Accumulation of the neutrophil-derived protein YKL-40 during storage of various blood components

Cintin, C.; Johansen, Julia S.; Skov, Flemming; Price, Paul A.; Nielsen, Hans Jørgen

doi:10.1007/s000110050732

Cited by 8 publications

(4 citation statements)

References 33 publications

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“…Similar results have been shown with histamine infusion and tumor growth [38]. Therefore, in addition to other tumor growth modulating bioactive substances present in blood components for transfusion, such as in particular PAI-1 [30,31], TIMP-1 [39,40], and YKL-40 [41,42], VEGF, and histamine may potentially participate in a concerted action, which may support the tumor growth stimulatory role of various blood transfusion components [43,44].…”

Section: Discussionsupporting

confidence: 73%

Extracellular accumulation of bioactive substances during preparation and storage of various platelet concentrates

et al. 2001

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Background: Side effects of platelet transfusion may be associated with infusion of bioactive substances. We therefore studied extracellular accumulation of histamine, plasminogen activator inhibitor (PAI)-1, vascular endothelial growth factor (VEGF), and interleukin (IL)-6 during preparation and storage of various platelet concentrates. Methods: Twenty buffy-coat-derived platelet pools (BCPC) were prepared and stored in platelet additive solutions (PAS). Twelve apheresis platelet (APC) units were prepared using the COBE Spectra LRS, and 14 were prepared using the Fenwal Amicus Separator. After preparation half of the content was drawn from each APC unit. The normal ranges of the substances were determined in plasma from all donors, and the extracellular concentrations of the substances were determined in supernatants collected on days 0, 1, 3, 5, and 7 of storage from all platelet preparations. Results: The platelet counts were not significantly different in BCPC units and APC units. The BCPC units had a significantly higher white cell count than the APC units (P < 0.0001), but the count was significantly higher in the Amicus APC units than in the COBE APC units (P < 0.0001). The extracellular histamine concentration was significantly (P < 0.001) increased in BCPC units after preparation and without further increase during storage, while there was no accumulation of histamine in APC units. After preparation the PAI-1 concentration was significantly (P < 0.02) higher in BCPC units than in APC units, but during storage PAI-1 increased significantly (P < 0.05) more in APC units than in BCPC units. Similarly, VEGF concentration was significantly (P < 0.05) higher in BCPC units than in APC units after preparation. During storage, however, VEGF increased more in BCPC units compared with COBE Spectra APC units (P < 0.05), but compared with Amicus Separator APC units only for the first 3 days of storage. At days 5 and 7 of storage the VEGF concentration was significantly higher in the Amicus APC units than in the COBE APC units (P < 0.05). IL-6 was not detectable in any of the concentrates after preparation or during storage. Conclusion: Platelet concentrates prepared by the apheresis method may contain less white cell derived bioactive substances than platelet concentrates prepared by the buffy-coat method. However, a substantial storage time dependent platelet derived bioactive substance accumulation takes place in all platelet concentrates tested, presumably due to platelet disintegration. Am. J. Hematol. 67:157-162, 2001.

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Section: Discussionsupporting

confidence: 73%

Extracellular accumulation of bioactive substances during preparation and storage of various platelet concentrates

et al. 2001

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“…In particular, in contrast with previous evidence from CSF [ 7 ], the plasmatic levels of CHI3L1 did not correlate with the score of the executive and visuo–spatial neuropsychological tests. The only correlation that was observed was with haemoglobin and RBC; this is consistent with previous evidence, since CHI3L1 seems to be more concentrated in RBCs [ 22 ].…”

Section: Discussionsupporting

confidence: 91%

Plasma CHI3L1 in Amyotrophic Lateral Sclerosis: A Potential Differential Diagnostic Biomarker

