1) Brown S. J. and McLean W. H. (2012) One remarkable molecule: filaggrin. J Invest Dermatol, 132, 751-762.
2) Candi E., Schmidt R., and Melino G. (2005) The cornified envelope: a model of cell death in the skin. Nat Rev Mol Cell Biol, 6, 328-340.
3) Bouwstra J. A. and Ponec M. (2006) The skin barrier in healthy and diseased state. Biochim Biophys Acta, 1758, 2080-2095.
4) Hirabayashi T., Murakami M., and Kihara A. (2019) The role of PNPLA1 in ω-O-acylceramide synthesis and skin barrier function. Biochim Biophys Acta Mol Cell Biol Lipids, 1864, 869-879.
5) Feingold K. R. and Elias P. M. (2014) Role of lipids in the formation and maintenance of the cutaneous permeability barrier. Biochim Biophys Acta, 1841, 280-294.
6) Kihara A. (2016) Synthesis and degradation pathways, functions, and pathology of ceramides and epidermal acylceramides. Prog Lipid Res, 63, 50-69.
7) Bouwstra J. A. and Honeywell-Nguyen P. L. (2002) Skin structure and mode of action of vesicles. Adv Drug Deliv Rev, 54 Suppl 1, S41-55.
8) Lundborg M., Narangifard A., Wennberg C. L., Lindahl E., Daneholt B., et al. (2018) Human skin barrier structure and function analyzed by cryo-EM and molecular dynamics simulation. J Struct Biol, 203, 149-161.
9) Maier H., Meixner M., Hartmann D., Sandhoff R., Wang-Eckhardt L., et al. (2011) Normal fur development and sebum production depends on fatty acid 2-hydroxylase expression in sebaceous glands. J Biol Chem, 286, 25922-25934.
10) Kawana M., Miyamoto M., Ohno Y., and Kihara A. (2020) Comparative profiling and comprehensive quantification of stratum corneum ceramides in humans and mice by LC/MS/MS. J Lipid Res, 61, 884-895.
11) Oji V., Tadini G., Akiyama M., Blanchet Bardon C., Bodemer C., et al. (2010) Revised nomenclature and classification of inherited ichthyoses: results of the First Ichthyosis Consensus Conference in Soreze 2009. J Am Acad Dermatol, 63, 607-641.
12) Aldahmesh M. A., Mohamed J. Y., Alkuraya H. S., Verma I. C., Puri R. D., et al. (2011) Recessive mutations in ELOVL4 cause ichthyosis, intellectual disability, and spastic quadriplegia. Am J Hum Genet, 89, 745-750.
13) Klar J., Schweiger M., Zimmerman R., Zechner R., Li H., et al. (2009) Mutations in the fatty acid transport protein 4 gene cause the ichthyosis prematurity syndrome. Am J Hum Genet, 85, 248- 253.
14) Kutkowska-Kazmierczak A., Rydzanicz M., Chlebowski A., Klosowska-Kosicka K., Mika A., et al. (2018) Dominant ELOVL1 mutation causes neurological disorder with ichthyotic keratoderma, spasticity, hypomyelination and dysmorphic features. J Med Genet, 55, 408-414.
15) Lefevre C., Jobard F., Caux F., Bouadjar B., Karaduman A., et al. (2001) Mutations in CGI-58, the gene encoding a new protein of the esterase/lipase/thioesterase subfamily, in Chanarin- Dorfman syndrome. Am J Hum Genet, 69, 1002-1012.
16) Miyamoto M., Itoh N., Sawai M., Sassa T., and Kihara A. (2020) Severe skin permeability barrier dysfunction in knockout mice deficient in a fatty acid ω-hydroxylase crucial to acylceramide production. J Invest Dermatol, 140, 319-326 e314.
17) Li W., Sandhoff R., Kono M., Zerfas P., Hoffmann V., et al. (2007) Depletion of ceramides with very long chain fatty acids causes defective skin permeability barrier function, and neonatal lethality in ELOVL4 deficient mice. Int J Biol Sci, 3, 120-128.
