YKL-40 and LAMPs as possible markers in neuroinflammation and autophagy during central nervous system infections

References

• Giovane RA, Lavender PD. Central nervous system infections. Prim Care Clin off Pract. 2018;45(3):1–9.
   PubMed Web of Science ®Google Scholar
• Archibald LK, Quisling RG, Archibald LK, et al. Central nervous system infections. Textb Neurointensive Care. 2013;427–517. https://link.springer.com/chapter/10.1007/978-1-4471-5226-2_22
   Google Scholar
• Enfermedades Infecciosas y Microbiología Clínica. 2012; [cited 2024 Mar 10]; Available from: www.elsevier.es/eimc.
   Google Scholar
• Parikh V, Tucci V, Galwankar S. Infections of the nervous system. Int J Crit Illn Inj Sci. 2012;2(2):82–97. https://pubmed.ncbi.nlm.nih.gov/22837896/
   PubMedGoogle Scholar
• Vila J, Bosch J, Muñoz-Almagro C. Molecular diagnosis of the Central nervous system (CNS) infections. Enferm Infecc Microbiol Clin. 2020;3:1. doi: 10.1016/j.eimc.2020.03.001.
   Google Scholar
• Ramanan P, Bryson AL, Binnicker MJ, et al. Syndromic panel-based testing in clinical microbiology. Clin Microbiol Rev. 2017;31(1):77. https://pubmed.ncbi.nlm.nih.gov/29142077/
   Web of Science ®Google Scholar
• Vora NM, Holman RC, Mehal JM, et al. Burden of encephalitis-associated hospitalizations in the United States, 1998–2010. Neurology. 2014;82(5):443–451. https://pubmed.ncbi.nlm.nih.gov/24384647/ doi: 10.1212/WNL.0000000000000086.
   PubMed Web of Science ®Google Scholar
• Sulaiman T, Salazar L, Hasbun R. Acute versus subacute community-acquired meningitis: analysis of 611 patients. Medicine. 2017;96(36):54. https://pubmed.ncbi.nlm.nih.gov/28885354/
   Web of Science ®Google Scholar
• Lautner R, Mattsson N, Schöll M, et al. Biomarkers for microglial activation in Alzheimer’s disease. Int J Alzheimers Dis. 2011;2011:939426. https://pubmed.ncbi.nlm.nih.gov/22114747/ doi: 10.4061/2011/939426.
   PubMedGoogle Scholar
• Shao R. YKL-40 acts as an angiogenic factor to promote tumor angiogenesis. Front Physiol. 2013;4:122. doi: 10.3389/fphys.2013.00122.
   PubMed Web of Science ®Google Scholar
• Schultz NA, Johansen JS. YKL-40 – a protein in the field of translational medicine: a role as a biomarker in cancer patients? Cancers. 2010;2(3):1453–1491. https://www.mdpi.com/2072-6694/2/3/1453/htm doi: 10.3390/cancers2031453.
   PubMedGoogle Scholar
• He CH, Lee CG, Dela Cruz CS, et al. Chitinase 3-like 1 regulates cellular and tissue responses via IL-13 receptor α2. Cell Rep. 2013;4(4):830–841. https://pubmed.ncbi.nlm.nih.gov/23972995/.
   PubMed Web of Science ®Google Scholar
• Väänänen T, Koskinen A, Paukkeri E-L, et al. YKL-40 as a novel factor associated with inflammation and catabolic mechanisms in osteoarthritic joints. Mediators Inflamm. 2014;2014:215140. https://pubmed.ncbi.nlm.nih.gov/25132728/ doi: 10.1155/2014/215140.
   PubMed Web of Science ®Google Scholar
• Johansen JS, Jensen BV, Roslind A, et al. Serum YKL-40, a new prognostic biomarker in cancer patients? Cancer Epidemiol Biomarkers Prev. 2006;15(2):194–202. https://pubmed.ncbi.nlm.nih.gov/16492905/ doi: 10.1158/1055-9965.EPI-05-0011.
