Phospholipase A1 from Trypanosoma cruzi infective stages generates lipid messengers that activate host cell protein kinase c

Parasitology ◽  
2006 ◽  
Vol 134 (4) ◽  
pp. 491-502 ◽  
Author(s):  
M. L. BELAUNZARÁN ◽  
M. J. WAINSZELBAUM ◽  
E. M. LAMMEL ◽  
G. GIMENEZ ◽  
M. M. ALOISE ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Trypanosoma Cruzi ◽  
Vero Cell ◽  
Host Cell ◽  
Host Cells ◽  
Cell Protein ◽  
Host Cell Protein ◽  
Cell Lipid ◽  
Kinase C

Here we have studied phospholipase A1 (Plase A1) from Trypanosoma cruzi infective stages and it's possible role regarding the interaction with mammalian host cells. Plase A1 was mainly detected as a membrane-bound activity in the infective amastigote and trypomastigote stages, being remarkably higher with respect to the non-infective epimastigotes. It is noteworthy that only the infective stages secreted Plase A1. Moreover, along the differentiation process from epimastigotes into metacyclic trypomastigotes, the secreted enzyme activity increased simultaneously with the appearance of metacyclic forms, as expected. Since this enzyme is predominantly membrane-associated and secreted by the infective stages, Vero cell lipid profile modifications were analysed after interaction with either intact infective parasites or purified T. cruzi Plase A1. Significant changes in Vero cell lipid composition were observed, with the appearance of free fatty acids, diacylglycerol and lysophosphatidylcholine. Concomitantly with the generation of second lipid messengers, host cell protein kinase C activation was demonstrated. These results indicate that T. cruzi Plase A1 could play a critical role in the early events of parasite-host cell interaction that precede invasion.

scholarly journals The Campylobacter jejuni CiaD effector co-opts the host cell protein IQGAP1 to promote cell entry

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Nicholas M. Negretti ◽  
Christopher R. Gourley ◽  
Prabhat K. Talukdar ◽  
Geremy Clair ◽  
Courtney M. Klappenbach ◽  
...  
Keyword(s):  
Host Cell ◽  
Campylobacter Jejuni ◽  
Foodborne Pathogen ◽  
Small Gtpase ◽  
Host Cells ◽  
Cell Protein ◽  
Host Cell Protein ◽  
Cell Binding ◽  
Actin Reorganization ◽  
Cell Cytosol

AbstractCampylobacter jejuni is a foodborne pathogen that binds to and invades the epithelial cells lining the human intestinal tract. Maximal invasion of host cells by C. jejuni requires cell binding as well as delivery of the Cia proteins (Campylobacter invasion antigens) to the host cell cytosol via the flagellum. Here, we show that CiaD binds to the host cell protein IQGAP1 (a Ras GTPase-activating-like protein), thus displacing RacGAP1 from the IQGAP1 complex. This, in turn, leads to the unconstrained activity of the small GTPase Rac1, which is known to have roles in actin reorganization and internalization of C. jejuni. Our results represent the identification of a host cell protein targeted by a flagellar secreted effector protein and demonstrate that C. jejuni-stimulated Rac signaling is dependent on IQGAP1.

Rapid response of protein synthesis to insulin in 3T3 cells: Effects of protein kinase C depletion and differences from the response to serum repletion

1986 ◽  
Vol 6 (9) ◽  
pp. 797-804 ◽  
Author(s):  
John E. Hesketh ◽  
Gillian P. Campbell ◽  
Peter J. Reeds
Keyword(s):  
Protein Synthesis ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Actinomycin D ◽  
Calf Serum ◽  
Cell Protein ◽  
Foetal Calf Serum ◽  
3T3 Cells ◽  
Kinase C

Quiescent 3T3 cells grown in media containing 4% foetal calf serum showed different responses to insulin and to serum repletion (to 12%). Insulin stimulated protein synthesis within 1 h and this early response was insensitive to actinomycin D. The later insulin response showed progressive sensitivity to actinomycin D. The serum response was slower, not occurring until 1 h, and was inhibited by actinomycin D. Depletion of cell protein kinase C by pre-treatment with phorbol ester caused a total block of the immediate response to insulin but had little effect on the response to serum or the later response to insulin. Acute phorbol ester treatment stimulated protein synthesis.

scholarly journals Host cell Ca2+ and protein kinase C regulate innate recognition of Toxoplasma gondii

