References
- Kittelmann M. 3D electron microscopy of the ER. Methods Mol Biol. 2018;1691:15–21. doi:10.1007/978-1-4939-7389-7–2.
- Chen S, Novick P, Ferro-Novick S. ER structure and function. Curr Opin Cell Biol. 2013;25(4):428–433. doi:10.1016/j.ceb.2013.02.006.
- Zhang Z, Zhou H, Ouyang X, Dong Y, Sarapultsev A, Luo S, et al. Multifaceted functions of sting in human health and disease: from molecular mechanism to targeted strategy. Signal Transduct Target Ther. 2022;7(1):394. doi:10.1038/s41392-022-01252-z.
- Merighi A, Lossi L. Endoplasmic reticulum stress signaling and neuronal cell death. Int J Mol Sci. 2022;23(23):15186. doi:10.3390/ijms232315186.
- Parlakgül G, Arruda AP, Pang S, Cagampan E, Min N, Güney E, et al. Regulation of liver subcellular architecture controls metabolic homeostasis. Nature. 2022;603(7902):736–742. doi:10.1038/s41586-022-04488-5.
- Auer J. Some hitherto undescribed structures found in the large lymphocytes of a case of acute leukaemia. Am J Med Sci. 1906;131(6):1002–1015. doi:10.1097/00000441-190606000-00008.
- Castoldi GL, Liso V, Specchia G, Tomasi P. Acute promyelocytic leukemia: morphological aspects. Leukemia. 1994;8:1441–1446.
- Yue QF, Xiong B, Chen WX, Liu XY. Comparative study of the efficacy of wright-giemsa stain and Liu’s stain in the detection of Auer rods in acute promyelocytic leukemia. Acta Histochem. 2014;116(6):1113–1116. doi:10.1016/j.acthis.2014.05.005.
- Yanagihara ET, Naeim F, Gale RP, Austin G, Waisman J. Acute lymphoblastic leukemia with giant intracytoplasmic inclusions. Am J Clin Pathol. 1980;74(3):345–349. doi:10.1093/ajcp/74.3.345.
- Ru YX, Dong SX, Liu J, Eyden B. Development of Auer bodies from giant inclusions associated with rough endoplasmic reticulum in acute promyelocytic leukemia. Blood Sci. 2022;5(2):111–117. doi:10.1097/BS9.0000000000000145.
- Schwarz DS, Blower MD. The endoplasmic reticulum: structure, function and response to cellular signaling. Cell Mol Life Sci. 2016;73(1):79–94. doi:10.1007/s00018-015-2052-6.
- Arber DA, Orazi A, Hasserjian R, et al. The 2016 revision to the World Health Organization classification of myeloid neoplasms and acute leukemia. Blood. 2016;127(20):2391–2405. doi:10.1182/blood-2016-03-643544.
- Roels F, Wisse E, Brest BDE, Meulen J. Cytochemical discrimination between catalases and peroxidases using diaminobenzidine. Histochemistry. 1975;41(4):281–312. doi:10.1007/BF00490073.
- Westrate LM, Lee JE, Prinz WA, Voeltz GK. Form follows function: the importance of endoplasmic reticulum shape. Annu Rev Biochem. 2015;84(1):791–811. doi:10.1146/annurev-biochem-072711-163501.
- Obara CJ, Moore AS, Lippincott-Schwartz J. Structural diversity within the endoplasmic reticulum from the microscale to the nanoscale. Cold Spring Harb Perspect Biol. 2023;15(6):a041259. doi:10.1101/cshperspect.a041259.
- Reid DW, Nicchitta CV. Diversity and selectivity in mRNA translation on the endoplasmic reticulum. Nat Rev Mol Cell Biol. 2015;16(4):221–231. doi:10.1038/nrm3958.
- Perkins HT, Allan V. Intertwined and finely balanced: Endoplasmic reticulum morphology, dynamics, function, and diseases. Cells. 2021;10(9):2341. doi:10.3390/cells10092341.
- Ackerman GA. Microscopic and histochemical studies on the Auer bodies in leukemic cells. Blood. 1950;5(9):847–863. doi:10.1182/blood.V5.9.847.847.
- Newburger PE, Novak TJ, McCaffrey RP. Eosinophilic cytoplasmic inclusions in fetal leukocytes: are Auer bodies a recapitulation of fetal morphology? Blood. 1983;61(3):593–595. doi:10.1182/blood.V61.3.593.593.
- Lejeune F, Turpin F, Lortholary P. Unusual giant inclusions in blast cells during acute transformation of chronic myeloid leukemia cytochemical and ultrastructural study. Pathol Biol (Paris). 1978;26:7–11.
- Schmalzl F, Huhn D, Asamer H, Rindler R, Braunsteiner H. Cytochemistry and ultrastructure of pathologic granulation in myelogenous leukemia. Blut. 1973;27(4):243–260. doi:10.1007/BF01637437.
