The endothelium as physiological source of properdin: role of wall shear stress

Bongrazio, Mauro; Pries, Axel R.; Zakrzewicz, Andreas

doi:10.1016/s0161-5890(02)00215-8

Cited by 50 publications

(44 citation statements)

References 32 publications

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“…Properdin is significant in the defense against Neisseria species, and Neisseria gonorrhea was claimed to directly bind properdin (7), findings that have been extrapolated to N. meningitidis (37). Endothelial cells are a source of serum properdin (38), and properdin has been shown to interact with various glycosaminoglycans on endogenous cells (25,39,40).…”

Section: Discussionmentioning

confidence: 99%

Properdin binding to complement activating surfaces depends on initial C3b deposition

Harboe

Johnson

Nymo

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Two functions have been assigned to properdin; stabilization of the alternative convertase, C3bBb, is well accepted, whereas the role of properdin as pattern recognition molecule is controversial. The presence of nonphysiological aggregates in purified properdin preparations and experimental models that do not allow discrimination between the initial binding of properdin and binding secondary to C3b deposition is a critical factor contributing to this controversy. In previous work, by inhibiting C3, we showed that properdin binding to zymosan and Escherichia coli is not a primary event, but rather is solely dependent on initial C3 deposition. In the present study, we found that properdin in human serum bound dose-dependently to solid-phase myeloperoxidase. This binding was dependent on C3 activation, as demonstrated by the lack of binding in human serum with the C3-inhibitor compstatin Cp40, in C3-depleted human serum, or when purified properdin is applied in buffer. Similarly, binding of properdin to the surface of human umbilical vein endothelial cells or Neisseria meningitidis after incubation with human serum was completely C3-dependent, as detected by flow cytometry. Properdin, which lacks the structural homology shared by other complement pattern recognition molecules and has its major function in stabilizing the C3bBb convertase, was found to bind both exogenous and endogenous molecular patterns in a completely C3-dependent manner. We therefore challenge the view of properdin as a pattern recognition molecule, and argue that the experimental conditions used to test this hypothesis should be carefully considered, with emphasis on controlling initial C3 activation under physiological conditions.

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Section: Discussionmentioning

confidence: 99%

Properdin binding to complement activating surfaces depends on initial C3b deposition

Harboe

Johnson

Nymo

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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“…HUVECs were isolated and cultivated as described previously 14 using Endothelial Cell Basal Medium MV1 with Cell Growth Supplement Pack MV1 (PromoCell, Heidelberg, Germany) and used at passage one. All of the cells were exposed to shear stress 1 day after confluence.…”

Section: Experimental Procedures Cell Culturementioning

confidence: 99%

“…Using the Transcriptor first-strand cDNA synthesis kit (Roche Diagnostics, Mannheim, Germany), cDNA was synthesized from 2 g of total RNA using oligo dT [12][13][14][15][16][17][18] and 5 U of Avian Myeloblastosis Virus reverse transcriptase at 50°C for 60 minutes, followed by heating to 85°C for 5 minutes.…”

Section: Rna Isolation and Reverse Transcriptionmentioning

confidence: 99%

Pulsatile Atheroprone Shear Stress Affects the Expression of Transient Receptor Potential Channels in Human Endothelial Cells

et al. 2012

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Abstract-The goal of the study was to assess whether pulsatile atheroprone shear stress modulates the expression of transient receptor potential (TRP) channels, TRPC3, TRPC6, TRPM7, and TRPV1 mRNA, in human umbilical vascular endothelial cells. Exposure of cultured vascular endothelial cells to defined shear stress, producing a constant laminar flow (generating a shear stress of 6 dyne/cm 2 ), laminar pulsatile atheroprotective flow (with a mean shear stress of 20 dyne/cm 2 ), or laminar atheroprone bidirectional flow (with a mean shear stress of 0 dyne/cm 2 ) differentially induced TRPC6 and TRPV1 mRNA as measured by quantitative real-time RT-PCR and normalized to GAPDH expression. Thereby, TRPC6 and TRPV1 mRNA expressions were significantly increased after 24 hours of exposure to an atheroprone flow profile compared with an atheroprotective flow profile. Furthermore, the expression of transcription factors GATA1 and GATA4 was significantly correlated with the expression of TRPC6 mRNA. In contrast, after 24 hours of constant laminar flow, the expression of TRPC6 and TRPV1 mRNA was unchanged, whereas the expression of TRPC3 and TRPM7 was significantly higher in endothelial cells exposed to shear stress in comparison with endothelial cells grown under static conditions. There was a significant association between the expression of TRPC6 and tumor necrosis factor-␣ mRNA in human vascular tissue. No-flow and atheroprone flow conditions are equally characterized by an increase in the expression of tumor necrosis factor-␣; however, inflammation-associated endothelial cell reactions may be further aggravated at atheroprone flow conditions by the increase of TRPV1 and TRPC6, as observed in our study. (Hypertension. 2012;59:1232-1240.)

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“…It is a plasma protein synthesized by monocytes, hepatocytes, mast cells, T cells (45,46,49), and shear-stressed endothelial cells (6) and is also a component of the secondary granules in neutrophils (PMN) (53). Patients with properdin deficiency have a higher risk of meningococcal disease than the general population (14), and an association has also recently been found with recurrent otitis media and pneumonia (44).…”

mentioning

confidence: 99%

Native Properdin Binds toChlamydia pneumoniaeand Promotes Complement Activation

2011

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Activation of complement represents one means of natural resistance to infection from a wide variety of potential pathogens. Recently, properdin, a positive regulator of the alternative pathway of complement, has been shown to bind to surfaces and promote complement activation. Here we studied whether properdinmediated complement activation occurs on the surface of Chlamydia pneumoniae, an obligate intracellular Gram-negative bacterium that causes 10 to 20% of community-acquired pneumonia. We have determined for the first time that the physiological P 2 , P 3 , and P 4 forms of human properdin bind to the surface of Chlamydia pneumoniae directly. The binding of these physiological forms accelerates complement activation on the Chlamydia pneumoniae surface, as measured by C3b and C9 deposition. Finally, properdin-depleted serum could not control Chlamydia pneumoniae infection of HEp-2 cells compared with normal human serum. However, after addition of native properdin, the properdin-depleted serum recovered the ability to control the infection. Altogether, our data suggest that properdin is a pattern recognition molecule that plays a role in resistance to Chlamydia infection.

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The endothelium as physiological source of properdin: role of wall shear stress

Cited by 50 publications

References 32 publications

Properdin binding to complement activating surfaces depends on initial C3b deposition

Properdin binding to complement activating surfaces depends on initial C3b deposition

Pulsatile Atheroprone Shear Stress Affects the Expression of Transient Receptor Potential Channels in Human Endothelial Cells

Native Properdin Binds toChlamydia pneumoniaeand Promotes Complement Activation

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