18) Ohno Y., Suto S., Yamanaka M., Mizutani Y., Mitsutake S., et al. (2010) ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid synthesis. Proc Natl Acad Sci U S A, 107, 18439- 18444.
19) Sassa T., Ohno Y., Suzuki S., Nomura T., Nishioka C., et al. (2013) Impaired epidermal permeability barrier in mice lacking elovl1, the gene responsible for very-long-chain fatty acid production. Mol Cell Biol, 33, 2787-2796.
20) Ohno Y., Nakamichi S., Ohkuni A., Kamiyama N., Naoe A., et al. (2015) Essential role of the cytochrome P450 CYP4F22 in the production of acylceramide, the key lipid for skin permeability barrier formation. Proc Natl Acad Sci U S A, 112, 7707-7712.
21) Mizutani Y., Mitsutake S., Tsuji K., Kihara A., and Igarashi Y. (2009) Ceramide biosynthesis in keratinocyte and its role in skin function. Biochimie, 91, 784-790.
22) Yamamoto H., Hattori M., Chamulitrat W., Ohno Y., and Kihara A. (2020) Skin permeability barrier formation by the ichthyosis-causative gene FATP4 through formation of the barrier lipid ω-O-acylceramide. Proc Natl Acad Sci U S A, 117, 2914-2922.
23) Hirabayashi T., Anjo T., Kaneko A., Senoo Y., Shibata A., et al. (2017) PNPLA1 has a crucial role in skin barrier function by directing acylceramide biosynthesis. Nat Commun, 8, 14609.
24) Kien B., Grond S., Haemmerle G., Lass A., Eichmann T. O., et al. (2018) ABHD5 stimulates PNPLA1-mediated ω-O-acylceramide biosynthesis essential for a functional skin permeability barrier. J Lipid Res, 59, 2360-2367.
25) Ohno Y., Kamiyama N., Nakamichi S., and Kihara A. (2017) PNPLA1 is a transacylase essential for the generation of the skin barrier lipid ω-O-acylceramide. Nat Commun, 8, 14610.
26) Ohno Y., Nara A., Nakamichi S., and Kihara A. (2018) Molecular mechanism of the ichthyosis pathology of Chanarin-Dorfman syndrome: Stimulation of PNPLA1-catalyzed ω-O-acylceramide production by ABHD5. J Dermatol Sci, 92, 245-253.
27) Jennemann R., Rabionet M., Gorgas K., Epstein S., Dalpke A., et al. (2012) Loss of ceramide synthase 3 causes lethal skin barrier disruption. Hum Mol Genet, 21, 586-608.
28) D'Angelo G., Polishchuk E., Di Tullio G., Santoro M., Di Campli A., et al. (2007) Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide. Nature, 449, 62-67.
29) Futerman A. H. and Pagano R. E. (1991) Determination of the intracellular sites and topology of glucosylceramide synthesis in rat liver. Biochem J, 280 ( Pt 2), 295-302.
30) Akiyama M. (2014) The roles of ABCA12 in epidermal lipid barrier formation and keratinocyte differentiation. Biochim Biophys Acta, 1841, 435-440.
31) Breiden B. and Sandhoff K. (2014) The role of sphingolipid metabolism in cutaneous permeability barrier formation. Biochim Biophys Acta, 1841, 441-452.
32) Uchida Y. and Holleran W. M. (2008) ω-O-acylceramide, a lipid essential for mammalian survival. J Dermatol Sci, 51, 77-87.
33) Zheng Y., Yin H., Boeglin W. E., Elias P. M., Crumrine D., et al. (2011) Lipoxygenases mediate the effect of essential fatty acid in skin barrier formation: a proposed role in releasing ω- hydroxyceramide for construction of the corneocyte lipid envelope. J Biol Chem, 286, 24046- 24056.