   PubMed Web of Science ®Google Scholar
• Wennström M, Surova Y, Hall S, et al. The inflammatory marker YKL-40 is elevated in cerebrospinal fluid from patients with Alzheimer’s but not Parkinson’s disease or dementia with Lewy bodies. PLoS One. 2015;10(8):e0135458. doi: 10.1371/journal.pone.0135458.
   PubMed Web of Science ®Google Scholar
• Kazakova MH, Batalov AZ, Mateva NG, et al. YKL-40 and cytokines – a new diagnostic constellation in rheumatoid arthritis? Folia Med. 2017;59(1):37–42. https://pubmed.ncbi.nlm.nih.gov/28384116/ doi: 10.1515/folmed-2017-0013.
   Google Scholar
• Karalilova R, Kazakova M, Sapundzhieva T, et al. Serum YKL-40 and IL-6 levels correlate with ultrasound findings of articular and periarticular involvement in patients with systemic sclerosis. Rheumatol Int. 2019;39(11):1841–1848. https://pubmed.ncbi.nlm.nih.gov/31375891/ doi: 10.1007/s00296-019-04402-9.
   PubMed Web of Science ®Google Scholar
• Kazakova MH, Pavlov GA, Dichev VD, et al. Relationship between YKL-40, neuron-specific enolase, tumor necrosis factor-a, interleukin-6, and clinical assessment scores in traumatic brain injury. Arch Trauma Res. 2021;10(1):23. https://www.archtrauma.com/article.asp?issn=2251-953X;year=2021;volume=10;issue=1;spage=23;epage=29;aulast=Kazakova doi: 10.4103/atr.atr_43_20.
   Web of Science ®Google Scholar
• Østergaard C, Johansen JS, Benfield T, et al. YKL-40 is elevated in cerebrospinal fluid from patients with purulent meningitis. Clin Diagn Lab Immunol. 2002;9(3):598–604. https://pubmed.ncbi.nlm.nih.gov/11986266/ doi: 10.1128/cdli.9.3.598-604.2002.
   PubMedGoogle Scholar
• Craig-Schapiro R, Perrin RJ, Roe CM, et al. YKL-40: a novel prognostic fluid biomarker for preclinical alzheimer’s disease. Biol Psychiatry. 2010;68(10):903–912. https://pubmed.ncbi.nlm.nih.gov/21035623/
   PubMed Web of Science ®Google Scholar
• Chen J, Ding Y, Zheng D, et al. Elevation of YKL-40 in the CSF of anti-NMDAR encephalitis patients is associated with poor prognosis. Front Neurol. 2018;9(OCT):727. www.frontiersin.org doi: 10.3389/fneur.2018.00727.
   PubMedGoogle Scholar
• Li J, Li H, Wang Y, et al. CHI3L1 in the CSF is a potential biomarker for anti-leucine-rich glioma inactivated 1 encephalitis. Front Immunol. 2022;13:1071219. doi: 10.3389/fimmu.2022.1071219.
   PubMed Web of Science ®Google Scholar
• Czupryna P, Kulczyńka-Przybik A, Mroczko B, et al. Assessment of the YKL-40 concentration in patients with tick-borne encephalitis. Ticks Tick Borne Dis. 2022;13(2):101895.
   PubMed Web of Science ®Google Scholar
• Kronborg G, Ostergaard C, Weis N, et al. Serum level of YKL-40 is elevated in patients with Streptococcus pneumoniae bacteremia and is associated with the outcome of the disease. Scand J Infect Dis. 2002;34(5):323–326. https://pubmed.ncbi.nlm.nih.gov/12069012/
   PubMed Web of Science ®Google Scholar
• Orvedahl A, Levine B. Autophagy and viral neurovirulence. Cell Microbiol. 2008;10(9):1747–1756.
