Platelet release products modulate some aspects of polymorphonuclear leukocyte activation

A, Allegrezza-Giulietti; Serretti, R.; Beccerica, E; Muti, S.; Ferretti, Gianna; Cervini, C

doi:10.1002/jcb.240470310

Cited by 4 publications

(2 citation statements)

References 30 publications

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“…In this study, we obtained no direct evidence regarding the activation status of platelets in fibrin matrices; however, the relative resting status of leukocytes indicates that platelets may be less activated than leukocytes . Taken together with basic diffusability under low‐speed centrifugation, it is plausible that growth factors do not diffuse away to extra‐matrix spaces but stay longer within the matrix.…”

Section: Discussioncontrasting

confidence: 55%

“…Thus, the differences in centrifugal force may not reflect clear differences in platelet and In this study, we obtained no direct evidence regarding the activation status of platelets in fibrin matrices; however, the relative resting status of leukocytes indicates that platelets may be less activated than leukocytes. [26][27][28][29] Based on a number of preclinical and clinical studies and distributors' sales, we speculate that the A-PRF protocol is the most commonly used for the preparation of generic PRF matrices.…”

Section: The Essential Difference Between A-prf and Cgf Preparationmentioning

confidence: 99%

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Distribution of platelets, transforming growth factor‐β1, platelet‐derived growth factor‐BB, vascular endothelial growth factor and matrix metalloprotease‐9 in advanced platelet‐rich fibrin and concentrated growth factor matrices

Takahashi

Tsujino²,

Yamaguchi

et al. 2019

J of Invest & Clin Dent

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Aim Platelet‐rich fibrin (PRF) matrices are compared with regard to their ability to retain and release growth factors. Although this ability is thought to influence regenerative outcomes, it remains unclear how it is regulated. To address this question, we compared advanced PRF (A‐PRF) and concentrated growth factor (CGF) matrices in terms of distribution of platelets, transforming growth factor‐β1, platelet‐derived growth factor‐BB, vascular endothelial growth factor and matrix metalloprotease‐9 (MMP9). Methods Blood samples were obtained in glass tubes and immediately centrifuged to prepare A‐PRF or CGF matrix according to their specific protocols. Both matrices were compressed, embedded in paraffin and subjected to immunohistochemical examination. Results Leukocytes and plasma proteins were localized on the proximal surface including the interface corresponding to buffy coat. In A‐PRF, platelets were distributed homogenously, while growth factors and fibronectin were localized on the distal surface and MMP9 was mainly colocalized with leukocytes. In CGF, in contrast, platelets were localized on and below the proximal surface like leukocytes, growth factors were diffused homogenously and MMP9 was found in the plasma protein layers. Conclusion Although these preparations do not allow accurate quantification, platelet counts and growth factor levels seemed higher and leukocytes were less activated in A‐PRF. This may explain A‐PRF’s higher ability to release growth factors.

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Section: Discussioncontrasting

confidence: 55%

Section: The Essential Difference Between A-prf and Cgf Preparationmentioning

confidence: 99%

Distribution of platelets, transforming growth factor‐β1, platelet‐derived growth factor‐BB, vascular endothelial growth factor and matrix metalloprotease‐9 in advanced platelet‐rich fibrin and concentrated growth factor matrices

Takahashi

Tsujino²,

Yamaguchi

et al. 2019

J of Invest & Clin Dent

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Influence of nifedipine on plasma membrane fluidity and oxidative burst of polymorphonuclear leucocytes

et al. 1995

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It has been demonstrated that the calcium antagonist nifedipine inhibits the reactive oxygen species (ROS) production by polymorphonuclear leucocytes (PMNLs) activated with phorbol myristate acetate (PMA), but the mechanism underlying this effect is still unknown. In the present study we investigated the influence of nifedipine on the PMNL plasma membrane using 1-(4-trimethylaminophenyl)-6-phenyl-1,3,5,hexatriene (TMA-DPH) fluorescence polarization (P) and on PMA- and N-formyl-methionyl-leucyl-phenylalanine (FMLP)-induced ROS production, measured by luminol-dependent chemiluminescence (CL). The plasma membrane fluidity of untreated PMNLs, expressed as P, was 0.371 +/- 0.008. After preincubation of 15 min, nifedipine induced a significant change in P values only at a concentration of 10(-4) M (P = 0.00018). After preincubation of 60 min significant changes in P values were also observed at concentrations of 10(-6) M (P = 0.023) and 10(-7) M (P = 0.023). PMA-induced ROS production by PMNLs was markedly inhibited by nifedipine. Nifedipine also determined a striking change in the FMLP-induced CL response, characterized by both an overall inhibition of PMNL activity and a modification of the kinetics of the oxidative burst (rapid increase in ROS production followed by a pronounced drop in the PMNL response). Such a pattern was found at concentrations of 10(-4) M (preincubation time: 15 min), 10(-6) M and 10(-7) M (preincubation time: 60 min). These findings indicate that nifedipine directly interacts with the PMNLs by inducing a marked decrease in plasma membrane fluidity and an inhibition of the oxidative burst.

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Influence of dichloromethylene diphosphonate on reactive oxygen species production by human neutrophils

et al. 1993

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Biphosphonates suppress bone destruction in various diseases. Several studies have demonstrated the potential use of biphosphonate in arthritis. The results of these studies indicate that the effectiveness of the biphosphonates, for inhibiting the arthritic process, is related to their antiresorptive properties. It has been shown that the generation of reactive oxygen species is associated with the formation of new osteoclasts and enhanced bone resorption. We studied the effects of the dichloromethylene diphosphonate on the reactive oxygen species production by activated polymorphonuclear leucocytes, measured by chemiluminescence. Our results indicate a dose-dependent inhibitory effect of dichloromethylene diphosphonate on reactive oxygen species production by polymorphonuclear leucocytes stimulated with N-formil-methionyl-leucyl-phenylalanine, the calcium ionophore A23187 and phorbol myristate acetate. The mechanisms by which this biphosphonate inhibits the reactive oxygen species production by activated polymorphonuclear leucocytes are discussed.

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Platelet release products modulate some aspects of polymorphonuclear leukocyte activation

Cited by 4 publications

References 30 publications

Distribution of platelets, transforming growth factor‐β1, platelet‐derived growth factor‐BB, vascular endothelial growth factor and matrix metalloprotease‐9 in advanced platelet‐rich fibrin and concentrated growth factor matrices

Distribution of platelets, transforming growth factor‐β1, platelet‐derived growth factor‐BB, vascular endothelial growth factor and matrix metalloprotease‐9 in advanced platelet‐rich fibrin and concentrated growth factor matrices

Influence of nifedipine on plasma membrane fluidity and oxidative burst of polymorphonuclear leucocytes

Influence of dichloromethylene diphosphonate on reactive oxygen species production by human neutrophils

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