34) Nemes Z., Marekov L. N., Fesus L., and Steinert P. M. (1999) A novel function for transglutaminase 1: attachment of long-chain ω-hydroxyceramides to involucrin by ester bond formation. Proc Natl Acad Sci U S A, 96, 8402-8407.
35) Takeichi T., Hirabayashi T., Miyasaka Y., Kawamoto A., Okuno Y., et al. (2020) SDR9C7 catalyzes critical dehydrogenation of acylceramides for skin barrier formation. J Clin Invest, 130, 890-903.
36) Akiyama M. (2011) Updated molecular genetics and pathogenesis of ichthiyoses. Nagoya J Med Sci, 73, 79-90.
37) Shigehara Y., Okuda S., Nemer G., Chedraoui A., Hayashi R., et al. (2016) Mutations in SDR9C7 gene encoding an enzyme for vitamin A metabolism underlie autosomal recessive congenital ichthyosis. Hum Mol Genet, 25, 4484-4493.
38) Sniegorska D., Kowalewski C., and Wertheim-Tysarowska K. (2016) [Epidermal barrier - molecular structure and disorders in selected ichthyoses]. Postepy Biochem, 62, 36-45.
39) Cho K. H., Shim S. H., and Kim M. (2018) Clinical, biochemical, and genetic aspects of Sjögren- Larsson syndrome. Clin Genet, 93, 721-730.
40) Rizzo W. B. (2007) Sjögren-Larsson syndrome: molecular genetics and biochemical pathogenesis of fatty aldehyde dehydrogenase deficiency. Mol Genet Metab, 90, 1-9.
41) Rizzo W. B. and Carney G. (2005) Sjögren-Larsson syndrome: diversity of mutations and polymorphisms in the fatty aldehyde dehydrogenase gene (ALDH3A2). Hum Mutat, 26, 1-10.
42) Rizzo W. B. (2014) Fatty aldehyde and fatty alcohol metabolism: review and importance for epidermal structure and function. Biochim Biophys Acta, 1841, 377-389.
43) Rizzo W. B. (2011) The role of fatty aldehyde dehydrogenase in epidermal structure and function. Dermatoendocrinol, 3, 91-99.
44) Ito M., Oguro K., and Sato Y. (1991) Ultrastructural study of the skin in Sjögren-Larsson syndrome. Arch Dermatol Res, 283, 141-148.
45) Rizzo W. B., S'Aulis D., Jennings M. A., Crumrine D. A., Williams M. L., et al. (2010) Ichthyosis in Sjögren-Larsson syndrome reflects defective barrier function due to abnormal lamellar body structure and secretion. Arch Dermatol Res, 302, 443-451.
46) Haug S. and Braun-Falco M. (2006) Restoration of fatty aldehyde dehydrogenase deficiency in Sjögren-Larsson syndrome. Gene Ther, 13, 1021-1026.
47) Jagell S. and Liden S. (1982) Ichthyosis in the Sjögren-Larsson syndrome. Clin Genet, 21, 243- 252.
48) Nakajima K., Sano S., Uchida Y., Akiyama M., Morita Y., et al. (2011) Altered lipid profiles in the stratum corneum of Sjögren-Larsson syndrome. J Dermatol Sci, 63, 64-66.
49) Willemsen M. A., Van Der Graaf M., Van Der Knaap M. S., Heerschap A., Van Domburg P. H., et al. (2004) MR imaging and proton MR spectroscopic studies in Sjögren-Larsson syndrome: characterization of the leukoencephalopathy. AJNR Am J Neuroradiol, 25, 649-657.
50) Jackson B., Brocker C., Thompson D. C., Black W., Vasiliou K., et al. (2011) Update on the aldehyde dehydrogenase gene (ALDH) superfamily. Hum Genomics, 5, 283-303.
51) Marchitti S. A., Brocker C., Stagos D., and Vasiliou V. (2008) Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily. Expert Opin Drug Metab Toxicol, 4, 697-720.
