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Upregulation of macrophage plasma membrane and nuclear phospholipase D activity on ligation of the alpha2-macroglobulin signaling receptor: involvement of heterotrimeric and monomeric G proteins.

Publication ,  Journal Article
Misra, UK; Pizzo, SV
Published in: Arch Biochem Biophys
March 1, 1999

The effect of ligating the alpha2-macroglobulin signaling receptor (alpha2MSR) with receptor-recognized forms of alpha2M (alpha2M*) was studied with respect to phospholipase D (PLD) activity in murine macrophages, their plasma membranes, and nuclei. PLD activity in plasma membranes and nuclei increased linearly up to a ligand concentration of about 100 pM of either alpha2M* or a cloned and expressed receptor binding fragment (RBF). The RBF binding site mutant K1370A, which binds with high affinity to alpha2MSR, also increased nuclear PLD activity comparable to RBF and alpha2M*. Phorbol dibutyrate caused a two- to threefold stimulation of membrane and nuclear PLD activity, whereas PLD activity was nearly abolished by downregulation of protein kinase C; prior treatment with staurosporin, genestein, cyclosporin A, actinomycin D; or chelation of intracellular Ca2+. In permeabilized macrophages, isolated plasma membranes, and nuclei, GTP-gamma-S increased alpha2M*-stimulated PLD activity via a pertussis toxin-insensitive G protein and this effect was abolished on preincubation with GDP-beta-S. Incubation of plasma membranes with polyclonal antibody against sARFII, or the addition of cytosol which was immunoprecipitated with antibody against sARFII, greatly reduced alpha2M*-stimulated PLD activity in the presence of GTP-gamma-S. Preincubation of plasma membranes with GDP-beta-S prior to the addition of GTP-gamma-S and recombinant ARF1 significantly inhibited alpha2M*-stimulation of PLD activity. Nuclear PLD activity was maximally stimulated in the presence of both GTP-gamma-S and rARF1, whereas plasma membrane PLD activity was maximally stimulated in the presence of rARF1, GTP-gamma-S, RhoA, and ATP. In contrast, nuclear PLD activity was not affected by RhoA either alone or in combination with GTP-gamma-S or ATP.

Duke Scholars

Published In

Arch Biochem Biophys

DOI

ISSN

0003-9861

Publication Date

March 1, 1999

Volume

363

Issue

1

Start / End Page

68 / 80

Location

United States

Related Subject Headings

  • rhoA GTP-Binding Protein
  • alpha-Macroglobulins
  • Up-Regulation
  • Signal Transduction
  • Receptors, Immunologic
  • Protein Binding
  • Phospholipase D
  • Mice, Inbred C57BL
  • Mice
  • Macrophages, Peritoneal
 

Citation

APA
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ICMJE
MLA
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Misra, U. K., and S. V. Pizzo. “Upregulation of macrophage plasma membrane and nuclear phospholipase D activity on ligation of the alpha2-macroglobulin signaling receptor: involvement of heterotrimeric and monomeric G proteins.Arch Biochem Biophys 363, no. 1 (March 1, 1999): 68–80. https://doi.org/10.1006/abbi.1998.1074.
Misra, U. K., and S. V. Pizzo. “Upregulation of macrophage plasma membrane and nuclear phospholipase D activity on ligation of the alpha2-macroglobulin signaling receptor: involvement of heterotrimeric and monomeric G proteins.Arch Biochem Biophys, vol. 363, no. 1, Mar. 1999, pp. 68–80. Pubmed, doi:10.1006/abbi.1998.1074.
Journal cover image

Published In

Arch Biochem Biophys

DOI

ISSN

0003-9861

Publication Date

March 1, 1999

Volume

363

Issue

1

Start / End Page

68 / 80

Location

United States

Related Subject Headings

  • rhoA GTP-Binding Protein
  • alpha-Macroglobulins
  • Up-Regulation
  • Signal Transduction
  • Receptors, Immunologic
  • Protein Binding
  • Phospholipase D
  • Mice, Inbred C57BL
  • Mice
  • Macrophages, Peritoneal