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B Phosphorylation for Induction of Proinflammatory Cytokines Synthesis by Macrophages Indicates Functional Similarity of Receptors Triggered by Glycosylphosphatidylinositol Anchors from Parasitic Protozoa and Bacterial Lipopolysaccharide1
*
René Rachou Research Center-Fundaçao Oswaldo Cruz and Department of Biochemistry and Immunology, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, Brazil;
Department of Parasitology, Instituto de Ciências Biológicas, Universidade de São Paulo, São Paulo, Brazil;
Discipline of Cell Biology Biologia Celular, Universidade Federal de São Paulo, São Paulo, Brazil; and
Division of Molecular Parasitology and
¶ Medical Research Council Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee, United Kingdom
In the present study, we evaluated the ability of
GPI-anchored mucin-like glycoproteins purified from Trypanosoma
cruzi trypomastigotes (tGPI-mucin) to trigger phosphorylation
of different mitogen-activated protein kinases (MAPKs) and related
transcription factors in inflammatory macrophages. Kinetic experiments
show that the peak of extracellular signal-related kinase
(ERK)-1/ERK-2, stress-activated protein kinase (SAPK)
kinase-1/mitogen-activated protein kinase (MAPK) kinase-4, and
p38/SAPK-2, phosphorylation occurs between 15 and 30 min after
macrophage stimulation with tGPI-mucin or GPI anchors highly purified
from tGPI-mucins (tGPI). The use of the specific inhibitors of
ERK-1/ERK-2 (PD 98059) and p38/SAPK-2 (SB 203580) phosphorylation also
indicates the role of MAPKs, with possible involvement of cAMP response
element binding protein, in triggering TNF-
and IL-12 synthesis by
IFN-
-primed-macrophages exposed to tGPI or tGPI-mucin. In addition,
tGPI-mucin and tGPI were able to induce phosphorylation of I
B, and
the use of SN50 peptide, an inhibitor of NF-B translocation,
resulted in 70% of TNF- synthesis by macrophages exposed to
tGPI-mucin. Finally, the similarity of patterns of MAPK and IB
phosphorylation, the concentration of drugs required to inhibit
cytokine synthesis, as well as cross-tolerization exhibited by
macrophages exposed to tGPI, tGPI-mucin, or bacterial LPS, suggest that
receptors with the same functional properties are triggered by these
different microbial glycoconjugates.
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