52) Kitamura T., Takagi S., Naganuma T., and Kihara A. (2015) Mouse aldehyde dehydrogenase ALDH3B2 is localized to lipid droplets via two C-terminal tryptophan residues and lipid modification. Biochem J, 465, 79-87.
53) Estey T., Piatigorsky J., Lassen N., and Vasiliou V. (2007) ALDH3A1: a corneal crystallin with diverse functions. Exp Eye Res, 84, 3-12.
54) Pappa A., Estey T., Manzer R., Brown D., and Vasiliou V. (2003) Human aldehyde dehydrogenase 3A1 (ALDH3A1): biochemical characterization and immunohistochemical localization in the cornea. Biochem J, 376, 615-623.
55) Lassen N., Bateman J. B., Estey T., Kuszak J. R., Nees D. W., et al. (2007) Multiple and additive functions of ALDH3A1 and ALDH1A1: cataract phenotype and ocular oxidative damage in Aldh3a1(-/-)/Aldh1a1(-/-) knock-out mice. J Biol Chem, 282, 25668-25676.
56) Nees D. W., Wawrousek E. F., Robison W. G., Jr., and Piatigorsky J. (2002) Structurally normal corneas in aldehyde dehydrogenase 3a1-deficient mice. Mol Cell Biol, 22, 849-855.
57) Kelson T. L., Secor McVoy J. R., and Rizzo W. B. (1997) Human liver fatty aldehyde dehydrogenase: microsomal localization, purification, and biochemical characterization. Biochim Biophys Acta, 1335, 99-110.
58) Keller M. A., Zander U., Fuchs J. E., Kreutz C., Watschinger K., et al. (2014) A gatekeeper helix determines the substrate specificity of Sjögren-Larsson Syndrome enzyme fatty aldehyde dehydrogenase. Nat Commun, 5, 4439.
59) Nakahara K., Ohkuni A., Kitamura T., Abe K., Naganuma T., et al. (2012) The Sjögren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway. Mol Cell, 46, 461-471.
60) Rizzo W. B., Heinz E., Simon M., and Craft D. A. (2000) Microsomal fatty aldehyde dehydrogenase catalyzes the oxidation of aliphatic aldehyde derived from ether glycerolipid catabolism: implications for Sjögren-Larsson syndrome. Biochim Biophys Acta, 1535, 1-9.
61) van den Brink D. M., van Miert J. N., Dacremont G., Rontani J. F., Jansen G. A., et al. (2004) Identification of fatty aldehyde dehydrogenase in the breakdown of phytol to phytanic acid. Mol Genet Metab, 82, 33-37.
62) Verhoeven N. M., Jakobs C., Carney G., Somers M. P., Wanders R. J., et al. (1998) Involvement of microsomal fatty aldehyde dehydrogenase in the α-oxidation of phytanic acid. FEBS Lett, 429, 225-228.
63) Willemsen M. A., Rotteveel J. J., de Jong J. G., Wanders R. J., L I. J., et al. (2001) Defective metabolism of leukotriene B4 in the Sjögren-Larsson syndrome. J Neurol Sci, 183, 61-67.
64) Ashibe B., Hirai T., Higashi K., Sekimizu K., and Motojima K. (2007) Dual subcellular localization in the endoplasmic reticulum and peroxisomes and a vital role in protecting against oxidative stress of fatty aldehyde dehydrogenase are achieved by alternative splicing. J Biol Chem, 282, 20763-20773.
65) Marchitti S. A., Brocker C., Orlicky D. J., and Vasiliou V. (2010) Molecular characterization, expression analysis, and role of ALDH3B1 in the cellular protection against oxidative stress. Free Radic Biol Med, 49, 1432-1443.
66) Marchitti S. A., Orlicky D. J., Brocker C., and Vasiliou V. (2010) Aldehyde dehydrogenase 3B1 (ALDH3B1): immunohistochemical tissue distribution and cellular-specific localization in normal and cancerous human tissues. J Histochem Cytochem, 58, 765-783.
67) Marchitti S. A., Orlicky D. J., and Vasiliou V. (2007) Expression and initial characterization of human ALDH3B1. Biochem Biophys Res Commun, 356, 792-798.