2006 ◽  
Vol 119 (22) ◽  
pp. 4789-4789 ◽  
Author(s):  
K. S. Masek ◽  
J. Fiore ◽  
M. Leitges ◽  
S.-F. Yan ◽  
B. D. Freedman ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Toxoplasma Gondii ◽  
Host Cell ◽  
Kinase C ◽  
Innate Recognition

Protein kinase C in Trypanosoma cruzi epimastigote forms: partial purification and characterization

1989 ◽  
Vol 36 (2) ◽  
pp. 101-108 ◽  
Author(s):  
María L. Gómez ◽  
Leonardo Erijman ◽  
Silvia Arauzo ◽  
Héctor N. Torres ◽  
María T. Téllez-Iñón
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Trypanosoma Cruzi ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Kinase C

scholarly journals Bryostatin 1 activates protein kinase C and induces monocytic differentiation of HL-60 cells

Blood ◽  
1988 ◽  
Vol 72 (1) ◽  
pp. 208-213 ◽  
Author(s):  
RM Stone ◽  
E Sariban ◽  
GR Pettit ◽  
DW Kufe
Keyword(s):  
Gene Expression ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Growth Inhibition ◽  
Phorbol Ester ◽  
Phorbol Esters ◽  
Cell Protein ◽  
Monocytic Differentiation ◽  
Bryostatin 1 ◽  
Kinase C

Phorbol esters induce the human HL-60 promyelocytic cell line to differentiate along a monocytic pathway. This induction of differentiation may involve phorbol ester-induced activation of the phospholipid- and calcium-dependent protein kinase C. Bryostatin 1, a macrocyclic lactone, has been shown to compete with phorbol esters for binding to protein kinase C. We have confirmed that bryostatin 1 translocates activity of protein kinase C from the cytosolic to membrane fractions of HL-60 cells. The present results also demonstrate that bryostatin 1 (10 nmol/L) induces monocytic differentiation of HL- 60 cells as determined by adherence, growth inhibition, appearance of monocyte cell surface antigens, and alpha-naphthyl acetate esterase staining. Furthermore, bryostatin 1 (10 nmol/L) downregulated c-myc expression and induced c-fos, c-fms, and tumor necrosis factor transcripts. These changes in gene expression induced by bryostatin 1 are similar to those associated with phorbol ester-induced monocytic differentiation of HL-60 cells. In contrast, exposure to a higher concentration of bryostatin 1 (100 nmol/L) had less of an effect on growth inhibition of HL-60 cells and changes in gene expression. Moreover, 100 nmol/L bryostatin 1 antagonized the cytostatic effects and adherence induced by phorbol esters. Our results thus suggest that bryostatin 1 activates HL-60 cell protein kinase C and that this effect is associated with induction of monocytic differentiation.

scholarly journals Phospholipase C activates protein kinase C and induces monocytic differentiation of HL-60 cells

Blood ◽  
1988 ◽  
Vol 72 (2) ◽  
pp. 739-744 ◽  
Author(s):  
RM Stone ◽  
BL Weber ◽  
DR Spriggs ◽  
DW Kufe
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase C ◽  
Inositol Phosphates ◽  
Cell Protein ◽  
Mrna Levels ◽  
Monocytic Differentiation ◽  
Cell Surface Antigens ◽  
Monocytic Cell ◽  
Kinase C

Phospholipase C (PLC)-mediated hydrolysis of membrane phospholipids results in the production of diacylglycerol, inositol phosphates, and choline metabolites. Inositol triphosphate increases calcium levels, while diacylglycerol activates protein kinase C. The present studies demonstrate that exogenous PLC generates inositol phosphates, releases choline metabolites, and activates protein kinase C in human HL-60 promyelocytic leukemia cells. PLC also induced monocytic differentiation of HL-60 cells as manifested by adherence, growth inhibition, and appearance of monocytic cell surface antigens. Furthermore, PLC treatment decreased c-myc mRNA levels and induced c- fos, c-fms, and tumor necrosis factor transcripts. The changes in gene expression induced by PLC are similar to those previously shown to be associated with phorbol ester-induced monocytic differentiation of HL- 60 cells. Our results thus demonstrate that exogenous PLC activates HL- 60 cell protein kinase C and that this effect is associated with induction of monocytic differentiation. PLC may therefore play a role in transducing signals from physiological inducers of monocytic differentiation.

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