   PubMed Web of Science ®Google Scholar
• Moy RH, Gold B, Molleston JM, et al. Antiviral autophagy restrictsRift valley fever virus infection and is conserved from flies to mammals. Immunity. 2014;40(1):51–65. https://pubmed.ncbi.nlm.nih.gov/24374193/ doi: 10.1016/j.immuni.2013.10.020.
   PubMed Web of Science ®Google Scholar
• C Bílý T, Palus M, Eyer L, et al. Electron tomography analysis of tick-borne encephalitis virus infection in human neurons. Sci Rep. 2015;5(1):10745. doi: 10.1038/srep10745.
   PubMedGoogle Scholar
• Cheng XT, Xie YX, Zhou B, et al. Revisiting LAMP1 as a marker for degradative autophagy-lysosomal organelles in the nervous system. Autophagy. 2018;14(8):1472–1474. https://www.tandfonline.com/doi/abs/ doi: 10.1080/15548627.2018.1482147.
   PubMed Web of Science ®Google Scholar
• Geng B, Pan J, Zhao T, et al. Chitinase 3-like 1-CD44 interaction promotes metastasis and epithelial-to-mesenchymal transition through β-catenin/erk/akt signaling in gastric cancer. J Exp Clin Cancer Res. 2018;37(1):208. https://pubmed.ncbi.nlm.nih.gov/30165890/ doi: 10.1186/s13046-018-0876-2.
   PubMedGoogle Scholar
• Rehli M, Niller HH, Ammon C, et al. Transcriptional regulation of CHI3L1, a marker gene for late stages of macrophage differentiation. J Biol Chem. 2003;278(45):44058–44067. https://pubmed.ncbi.nlm.nih.gov/12933821/
   PubMed Web of Science ®Google Scholar
• Connor JR, Dodds RA, Emery JG, et al. Human cartilage glycoprotein 39 (HC gp-39) mRNA expression in adult and fetal chondrocytes, osteoblasts and osteocytes by in-situ hybridization. Osteoarthr Cartil. 2000;8(2):87–95. https://pubmed.ncbi.nlm.nih.gov/10772238/
   PubMed Web of Science ®Google Scholar
• Ringsholt M, Høgdall EVS, Johansen JS, et al. YKL-40 protein expression in normal adult human tissues–an immunohistochemical study. J Mol Histol. 2007;38(1):33–43. https://pubmed.ncbi.nlm.nih.gov/17242979/ doi: 10.1007/s10735-006-9075-0.
   PubMed Web of Science ®Google Scholar
• Zhao T, Su Z, Li Y, et al. Chitinase-3 like-protein-1 function and its role in diseases. Signal Transduct Target Ther. 2020;51(1):1–20. https://www.nature.com/articles/s41392-020-00303-7
   Google Scholar
• Kawada M, Seno H, Kanda K, et al. Chitinase 3-like 1 promotes macrophage recruitment and angiogenesis in colorectal cancer. Oncogene. 2012;31(26):3111–3123. https://pubmed.ncbi.nlm.nih.gov/22056877/ doi: 10.1038/onc.2011.498.
   PubMed Web of Science ®Google Scholar
• Peters PJ, Borst J, Oorschot V, et al. Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes. J Exp Med. 1991;173(5):1099–1109. https://pubmed.ncbi.nlm.nih.gov/2022921/ doi: 10.1084/jem.173.5.1099.
   PubMed Web of Science ®Google Scholar
• Krzewski K, Gil-Krzewska A, Nguyen V, et al. LAMP1/CD107a is required for efficient perforin delivery to lytic granules and NK-cell cytotoxicity. Blood. 2013;121(23):4672–4683. https://pubmed.ncbi.nlm.nih.gov/23632890/ doi: 10.1182/blood-2012-08-453738.
   PubMed Web of Science ®Google Scholar
• Cohnen A, Chiang SC, Stojanovic A, et al. Surface CD107a/LAMP-1 protects natural killer cells from degranulation-associated damage. Blood. 2013;122(8):1411–1418. https://pubmed.ncbi.nlm.nih.gov/23847195/ doi: 10.1182/blood-2012-07-441832.