Bombaci

Manera

Marco

et al. 2023

JCM

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(1) Background: Motor neuron diseases (MNDs) are fatal neurodegenerative diseases. Biomarkers could help with defining patients’ prognoses and stratifications. Besides neurofilaments, chitinases are a promising family of possible biomarkers which correlate with neuroinflammatory status. We evaluated the plasmatic levels of CHI3L1 in MNDs, MND mimics, and healthy controls (HCs). (2) Methods: We used a sandwich ELISA to quantify the CHI3L1 in plasma samples from 44 MND patients, 7 hereditary spastic paraplegia (HSP) patients, 9 MND mimics, and 19 HCs. We also collected a ALSFRSr scale, MRC scale, spirometry, mutational status, progression rate (PR), blood sampling, and neuropsychological evaluation. (3) Results: The plasma levels of the CHI3L1 were different among groups (p = 0.005). Particularly, the MND mimics showed higher CHI3L1 levels compared with the MND patients and HCs. The CHI3L1 levels did not differ among PMA, PLS, and ALS, and we did not find a correlation among the CHI3L1 levels and clinical scores, spirometry parameters, PR, and neuropsychological features. Of note, the red blood cell count and haemoglobin was correlated with the CHI3L1 levels (respectively, p < 0.001, r = 0.63; p = 0.022, and r = 0.52). (4) Conclusions: The CHI3L1 plasma levels were increased in the MND mimics cohort compared with MNDs group. The increase of CHI3L1 in neuroinflammatory processes could explain our findings. We confirmed that the CHI3L1 plasma levels did not allow for differentiation between ALS and HCs, nor were they correlated with neuropsychological impairment.

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“…It is suggested that neutrophil-released YKL-40 acts as an autoantigen in rheumatoid arthritis (RA). Moreover, release of YKL-40 from specific neutrophil granules was suggested to lead to the post-transfusional complications and can be prevented by the pre-storage leukocyte depletion by filtration of whole blood (Cintin et al 2001). …”

Section: Intracellular Sorting and Modes Of Secretionmentioning

confidence: 99%

Human Chitinases and Chitinase-Like Proteins as Indicators for Inflammation and Cancer

2007

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Human Glyco_18 domain-containing proteins constitute a family of chitinases and chitinase-like proteins. Chitotriosidase and AMCase are true enzymes which hydrolyse chitin and have a C-terminal chitin-binding domain. YKL-40, YKL-39, SI-CLP and murine YM1/2 proteins possess solely Glyco_18 domain and do not have the hydrolytic activity. The major sources of Glyco_18 containing proteins are macrophages, neutrophils, epithelial cells, chondrocytes, synovial cells, and cancer cells. Both macrophages and neutrophils use the regulated secretory mechanism for the release of Glyco_18 containing proteins. Glyco_18 containing proteins are established biomarkers for human diseases. Chitotriosidase is overproduced by lipid-laden macrophages and is a major marker for the inherited lysosomal storage Gaucher disease. AMCase and murine lectin YM1 are upregulated in Th2-environment, and enzymatic activity of AMCase contributes to asthma pathogenesis. YKL proteins act as soluble mediators for the cell proliferation and migration, and are also involved in rheumatoid arthritis, inflammatory bowel disease, hepatic fibrosis and cirrhosis. Chitotriosidase and YKL-40 reflect the macrophage activation in atherosclerotic plaques. Serum level of YKL-40 is a diagnostic and prognostic marker for numerous types of solid tumors. YKL-39 is a marker for the activation of chondrocytes and the progression of the osteoarthritis in human. Recently identified SI-CLP is upregulated by Th2 cytokine IL-4 as well as by glucocorticoids. This unique feature of SI-CLP makes it an attractive candidate for the examination of individual sensitivity of patients to glucocorticoid treatment and prediction of side effects of glucocorticoid therapy. Human chitinases and chitinase-like proteins are found in tissues and circulation, and can be detected by non-invasive technologies.

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Accumulation of the neutrophil-derived protein YKL-40 during storage of various blood components

Abstract: YKL-40 appears to accumulate extracellularly in a time-dependent manner in standard erythrocyte components. Prestorage leukocyte depletion by filtration of whole blood may be an effective procedure to prevent extracellular YKL-40 accumulation during storage of erythrocyte components.

Cited by 8 publications

References 33 publications

Extracellular accumulation of bioactive substances during preparation and storage of various platelet concentrates

Extracellular accumulation of bioactive substances during preparation and storage of various platelet concentrates

Plasma CHI3L1 in Amyotrophic Lateral Sclerosis: A Potential Differential Diagnostic Biomarker

Human Chitinases and Chitinase-Like Proteins as Indicators for Inflammation and Cancer

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