- White JG, Clawson CC. The Chédiak-Higashi syndrome: ring-shaped lysosomes in circulating monocytes. Am J Pathol. 1979;96:781–798.
- Parkin JL, Brunning RD. Unusual configurations of endoplasmic reticulum in cells of acute promyelocytic leukemia. J Natl Cancer Inst. 1978;61:341–348.
- Kounatidis I, Stanifer ML, Phillips MA, Paul-Gilloteaux P, Heiligenstein X, Wang H, et al. 3D correlative cryo-structured illumination fluorescence and soft x-ray microscopy elucidates reovirus intracellular release pathway. Cell. 2020;182(2):515–530.e17. doi:10.1016/j.cell.2020.05.051.
- Weigel AV, Chang CL, Shtengel G, Xu CS, Hoffman DP, Freeman M, Iyer, N, et al. ER-to-Golgi protein delivery through an interwoven, tubular network extending from ER. Cell. 2021;184(9):2412–2429.e16. doi:10.1016/j.cell.2021.03.035.
- English AR, Voeltz GK. Endoplasmic reticulum structure and interconnections with other organelles. Cold Spring Harb Perspect Biol. 2013;5(4):a013227. doi:10.1101/cshperspect.a013227.
- Nauseef WM. Biosynthesis of human myeloperoxidase. Arch Biochem Biophys. 2018;642:1–9. doi:10.1016/j.abb.2018.02.001.
- Nauseef WM. Posttranslational processing of a human myeloid lysosomal protein, myeloperoxidase. Blood. 1987;70(4):1143–1150. PMID: 2820530. doi:10.1182/blood.V70.4.1143.1143.
- Kenny EF, Herzig A, Krüger R, Muth A, Mondal S, et al. Diverse stimuli engage different neutrophil extracellular trap pathways. eLife. 2017;6:e24437. doi:10.7554/eLife.24437.
- Metzler KD, Goosmann C, Lubojemska A, Zychlinsky A, Papayannopoulos V. A myeloperoxidase-containing complex regulates neutrophil elastase release and actin dynamics during NETosis. Cell Rep. 2014;8(3):883–896. doi:10.1016/j.celrep.2014.06.044.
- Nauseef WM. Myeloperoxidase deficiency. Hematol Oncol Clin North Am. 1988;2(1):135–158. doi:10.1016/S0889-8588(18)30634-8.
- Nauseef WM, McCormick S, Yi H. Roles of heme insertion and the mannose-6-phosphate receptor in processing of the human myeloid lysosomal enzyme, myeloperoxidase. Blood. 1992;80(10):2622–2633. doi:10.1182/blood.V80.10.2622.2622.
- Lin W, Chen H, Chen X, Guo C. The roles of neutrophil-derived myeloperoxidase (mpo) in diseases: The new progress. Antioxidants (Basel). 2024;13(1):132. doi:10.3390/antiox13010132.
- Rastogi P, Sharma S, Sreedharanunni S, Sharma P, Sachdeva MUS, Jain R, et al. Myeloperoxidase deficient acute promyelocytic leukemia: Report of two cases. Indian J Hematol Blood Transfus. 2018;34(2):372–374. doi:10.1007/s12288-017-0844-6.
- Gorius JB, Houssay D. Auer bodies in acute promyelocytic leukemia. Demonstration of their fine structure and peroxidase localization. Lab Invest. 1973;28:135–141.
- Payne CM, Harrow EJ. A cytochemical and ultrastructural study of acute myelomonocytic leukemia exhibiting the pseudo-Chediak-Higashi anomaly of leukemia and “splinter-type” Auer rods. Am J Clin Pathol. 1983;80(2):216–223. doi:10.1093/ajcp/80.2.216.
- Shaft D, Shtalrid M, Berebi A, Catovsky D, Resnitzky P. Ultrastructural characteristics and lysozyme content in hypergranular and variant type of acute promyelocytic leukaemia. Br J Haematol. 1998;103(3):729–739. doi:10.1046/j.1365-2141.1998.01065.x.
- Zassadowski F, Ades L, Schlageter MH, Chevret S, Guillemot I, Fenaux P, et al. Auer rods and differentiation in acute promyelocytic leukemia. Br J Haematol. 2008;142(6):998–1000. doi:10.1111/j.1365-2141.2008.07282.x.
- Sonda S, Pendin D, Daga A. ER morphology in the pathogenesis of hereditary spastic paraplegia. Cells. 2021;10(11):2870. doi:10.3390/cells10112870.
- Parashar S, Chidambaram R, Chen S, Liem CR, Griffis E, Lambert GG, et al. Endoplasmic reticulum tubules limit the size of misfolded protein condensates. eLife. 2021;10:e71642. doi:10.7554/eLife.71642.