Department of Pharmacy, University of Pisa Via Bonanno 6 56126 Pisa Italy giulia.bononi@farm.unipi.it valentina.citi@unipi.it alma.martelli@unipi.it giulio.poli@unipi.it tiziano.tuccinardi@unipi.it carlotta.granchi@unipi.it lara.testai@unipi.it vincenzo.calderone@unipi.it filippo.minutolo@unipi.it.
Department of Pharmacy, University of Pisa Via Bonanno 6 56126 Pisa Italy giulia.bononi@farm.unipi.it valentina.citi@unipi.it alma.martelli@unipi.it giulio.poli@unipi.it tiziano.tuccinardi@unipi.it carlotta.granchi@unipi.it lara.testai@unipi.it vincenzo.calderone@unipi.it filippo.minutolo@unipi.it.
Department of Pharmacy, University of Pisa Via Bonanno 6 56126 Pisa Italy giulia.bononi@farm.unipi.it valentina.citi@unipi.it alma.martelli@unipi.it giulio.poli@unipi.it tiziano.tuccinardi@unipi.it carlotta.granchi@unipi.it lara.testai@unipi.it vincenzo.calderone@unipi.it filippo.minutolo@unipi.it.
Center for Instrument Sharing of the University of Pisa (CISUP) Lungarno Pacinotti 43 56126 Pisa Italy.
Department of Pharmacy, University of Pisa Via Bonanno 6 56126 Pisa Italy giulia.bononi@farm.unipi.it valentina.citi@unipi.it alma.martelli@unipi.it giulio.poli@unipi.it tiziano.tuccinardi@unipi.it carlotta.granchi@unipi.it lara.testai@unipi.it vincenzo.calderone@unipi.it filippo.minutolo@unipi.it.
Department of Pharmacy, University of Pisa Via Bonanno 6 56126 Pisa Italy giulia.bononi@farm.unipi.it valentina.citi@unipi.it alma.martelli@unipi.it giulio.poli@unipi.it tiziano.tuccinardi@unipi.it carlotta.granchi@unipi.it lara.testai@unipi.it vincenzo.calderone@unipi.it filippo.minutolo@unipi.it.
Center for Instrument Sharing of the University of Pisa (CISUP) Lungarno Pacinotti 43 56126 Pisa Italy.
Department of Pharmacy, University of Pisa Via Bonanno 6 56126 Pisa Italy giulia.bononi@farm.unipi.it valentina.citi@unipi.it alma.martelli@unipi.it giulio.poli@unipi.it tiziano.tuccinardi@unipi.it carlotta.granchi@unipi.it lara.testai@unipi.it vincenzo.calderone@unipi.it filippo.minutolo@unipi.it.
Center for Instrument Sharing of the University of Pisa (CISUP) Lungarno Pacinotti 43 56126 Pisa Italy.
Department of Pharmacy, University of Pisa Via Bonanno 6 56126 Pisa Italy giulia.bononi@farm.unipi.it valentina.citi@unipi.it alma.martelli@unipi.it giulio.poli@unipi.it tiziano.tuccinardi@unipi.it carlotta.granchi@unipi.it lara.testai@unipi.it vincenzo.calderone@unipi.it filippo.minutolo@unipi.it.
Center for Instrument Sharing of the University of Pisa (CISUP) Lungarno Pacinotti 43 56126 Pisa Italy.
Department of Pharmacy, University of Pisa Via Bonanno 6 56126 Pisa Italy giulia.bononi@farm.unipi.it valentina.citi@unipi.it alma.martelli@unipi.it giulio.poli@unipi.it tiziano.tuccinardi@unipi.it carlotta.granchi@unipi.it lara.testai@unipi.it vincenzo.calderone@unipi.it filippo.minutolo@unipi.it.
Center for Instrument Sharing of the University of Pisa (CISUP) Lungarno Pacinotti 43 56126 Pisa Italy.