   PubMed Web of Science ®Google Scholar
• Künzli BM, Berberat PO, Zhu ZW, et al. Influences of the lysosomal associated membrane proteins (lamp-1, lamp-2) and mac-2 binding protein (mac-2-BP) on the prognosis of pancreatic carcinoma. Cancer. 2002;94(1):228–239. https://pubmed.ncbi.nlm.nih.gov/11815981/ doi: 10.1002/cncr.10162.
   PubMed Web of Science ®Google Scholar
• Lee S, Sato Y, Nixon RA. Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer’s-like axonal dystrophy. J Neurosci. 2011;31(21):7817–7830. https://pubmed.ncbi.nlm.nih.gov/21613495/
   PubMed Web of Science ®Google Scholar
• Rubinsztein DC, Mariño G, Kroemer G. Autophagy and aging. Cell. 2011;146(5):682–695. https://pubmed.ncbi.nlm.nih.gov/21884931/ doi: 10.1016/j.cell.2011.07.030.
   PubMed Web of Science ®Google Scholar
• Bar-Yosef T, Damri O, Agam G. Dual role of autophagy in diseases of the Central nervous system. Front Cell Neurosci. 2019;13:196. doi: 10.3389/fncel.2019.00196.
   PubMed Web of Science ®Google Scholar
• Sarafian V, Jadot M, Foidart J-M, et al. EXPRESSION oF lamp-1 and lamp-2 and their interactions with galectin-3 in human tumor cells. J Cancer. 1998;75:105–111. https://onlinelibrary.wiley.com/terms-and-conditions
   Web of Science ®Google Scholar
• Kristen H, Sastre I, Aljama S, et al. LAMP2 deficiency attenuates the neurodegeneration markers induced by HSV-1 infection. Neurochem Int. 2021;146:105032. doi: 10.1016/j.neuint.2021.105032.
   PubMed Web of Science ®Google Scholar
• Pang Y, Wu L, Tang C, et al. Autophagy-Inflammation interplay during infection: balancing pathogen clearance and host inflammation. Front Pharmacol. 2022;13:832750. www.frontiersin.org doi: 10.3389/fphar.2022.832750.
   PubMed Web of Science ®Google Scholar
• Jin M, Liu X, Klionsky DJ. SnapShot: selective autophagy. Cell. 2013;152(1-2):368–368.e2. Available fromhttps://pubmed.ncbi.nlm.nih.gov/23332767/
   PubMed Web of Science ®Google Scholar
• Biasizzo M, Kopitar-Jerala N. Interplay between NLRP3 inflammasome and autophagy. Front Immunol. 2020;11:591803. https://pubmed.ncbi.nlm.nih.gov/33163006/
   PubMed Web of Science ®Google Scholar
• Clemens DL, Horwitz MA. Characterization of the Mycobacterium mberctdosis phagosome and evidence that phagosomal maturation is inhibited. Available from: http://rupress.org/jem/article-pdf/181/1/257/1676619/257.pdf.
   Google Scholar
• Gordon SB, Irving GRB, Lawson RA, et al. Intracellular trafficking and killing of Streptococcus pneumoniae by human alveolar macrophages are influenced by opsonins. Infect Immun. 2000;68(4):2286–2293. doi: 10.1128/IAI.68.4.2286-2293.2000.
   PubMed Web of Science ®Google Scholar
• Read RC, Zimmerli S, Broaddus C, et al. The (alpha2–>8)-linked polysialic acid capsule of group B Neisseria meningitidis modifies multiple steps during interaction with human macrophages. Infect Immun. 1996;64(8):3210–3217. https://pubmed.ncbi.nlm.nih.gov/8757855/ doi: 10.1128/iai.64.8.3210-3217.1996.
   PubMed Web of Science ®Google Scholar
• Jonsson S, Musher DM, Chapman A, et al. Phagocytosis and killing of common bacterial pathogens of the lung by human alveolar macrophages. J Infect Dis. 1985;152(1):4–13. https://pubmed.ncbi.nlm.nih.gov/3874252/ doi: 10.1093/infdis/152.1.4.
