Proteomic analysis of extracellular vesicles derived from platelet concentrates treated with Mirasol® identifies biomarkers of platelet storage lesion

Hermida-Nogueira, Lidia; Barrachina, María N.; Izquierdo, Irene; García-Vence, Maria; Lacerenza, Serena; Bravo, Susana B.; Castrillo, Azucena; García, Agustín Merino

doi:10.1016/j.jprot.2019.103529

Cited by 28 publications

(32 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…After in-gel tryptic digestion of bands, peptides were extracted following an established protocol 35 , carrying out three incubations of 20 min each with 60% acetonitrile and 0.5% HCOOH. The resulting peptide extracts were pooled, concentrated and stored at − 20 °C.…”

Section: Lc-ms/ms Identification In the Secretome Profile Analysismentioning

confidence: 99%

“…Data dependent Acquisition workflow was performed in a TripleTOF 6600 System (Sciex, Redwood City, CA, USA) using parameters previously set up 35 . Source and interface conditions were the following: ionspray voltage floating (ISVF) 5,500 V, curtain gas (CUR) 25, collision energy (CE) 10 and ion source gas 1 (GS1) 25.…”

Section: Lc-ms/ms Identification In the Secretome Profile Analysismentioning

confidence: 99%

“…Samples from each condition (day 3, 7 and 21) were pooled using equal mixtures from the original ones in order to get a good representation of the peptides and proteins present in all samples. Run specifications were followed by an establish protocol 35 . Four microliters of each pool were separated into a micro-LC system Ekspert nLC425 (Eksigent Technologies, Dublin, CA, USA) using the same conditions as mentioned above.…”

Section: Differential Secretome Protein Quantitation At Days 3 7 Andmentioning

confidence: 99%

“…Samples were analysed by SWATH-MS acquisition method 35 performed in a TripleTOF 6600 LC-MS/MS system (AB Sciex, Redwood City, CA, USA) making 3 technical replicates per sample. For each sample set, the width of the 100 variable windows was optimized according to the ion density found in the DDA runs using a SWATH variable window calculator worksheet from Sciex (Sciex, Redwood City, CA, USA).…”

Section: Differential Secretome Protein Quantitation At Days 3 7 Andmentioning

confidence: 99%

See 3 more Smart Citations

Deciphering the secretome of leukocyte-platelet rich fibrin: towards a better understanding of its wound healing properties

Hermida-Nogueira

Barrachina

Morán

et al. 2020

Sci Rep

Self Cite

View full text Add to dashboard Cite

Leukocyte-platelet rich fibrin (L-PRF) is extensively used in the dentistry field and other clinical scenarios due to its regeneration properties. the goal of the present study was to depict the L-pRf secretome and how it changes over time. We obtained L-PRF membranes and cultured them in DMEM. The secretome was collected at days 3, 7 and 21. The secretome at day 3 was analysed by LC-MS/ MS and differences over time were analysed by Sequential Window Acquisition of all Theoretical Mass Spectra (SWATH). Overall, 705 proteins were identified in the secretome of L-PRF membranes after 3 days of culture, including growth factors (EGF, PDGFA) and proteins related to platelet and neutrophil degranulation. A total of 202 differentially secreted proteins were quantified by SWATH when comparing secretomes at days 3, 7 and 21. Most of them were enriched at day 3 such as MMP9, TSP1 and CO3. On the contrary, fibrinogen and CATS were found down-regulated at day 3. Growth factor and western blotting analysis corroborated the proteomic results. This is the most detailed proteome analysis of the L-PRF secretome to date. Proteins and growth factors identified, and their kinetics, provide novel information to further understand the wound healing properties of L-pRf. In the last two decades, the use of platelet-rich concentrates (PRC) has become very popular in different fields, especially in dentistry, due to their regeneration properties. Different scientists and companies have developed methods to obtained PRC with presence or absence of leukocytes but all of them with addition of anticoagulants to the tubes. In 2001, Choukroun et al. developed the second generation of PRC, Leukocyte platelet rich fibrin (L-PRF) 1 , which is obtained by blood centrifugation without anticoagulant in the tubes. Nowadays, L-PRF is the most commonly used PRC since it is easy to obtain and can be applied as a gel or compressed into a membrane depending on the application site. It has been mostly used in a dentistry field, especially for the treatment of osteonecrosis 2,3 , implant placement in bone-deficient sites 4 and sinus floor elevation 5. Additionally, L-PRF has started to be used in other clinical scenarios, for example for the treatment of chronic wounds, leg ulcers or diabetic foot 6 or for the treatment of ocular lesions 7. Wound healing is a complex process, which encompass different phases: haemostasis, inflammation, proliferation and remodelling. In each phase, different cell types take part in order to regenerate the tissue. Two types of blood cells, platelets and leukocytes, are among the cells that participate first. Growth factors, cytokines and other proteins released by these blood cells have chemoattractant properties that contribute to wound repair 8-10 .