Department of Pharmacy, University of Pisa Via Bonanno 6 56126 Pisa Italy giulia.bononi@farm.unipi.it valentina.citi@unipi.it alma.martelli@unipi.it giulio.poli@unipi.it tiziano.tuccinardi@unipi.it carlotta.granchi@unipi.it lara.testai@unipi.it vincenzo.calderone@unipi.it filippo.minutolo@unipi.it.
Center for Instrument Sharing of the University of Pisa (CISUP) Lungarno Pacinotti 43 56126 Pisa Italy.
Department of Animal Sciences, The Robert H. Smith Faculty of Agriculture, Food and Environment, The Hebrew University of Jerusalem, Rehovot 761001, Israel.
School of Pharmaceutical Science and Technology, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou 310024, China.
State Key Laboratory of Chemical Biology, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
The complement system provides vital immune protection against infectious agents by labeling them with complement fragments that enhance phagocytosis by immune cells. Many details of complement-mediat...
The complement receptors C3aR and C5aR1, whose signaling is selectively activated by anaphylatoxins C3a and C5a, are important regulators of both innate and adaptive immune responses. Dysregulations o...
An immunosuppressive microenvironment causes poor tumor T cell infiltration and is associated with reduced patient overall survival in colorectal cancer. How to improve treatment responses in these tu...
Following traumatic brain injury (TBI), a neuroinflammatory response can persist for years and contribute to the development of chronic neurological manifestations. Complement plays a central role in ...
Sarcoidosis (SA) is a granulomatous disorder, which mostly affects the lungs. Its clinical characteristics resemble tuberculosis (TB), but its treatment is different. The etiology of SA is unknown; ho...
Phagocytosis is the mechanism of the internalization of large particles, microorganisms and cellular debris. The complement pathway represents one of the first mechanisms of defense against infection ...
Here, we reveal that Dynamin-2 is recruited concomitantly with polymerized actin at the phagocytic cup and during phagosome formation and closure. Inhibition of Dynamin activity leads to stalled phago...
Dynamin-2 regulates the assembly of the F-actin phagocytic cup for successful CR3-mediated phagocytosis....
These results highlight an important role for Dynamin-2 in actin remodeling downstream of integrins....
Autoantibody production is a hallmark of systemic sclerosis (SSc) and the most extensively studied role of B cells in the pathogenesis of the disease. However, the potential involvement of innate immu...
Inhibition of terminal complement in neuromyelitis optica spectrum disorder (NMOSD) using eculizumab helps prevent relapses, but the exact mechanism of action of the drug remains unclear. Similarly, g...
Peripheral blood cell (PBMC) samples from 45 patients with NMOSD with aquaporin 4 (AQP4)-IgG, 18 disease controls, and 19 normal controls were analyzed for CD16 expression and complement receptors in ...
At baseline, the number of NKT cells was increased in NMOSD (p < 0.001), but the proportion that was CD16 positive was lower compared to normal and disease controls (p = 0.0012). NK cell count was nor...
Our results support an immunopathogenesis model in which complement pathway activation in NK/NKT cells upregulates CD16 expression that binds to antibody/antigen complexes. In the context of NMOSD, th...
To examine concentrations of circulating antibodies targeting C3a and C5a complement receptors in antineutrophil cytoplasmic autoantibody (ANCA)-associated vasculitis (AAV) and analyze their associati...
Concentrations of antibodies against C3a and C5a complement receptors (anti-C3aR and anti-C5aR) and plasma complement fragments C3a and C5a were determined in patients with AAV (n = 110; granulomatosi...
In AAV, anti-C3aR and anti-C5aR antibodies were decreased (P = 0.0026 and P ≤ 0.0001, respectively). In remission, anti-C3aR antibody concentrations rose to values comparable to healthy donors, wherea...
Low concentrations of anti-C5aR antibodies reflect disease activity and are associated with an increased risk for relapse in AAV....
In gastric cancer (GC), the therapeutic response of immune checkpoint blockade (ICB) remains suboptimal. Targeting myeloid cell checkpoints might be feasible as adjuvant to current ICB regimens. We so...