   PubMed Web of Science ®Google Scholar
• Liou B, Haffey WD, Greis KD, et al. The LIMP-2/SCARB2 binding motif on acid β-Glucosidase. J Biol Chem. 2014;289(43):30063–30074. http://www.jbc.org/article/S0021925820373385/fulltext doi: 10.1074/jbc.M114.593616.
   PubMed Web of Science ®Google Scholar
• Guo H, Zhang J, Zhang X, et al. SCARB2/LIMP-2 regulates IFN production of plasmacytoid dendritic cells by mediating endosomal translocation of TLR9 and nuclear translocation of IRF7. J Immunol. 2015;194(10):4737–4749. https://pubmed.ncbi.nlm.nih.gov/25862818/ doi: 10.4049/jimmunol.1402312.
   PubMed Web of Science ®Google Scholar
• Yamayoshi S, Yamashita Y, Li J, et al. Scavenger receptor B2 is a cellular receptor for enterovirus 71. Nat Med. 2009;15(7):798–801. https://pubmed.ncbi.nlm.nih.gov/19543282/ doi: 10.1038/nm.1992.
   PubMed Web of Science ®Google Scholar
• Pizarro-Cerdá J, Jonquières R, Gouin E, et al. Distinct protein patterns associated with Listeria monocytogenes InlA- or InlB-phagosomes. Cell Microbiol. 2002;4(2):101–115. https://onlinelibrary.wiley.com/doi/full/ doi: 10.1046/j.1462-5822.2002.00169.x.
   PubMed Web of Science ®Google Scholar
• Birmingham CL, Canadien V, Kaniuk NA, et al. Listeriolysin O allows Listeria monocytogenes replication in macrophage vacuoles. Nature. 2008;451(7176):350–354. https://pubmed.ncbi.nlm.nih.gov/18202661/ doi: 10.1038/nature06479.
   PubMed Web of Science ®Google Scholar
• Bleves S, Alonzo F, Bierne H, et al. To be cytosolic or vacuolar: the double life of Listeria monocytogenes background: the prototype of a cytosolic and disseminating bacterium. Front Cell Infect Microbiol. 2018;1:136. www.frontiersin.org
   Google Scholar
• Villar-Piqué A, Schmitz M, Hermann P, et al. Plasma YKL-40 in the spectrum of neurodegenerative dementia. J Neuroinflammation. 2019;16(1):145. https://jneuroinflammation.biomedcentral.com/articles/ doi: 10.1186/s12974-019-1531-3.
   PubMedGoogle Scholar
• Pinteac R, Montalban X, Comabella M. Chitinases and chitinase-like proteins as biomarkers in neurologic disorders. Neurol Neuroimmunol Neuroinflamm. 2020;8(1):e921. doi: 10.1212/NXI.0000000000000921.
   PubMed Web of Science ®Google Scholar
• Hermansson L, Yilmaz A, Axelsson M, et al. Cerebrospinal fluid levels of glial marker YKL-40 strongly associated with axonal injury in HIV infection. J Neuroinflammation. 2019;16(1):16. https://pubmed.ncbi.nlm.nih.gov/30678707/ doi: 10.1186/s12974-019-1404-9.
   PubMedGoogle Scholar
• Laforge M, Limou S, Harper F, et al. DRAM triggers lysosomal membrane permeabilization and cell death in CD4+ T cells infected with HIV. PLoS Pathog. 2013;9(5):e1003328. https://pubmed.ncbi.nlm.nih.gov/23658518/ doi: 10.1371/journal.ppat.1003328.
   PubMed Web of Science ®Google Scholar
• Levine B, Mizushima N, Virgin HW. Autophagy in immunity and inflammation. Nat. 2011;469(7330):323–335. https://www.nature.com/articles/nature09782 doi: 10.1038/nature09782.
   Google Scholar