show abstract

Section: Lc-ms/ms Identification In the Secretome Profile Analysismentioning

confidence: 99%

Section: Lc-ms/ms Identification In the Secretome Profile Analysismentioning

confidence: 99%

Section: Differential Secretome Protein Quantitation At Days 3 7 Andmentioning

confidence: 99%

Section: Differential Secretome Protein Quantitation At Days 3 7 Andmentioning

confidence: 99%

See 2 more Smart Citations

Deciphering the secretome of leukocyte-platelet rich fibrin: towards a better understanding of its wound healing properties

Hermida-Nogueira

Barrachina

Morán

et al. 2020

Sci Rep

Self Cite

View full text Add to dashboard Cite

show abstract

“…Their presence in platelet concentrates is associated with transfusion refractoriness and transfusion-related acute lung injury (TRALI) caused by inflammatory mediators, such as CD40L (CD154), P-selectin and mitochondrial DNA (of platelet origin), that constitute a strong pro-inflammatory stimulus (118)(119)(120)(121). It is because of that, that screening and characterizing the microparticle content in platelet concentrates constitutes a new quality improvement initiative for hospital blood banks in order to optimize the use of this limited blood product (122,123).…”

Section: Platelets As Carriers: "Beware Of Platelets Bearing Gifts"mentioning

confidence: 99%

Platelet-derived bio-products: Classification update, applications, concerns and new perspectives

Acebes-Huerta

Arias-Fernández

Bernardo

et al. 2020

Transfusion and Apheresis Science

View full text Add to dashboard Cite

Platelet derived bio-products in the form of platelet rich plasma, plasma rich in growth factors, or plasma-free platelet releasates, are being studied worldwide with the aim of proving their efficacy in tissue regeneration within many different clinical areas, such as traumatology, maxillofacial surgery, ophthalmology, dermatology and otorhinolaryngology, amongst others. The current lack of consensus in the preparation method and application form, or in the quality assessment of each bio-product, precludes adequate interpretation of the relevance of reported clinical outcomes, and while many clinicians are very positive about them, as many are sceptic. Relevant aspects of these products are considered to propose a classification nomenclature, which would aid at the comprehensive comparison of clinical outcomes of bio-products of the same characteristics. Finally, the uses of platelet-derived bio-products in in vitro culture (for cell therapy purposes) as a substitute of animal-origin sera, and other future perspectives of applications of platelet-derived bio-products are discussed.

show abstract

Glutathione S‐transferase omega class 1 (GSTO1)‐associated large extracellular vesicles are involved in tumor‐associated macrophage‐mediated cisplatin resistance in bladder cancer

Pan,

Chu,

Lin

et al. 2024

Molecular Oncology

View full text Add to dashboard Cite

Bladder cancer poses a significant challenge to chemotherapy due to its resistance to cisplatin, especially at advanced stages. Understanding the mechanisms behind cisplatin resistance is crucial for improving cancer therapy. The enzyme glutathione S‐transferase omega class 1 (GSTO1) is known to be involved in cisplatin resistance in colon cancer. This study focused on its role in cisplatin resistance in bladder cancer. Our analysis of protein expression in bladder cancer cells stimulated by secretions from tumor‐associated macrophages (TAMs) showed a significant increase in GSTO1. This prompted further investigation into the role of GSTO1 in bladder cancer. We found a strong correlation between GSTO1 expression and cisplatin resistance. Mechanistically, GSTO1 triggered the release of large extracellular vesicles (EVs) that promoted cisplatin efflux, thereby reducing cisplatin–DNA adduct formation and enhancing cisplatin resistance. Inhibition of EV release effectively counteracted the cisplatin resistance associated with GSTO1. In conclusion, GSTO1‐mediated EV release may contribute to cisplatin resistance caused by TAMs in bladder cancer. Strategies to target GSTO1 could potentially improve the efficacy of cisplatin in treating bladder cancer.

show abstract

Proteomic analysis of extracellular vesicles derived from platelet concentrates treated with Mirasol® identifies biomarkers of platelet storage lesion

Cited by 28 publications

References 38 publications

Deciphering the secretome of leukocyte-platelet rich fibrin: towards a better understanding of its wound healing properties

Deciphering the secretome of leukocyte-platelet rich fibrin: towards a better understanding of its wound healing properties

Platelet-derived bio-products: Classification update, applications, concerns and new perspectives

Glutathione S‐transferase omega class 1 (GSTO1)‐associated large extracellular vesicles are involved in tumor‐associated macrophage‐mediated cisplatin resistance in bladder cancer

Contact Info

Product

Resources

About