Plasma constituent integrity in pre-storage vs. post-storage riboflavin and UV-light treatment – A comparative study (original) (raw)
Transfusion, 2013
BACKGROUND: According to AABB standards, freshfrozen plasma (FFP) should be thawed at 30 to 37°C and expire after 24 hours. An increase in the aggressive management of trauma patients with thawed plasma has heightened the risk of plasma waste. One way to reduce plasma waste is to extend its shelf life, given that the full range of therapeutic efficacy is maintained. We evaluated the effect of prolonged storage at 1 to 6°C on the activity of Factor (F)V, FVII, and FVIII in plasma thawed at 37 or 45°C. STUDY DESIGN AND METHODS: Group O plasma from healthy donors (n = 20) was divided into 10 pairs and frozen and stored at not more than -18°C. One sample from each pair was thawed at 37 or 45°C, and all were stored at 1 to 6°C. Samples were analyzed for FV, FVII, and FVIII activity on Days 0, 5, 10, 15, and 20. RESULTS: Plasma thawing time was 17% less at 45°C than at 37°C. No differences were observed between thawing groups in coagulation activity of FV, FVII, and FVIII during the 20-day storage period (p > 0.12). In both groups, the activity of FV and FVIII decreased over time but remained within a normal range at 10 days. CONCLUSION: Although levels of plasma clotting factors are reduced in storage, therapeutic levels of FV and FVIII are maintained in thawed plasma stored for up to 10 days at 1 to 6°C. Thawing of FFP at 45°C decreases thawing time but does not affect the activity of FV, FVII, and FVIII. * Data are presented as the mean percent activity Ϯ SD. Reference ranges: FV, 34-108; FVII, 28-104; and FVIII, 50-178.
Fresh Frozen Plasma (FFP) Clinical Insights and Management
Uva Clinical Research Lab 2025 © Uva Clinical Anaesthesia and Intensive Care ISSN 2827-7198, 2025
Fresh Frozen Plasma (FFP) is an essential blood product used in the management of bleeding and coagulopathy. Although it is widely utilized in emergency, surgical, and critical care settings, FFP administration is not without risks. This article provides a comprehensive review of the adverse effects and toxicities associated with FFP transfusion, including nonimmunologic reactions such as citrate toxicity and transfusion-associated circulatory overload (TACO), as well as immunologic complications like transfusion-related acute lung injury (TRALI). The immunologic distinctions between immediate and delayed transfusion reactions are explored, with an emphasis on pathophysiology, clinical presentation, and therapeutic management. Special attention is given to citrate toxicity, a metabolic complication caused by calcium chelation, and the diagnostic differentiation between TACO and TRALI, both of which can present with acute pulmonary symptoms. Moreover, the article addresses contraindications, drug interactions, and the importance of cautious FFP use in specific clinical scenarios, such as anticoagulant reversal and volume expansion. It emphasizes the necessity of interdisciplinary coordination among physicians, nurses, pharmacists, and hematologists to ensure appropriate FFP administration, monitoring, and management of complications. The review concludes with a call for greater awareness among healthcare professionals regarding the potential risks of FFP, underscoring the need for stringent transfusion protocols, timely recognition of adverse events, and evidence-based clinical decision-making.
The effects of frozen tissue storage conditions on the integrity of RNA and protein.
2014
Unfixed tissue specimens most frequently are stored for long term research uses at either −80° C or in vapor phase liquid nitrogen (VPLN). There is little information concerning the effects such long term storage on tissue RNA or protein available for extraction. Aliquots of 49 specimens were stored for 5–12 years at −80° C or in VPLN. Twelve additional paired specimens were stored for 1 year under identical conditions. RNA was isolated from all tissues and assessed for RNA yield, total RNA integrity and mRNA integrity. Protein stability was analyzed by surface-enhanced or matrix-assisted laser desorprion ionization time of flight mass spectrometry (SELDI-TOF-MS, MALDI-TOF-MS) and nano-liquid chromatography electrospray ionization tandem mass spectrometry (nLC-ESI-MS/MS). RNA yield and total RNA integrity showed significantly better results for −80° C storage compared to VPLN storage; the transcripts that were preferentially degraded during VPLN storage were these involved in antigen presentation and processing. No consistent differences were found in the SELDI-TOF-MS, MALDI-TOF-MS or nLC-ESI-MS/MS analyses of specimens stored for more than 8 years at −80° C compared to those stored in VPLN. Long term storage of human research tissues at −80° C provides at least the same quality of RNA and protein as storage in VPLN.
Original Research Article Appropriate and Inappropriate Use of Fresh Frozen Plasma (FFP) and
2015
Aims: The aim of this study was to evaluate the usage of fresh frozen plasma (FFP) and packed cell volume (PCV) according to indications and to reduce inappropriate usage. Method: A two years retrospective study was conducted in Dr. S.C.G.M.C. and hospital blood bank. Based on the guidelines published by college of American pathologist, national health and medical research council and Australian society for blood transfusion FFP and PCV usage were categorized into appropriate and inappropriate. Pre and post transfusion INR/PT were recorded and the effect of FFP were studied in patients who received FFP Results: During two years study 1079 unit of FFP were used for 267 patients. Out of 267 patients only 125(46.81%) request were appropriate and 142(53.19%) were inappropriate requests. Pregnant female with active labour suffering from severe anaemia with shock was the commonest reason for inappropriate FFP use. Out of 125 appropriate request 100 patients were compared by evaluating Pre...
