocytes, and macrophages
AU - Yang, Kuender D.
AU - Augustine, Nancy H.
AU - Shaio, Men‐Fang ‐F
AU - Bohnsack, John F.
AU - Hill, Harry R.
PY - 1994/2
Y1 - 1994/2
N2 - Previous studies have shown that fibronectin (Fn) enhances phagocytosis and killing of antibody‐coated bacteria by neutrophils and macrophages. In an attempt to understand the mechanism of this enhancement, we have investigated the effects of Fn on phagocytosis‐related actin organization as well as respiratory burst activity in neutrophils, monocytes and culture‐derived macrophages. Employing an NBD‐phallacidin flow cytometric analysis of filamentous actin formation, we found that Fn promotes rapid actin polymerization within 30 seconds in neutrophils, monocytes, and macrophages, but not lymphocytes. Enhancement of actin polymerization by Fn was concentration‐dependent and mediated by a pertussis toxin‐ but not cholera toxin‐ sensitive G protein. Inhibition of protein kinase C by sphingosine (20 μM), calcium influx by verapamil (0.1 mM), or intracellular calcium mobilization by 8‐(N, N‐diethyl‐amino) octyl‐3,4,5‐trimethoxybenzoate HCI (TMB‐8; 0.1 mM) did not block Fn‐enhanced actin polymerization in phagocytes. Incubation of neutrophils and macrophages on microtiter plates precoated with Fn suppressed superoxide (O2−) production induced by IgG‐ and IgA‐ opsonized group B streptococci. In contrast, Fn significantly enhanced IgA‐ and IgG‐mediated O2− production by freshly isolated monocytes. These data suggest that Fn enhances phagocytosis, presumably through G protein‐coupled cytoskeleton reorganization and augments O2− production by circulating monocytes. In contrast, it appears to suppress O2− production by the active phagocytic cells, neutrophils and macrophages. This may result in enhanced phagocytosis and intracellular killing of microorganisms without damaging interstitial tissues. © 1994 Wiley‐Liss, Inc.
AB - Previous studies have shown that fibronectin (Fn) enhances phagocytosis and killing of antibody‐coated bacteria by neutrophils and macrophages. In an attempt to understand the mechanism of this enhancement, we have investigated the effects of Fn on phagocytosis‐related actin organization as well as respiratory burst activity in neutrophils, monocytes and culture‐derived macrophages. Employing an NBD‐phallacidin flow cytometric analysis of filamentous actin formation, we found that Fn promotes rapid actin polymerization within 30 seconds in neutrophils, monocytes, and macrophages, but not lymphocytes. Enhancement of actin polymerization by Fn was concentration‐dependent and mediated by a pertussis toxin‐ but not cholera toxin‐ sensitive G protein. Inhibition of protein kinase C by sphingosine (20 μM), calcium influx by verapamil (0.1 mM), or intracellular calcium mobilization by 8‐(N, N‐diethyl‐amino) octyl‐3,4,5‐trimethoxybenzoate HCI (TMB‐8; 0.1 mM) did not block Fn‐enhanced actin polymerization in phagocytes. Incubation of neutrophils and macrophages on microtiter plates precoated with Fn suppressed superoxide (O2−) production induced by IgG‐ and IgA‐ opsonized group B streptococci. In contrast, Fn significantly enhanced IgA‐ and IgG‐mediated O2− production by freshly isolated monocytes. These data suggest that Fn enhances phagocytosis, presumably through G protein‐coupled cytoskeleton reorganization and augments O2− production by circulating monocytes. In contrast, it appears to suppress O2− production by the active phagocytic cells, neutrophils and macrophages. This may result in enhanced phagocytosis and intracellular killing of microorganisms without damaging interstitial tissues. © 1994 Wiley‐Liss, Inc.
UR - https://www.scopus.com/pages/publications/0028012136
U2 - 10.1002/jcp.1041580217
DO - 10.1002/jcp.1041580217
M3 - 文章
C2 - 8106571
AN - SCOPUS:0028012136
SN - 0021-9541
VL - 158
SP - 347
EP - 353
JO - Journal of Cellular Physiology
JF - Journal of Cellular Physiology
IS - 2
ER -