68) Kitamura T., Naganuma T., Abe K., Nakahara K., Ohno Y., et al. (2013) Substrate specificity, plasma membrane localization, and lipid modification of the aldehyde dehydrogenase ALDH3B1. Biochim Biophys Acta, 1831, 1395-1401.
69) Kariya Y., Kihara A., Ikeda M., Kikuchi F., Nakamura S., et al. (2005) Products by the sphingosine kinase/sphingosine 1-phosphate (S1P) lyase pathway but not S1P stimulate mitogenesis. Genes Cells, 10, 605-615.
70) Kihara A., Anada Y., and Igarashi Y. (2006) Mouse sphingosine kinase isoforms SPHK1a and SPHK1b differ in enzymatic traits including stability, localization, modification, and oligomerization. J Biol Chem, 281, 4532-4539.
71) Kihara A., Mitsutake S., Mizutani Y., and Igarashi Y. (2007) Metabolism and biological functions of two phosphorylated sphingolipids, sphingosine 1-phosphate and ceramide 1-phosphate. Prog Lipid Res, 46, 126-144.
72) Olivera A., Kohama T., Tu Z., Milstien S., and Spiegel S. (1998) Purification and characterization of rat kidney sphingosine kinase. J Biol Chem, 273, 12576-12583.
73) Catala A. (2009) Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions. Chem Phys Lipids, 157, 1-11.
74) Yoritaka A., Hattori N., Uchida K., Tanaka M., Stadtman E. R., et al. (1996) Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease. Proc Natl Acad Sci U S A, 93, 2696-2701.
75) Wakashima T., Abe K., and Kihara A. (2014) Dual functions of the trans-2-enoyl-CoA reductase TER in the sphingosine 1-phosphate metabolic pathway and in fatty acid elongation. J Biol Chem, 289, 24736-24748.
76) Saba J. D. (2019) Fifty years of lyase and a moment of truth: sphingosine phosphate lyase from discovery to disease. J Lipid Res, 60, 456-463.
77) Yu F. P. S., Amintas S., Levade T., and Medin J. A. (2018) Acid ceramidase deficiency: Farber disease and SMA-PME. Orphanet J Rare Dis, 13, 121.
78) Mao C. and Obeid L. M. (2008) Ceramidases: regulators of cellular responses mediated by ceramide, sphingosine, and sphingosine-1-phosphate. Biochim Biophys Acta, 1781, 424-434.
79) Parveen F., Bender D., Law S. H., Mishra V. K., Chen C. C., et al. (2019) Role of Ceramidases in Sphingolipid Metabolism and Human Diseases. Cells, 8
80) Li C. M., Park J. H., He X., Levy B., Chen F., et al. (1999) The human acid ceramidase gene (ASAH): structure, chromosomal location, mutation analysis, and expression. Genomics, 62, 223- 231.
81) Bar J., Linke T., Ferlinz K., Neumann U., Schuchman E. H., et al. (2001) Molecular analysis of acid ceramidase deficiency in patients with Farber disease. Hum Mutat, 17, 199-209.
82) Sugita M., Dulaney J. T., and Moser H. W. (1972) Ceramidase deficiency in Farber's disease (lipogranulomatosis). Science, 178, 1100-1102.
83) Eliyahu E., Park J. H., Shtraizent N., He X., and Schuchman E. H. (2007) Acid ceramidase is a novel factor required for early embryo survival. FASEB J, 21, 1403-1409.
84) Kono M., Dreier J. L., Ellis J. M., Allende M. L., Kalkofen D. N., et al. (2006) Neutral ceramidase encoded by the Asah2 gene is essential for the intestinal degradation of sphingolipids. J Biol Chem, 281, 7324-7331.
85) Sakamoto W., Coant N., Canals D., Obeid L. M., and Hannun Y. A. (2018) Functions of neutral ceramidase in the Golgi apparatus. J Lipid Res, 59, 2116-2125.