Appropriate and Inappropriate Use of Fresh Frozen Plasma (FFP) and Packed Cell Volume (PCV)
International Journal of Health Sciences and Research, 2014
The aim of this study was to evaluate the usage of fresh frozen plasma (FFP) and packed cell volume (PCV) according to indications and to reduce inappropriate usage. Method: A two years retrospective study was conducted in Dr. S.C.G.M.C. and hospital blood bank. Based on the guidelines published by college of American pathologist, national health and medical research council and Australian society for blood transfusion FFP and PCV usage were categorized into appropriate and inappropriate. Pre and post transfusion INR/PT were recorded and the effect of FFP were studied in patients who received FFP Results: During two years study 1079 unit of FFP were used for 267 patients. Out of 267 patients only 125(46.81%) request were appropriate and 142(53.19%) were inappropriate requests. Pregnant female with active labour suffering from severe anaemia with shock was the commonest reason for inappropriate FFP use. Out of 125 appropriate request 100 patients were compared by evaluating Pre and post transfusion PT/INR by using fully automated coagulometer. Total 993 PCV units were transfused in 445 patients out of which 358 were appropriate and 87 were inappropriate as per the guidelines. Highest appropriate request were from pediatric department followed by gynaecology department. Conclusion: Inappropriate use of FFP and PCV not only increase the treatment costs, but also causes loss of productive power and exposes the patient to the unnecessary side effects of transfusion. Inappropriate FFP and PCV transfusion should be prevented by means of education and awareness programme by establishing the hospital transfusion guidelines
Clinical application for the preservation of phospho-proteins through in-situ tissue stabilization
Proteome Science, 2010
Background Protein biomarkers will play a pivotal role in the future of personalized medicine for both diagnosis and treatment decision-making. While the results of several pre-clinical and small-scale clinical studies have demonstrated the value of protein biomarkers, there have been significant challenges to translating these findings into routine clinical care. Challenges to the use of protein biomarkers include inter-sample variability introduced by differences in post-collection handling and ex vivo degradation of proteins and protein modifications. Results In this report, we re-create laboratory and clinical scenarios for sample collection and test the utility of a new tissue stabilization technique in preserving proteins and protein modifications. In the laboratory setting, tissue stabilization with the Denator Stabilizor T1 resulted in a significantly higher yield of phospho-protein when compared to standard snap freeze preservation. Furthermore, in a clinical scenario, tissue stabilization at collection resulted in a higher yield of total phospho-protein, total phospho-tyrosine, pErkT202/Y204 and pAktS473 when compared to standard methods. Tissue stabilization did not have a significant effect on other post-translational modifications such as acetylation and glycosylation, which are more stable ex-vivo. Tissue stabilization did decrease total RNA quantity and quality. Conclusion Stabilization at the time of collection offers the potential to better preserve tissue protein and protein modification levels, as well as reduce the variability related to tissue processing delays that are often associated with clinical samples.
Freeze-dried plasma proteins are stable at room temperature for at least 1 year
Clinical proteomics, 2017
Thirty human EDTA plasma samples from male and female subjects ranging in age from 24 to 74 years were collected on ice, processed ice cold and stored frozen at -80 °C, in liquid nitrogen (LN2), or freeze dried and stored at room temperature in a desiccator (FDRT) or freeze dried and stored at -20 °C for 1 year (FD-20). In a separate experiment, EDTA plasma samples were collected onto ice, processed ice cold and maintained on ice ± protease inhibitors versus incubated at room temperature for up to 96 h. Random and independent sampling by liquid chromatography and tandem mass spectrometry (LC-ESI-MS/MS), as correlated by the MASCOT, OMSSA, X!TANDEM and SEQUEST algorithms, showed that tryptic peptides from complement component 4B (C4B) were rapidly released in plasma at room temperature. Random sampling by LC-ESI-MS/MS showed that peptides from C4B were undetectable on ice, but peptides were cleaved from the mature C4B protein including NGFKSHALQLNNR within as little as 1 h at room te...
Plasma cryoprecipitation studies: Major increase in fibrinogen yield by albumin enrichment of plasma
Thrombosis Research, 1995
The present studies compared fibrinogen yields of cryoprecipitate (Cr) obtained under differing conditions, and focused on yields from albumin enriched plasma. Addition of human albumin to fresh plasma collected into CPDA-1, citrate,or heparin (4 U/ml) resulted in an average of 2.8 fold (& 0.34 SD, n= 17) increase in yields of Cr fibrinogen. This albumin effect was shown with undefatted and defatted albumin, fibrinogen yields increasing in the range of 2-6 g of albumin added/d1 of plasma and plateauing thereafter. Similarly increased were yields of fibronectin, plasminogen and factor XIII, but not of factor VIII or of von Willebrand factor. By electrophoretic analyses, Cr fibrinogen from albumin enriched and that from untreated plasma did not differ. Fibrin related measurements disclosed that the albumin enhancement of fibrinogen yield did not result from increased fibrin formation in Cr. This enhancement was shown in plasma that had been enriched with soluble fibrin to increase its yield and in that which had been subjected to hirudin, to high ionic strength, or to dilution to decrease its Cr fibrinogen yield. The results suggest a water exclusion effect, inducing cryoprecipitation of otherwise soluble fibrin/fibrinogen complexes. Plasma forms an insoluble precipitate when after freezing it is thawed at melting ice or refrigeration temperatures (1). The mechanism of this precipitation is partly understood. Also known as cryoprecipitation, it was ascribed to a salting out process (2), in that proteins enriching plasma cryoprecipitate were also precipitated early as the concentrations of NaCl in plasma were increased. According to this explanation, as solutes become progressively concentrated during loss of water from liquid phase, different proteins precipitate out according to their solubility limits. Other investigations (3-5) underscored the importance of soluble fibrin/fibrinogen complexes and of fibronectin, known to cryoprecipitate whether in