86) Hu W., Xu R., Sun W., Szulc Z. M., Bielawski J., et al. (2010) Alkaline ceramidase 3 (ACER3) hydrolyzes unsaturated long-chain ceramides, and its down-regulation inhibits both cell proliferation and apoptosis. J Biol Chem, 285, 7964-7976.
87) Mao C., Xu R., Szulc Z. M., Bielawska A., Galadari S. H., et al. (2001) Cloning and characterization of a novel human alkaline ceramidase. A mammalian enzyme that hydrolyzes phytoceramide. J Biol Chem, 276, 26577-26588.
88) Sun W., Jin J., Xu R., Hu W., Szulc Z. M., et al. (2010) Substrate specificity, membrane topology, and activity regulation of human alkaline ceramidase 2 (ACER2). J Biol Chem, 285, 8995-9007.
89) Xu R., Jin J., Hu W., Sun W., Bielawski J., et al. (2006) Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P. FASEB J, 20, 1813-1825.
90) Liakath-Ali K., Vancollie V. E., Lelliott C. J., Speak A. O., Lafont D., et al. (2016) Alkaline ceramidase 1 is essential for mammalian skin homeostasis and regulating whole-body energy expenditure. J Pathol, 239, 374-383.
91) Naganuma T., Takagi S., Kanetake T., Kitamura T., Hattori S., et al. (2016) Disruption of the Sjögren-Larsson syndrome gene Aldh3a2 in mice increases keratinocyte growth and retards skin barrier recovery. J Biol Chem, 291, 11676-11688.
92) Kanetake T., Sassa T., Nojiri K., Sawai M., Hattori S., et al. (2019) Neural symptoms in a gene knockout mouse model of Sjögren-Larsson syndrome are associated with a decrease in 2- hydroxygalactosylceramide. FASEB J, 33, 928-941.
93) Hoshi M., Williams M., and Kishimoto Y. (1973) Characterization of brain cerebrosides at early stages of development in the rat. J Neurochem, 21, 709-712.
94) Alderson N. L., Rembiesa B. M., Walla M. D., Bielawska A., Bielawski J., et al. (2004) The human FA2H gene encodes a fatty acid 2-hydroxylase. J Biol Chem, 279, 48562-48568.
95) Kruer M. C., Paisan-Ruiz C., Boddaert N., Yoon M. Y., Hama H., et al. (2010) Defective FA2H leads to a novel form of neurodegeneration with brain iron accumulation (NBIA). Ann Neurol, 68, 611-618.
96) Potter K. A., Kern M. J., Fullbright G., Bielawski J., Scherer S. S., et al. (2011) Central nervous system dysfunction in a mouse model of FA2H deficiency. Glia, 59, 1009-1021.
97) Alderson N. L., Maldonado E. N., Kern M. J., Bhat N. R., and Hama H. (2006) FA2H-dependent fatty acid 2-hydroxylation in postnatal mouse brain. J Lipid Res, 47, 2772-2780.
98) Cao L., Huang X. J., Chen C. J., and Chen S. D. (2013) A rare family with Hereditary Spastic Paraplegia Type 35 due to novel FA2H mutations: a case report with literature review. J Neurol Sci, 329, 1-5.
99) Edvardson S., Hama H., Shaag A., Gomori J. M., Berger I., et al. (2008) Mutations in the fatty acid 2-hydroxylase gene are associated with leukodystrophy with spastic paraparesis and dystonia. Am J Hum Genet, 83, 643-648.
100) Schumacher F., Neuber C., Finke H., Nieschalke K., Baesler J., et al. (2017) The sphingosine 1- phosphate breakdown product, (2E)-hexadecenal, forms protein adducts and glutathione conjugates in vitro. J lipid research, 58, 1648-1660.
101) Honda Y., Kitamura T., Naganuma T., Abe T., Ohno Y., et al. (2018) Decreased skin barrier lipid acylceramide and differentiation-dependent gene expression in ichthyosis gene Nipal4-knockout mice. J Invest Dermatol, 138, 741-749.
102) Hama H. (2010) Fatty acid 2-hydroxylation in mammalian sphingolipid biology. Biochim Biophys Acta, 1801, 405-414.
103) Eckhardt M., Yaghootfam A., Fewou S. N., Zoller I., and Gieselmann V. (2005) A mammalian fatty acid hydroxylase responsible for the formation of α-hydroxylated galactosylceramide in myelin. Biochem J, 388, 245-254.
104) Zhu G., Koszelak-Rosenblum M., Connelly S. M., Dumont M. E., and Malkowski M. G. (2015) The crystal structure of an integral membrane fatty acid α-hydroxylase. J biol chem, 290, 29820- 29833.
105) Lass A., Zimmermann R., Haemmerle G., Riederer M., Schoiswohl G., et al. (2006) Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome. Cell Metab, 3, 309-319.
106) Yang A., Mottillo E. P., Mladenovic-Lucas L., Zhou L., and Granneman J. G. (2019) Dynamic interactions of ABHD5 with PNPLA3 regulate triacylglycerol metabolism in brown adipocytes. Nat Metab, 1, 560-569.
107) Takeichi T. and Akiyama M. (2016) Inherited ichthyosis: Non-syndromic forms. J Dermatol, 43, 242-251.
108) Lord C. C., Thomas G., and Brown J. M. (2013) Mammalian alpha beta hydrolase domain (ABHD) proteins: Lipid metabolizing enzymes at the interface of cell signaling and energy metabolism. Biochim Biophys Acta, 1831, 792-802.
109) Brown A. L. and Mark Brown J. (2017) Critical roles for α/β hydrolase domain 5 (ABHD5)/comparative gene identification-58 (CGI-58) at the lipid droplet interface and beyond. Biochim Biophys Acta Mol Cell Biol Lipids, 1862, 1233-1241.
110) Ikeda M., Kihara A., and Igarashi Y. (2004) Sphingosine-1-phosphate lyase SPL is an endoplasmic reticulum-resident, integral membrane protein with the pyridoxal 5'-phosphate binding domain exposed to the cytosol. Biochem Biophys Res Commun, 325, 338-343.
111) Edagawa M., Sawai M., Ohno Y., and Kihara A. (2018) Widespread tissue distribution and synthetic pathway of polyunsaturated C24:2 sphingolipids in mammals. Biochim Biophys Acta Mol Cell Biol Lipids, 1863, 1441-1448.
112) Houben E., Holleran W. M., Yaginuma T., Mao C., Obeid L. M., et al. (2006) Differentiation- associated expression of ceramidase isoforms in cultured keratinocytes and epidermis. J Lipid Res, 47, 1063-1070.
113) Sun W., Xu R., Hu W., Jin J., Crellin H. A., et al. (2008) Upregulation of the human alkaline ceramidase 1 and acid ceramidase mediates calcium-induced differentiation of epidermal keratinocytes. J Invest Dermatol, 128, 389-397.
114) Hanada K. (2003) Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Biochim Biophys Acta, 1632, 16-30.
115) Kihara A. and Igarashi Y. (2004) FVT-1 is a mammalian 3-ketodihydrosphingosine reductase with an active site that faces the cytosolic side of the endoplasmic reticulum membrane. J Biol Chem, 279, 49243-49250.
116) Michel C., van Echten-Deckert G., Rother J., Sandhoff K., Wang E., et al. (1997) Characterization of ceramide synthesis. A dihydroceramide desaturase introduces the 4,5-trans-double bond of sphingosine at the level of dihydroceramide. J Biol Chem, 272, 22432-22437.
117) Kihara A. (2012) Very long-chain fatty acids: elongation, physiology and related disorders. J Biochem, 152, 387-395.
118) Sassa T. and Kihara A. (2014) Metabolism of very long-chain fatty acids: genes and pathophysiology. Biomol Ther (Seoul), 22, 83-92.
論文の公開元へ
