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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
The '''ASAH1''' [[gene]] encodes in humans the ''acid [[ceramidase]]'' [[enzyme]].<ref name="pmid8955159">{{cite journal | vauthors = Koch J, Gärtner S, Li CM, Quintern LE, Bernardo K, Levran O, Schnabel D, Desnick RJ, Schuchman EH, Sandhoff K | title = Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease | journal = The Journal of Biological Chemistry | volume = 271 | issue = 51 | pages = 33110–5 | date = December 1996 | pmid = 8955159 | pmc =  | doi = 10.1074/jbc.271.51.33110 }}</ref><ref name="pmid10610716">{{cite journal | vauthors = Li CM, Park JH, He X, Levy B, Chen F, Arai K, Adler DA, Disteche CM, Koch J, Sandhoff K, Schuchman EH | title = The human acid ceramidase gene (ASAH): structure, chromosomal location, mutation analysis, and expression | journal = Genomics | volume = 62 | issue = 2 | pages = 223–31 | date = December 1999 | pmid = 10610716 | pmc =  | doi = 10.1006/geno.1999.5940 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ASAH1 N-acylsphingosine amidohydrolase (acid ceramidase) 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=427| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = N-acylsphingosine amidohydrolase (acid ceramidase) 1
| HGNCid = 735
| Symbol = ASAH1
| AltSymbols =; AC; ASAH; FLJ21558; FLJ22079; PHP; PHP32
| OMIM = 228000
| ECnumber = 
| Homologene = 10504
| MGIid = 1277124
| GeneAtlas_image1 = PBB_GE_ASAH1_210980_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ASAH1_213702_x_at_tn.png
| Function = {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0017040 |text = ceramidase activity}} {{GNF_GO|id=GO:0046912 |text = transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006631 |text = fatty acid metabolic process}} {{GNF_GO|id=GO:0006672 |text = ceramide metabolic process}} {{GNF_GO|id=GO:0019752 |text = carboxylic acid metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 427
    | Hs_Ensembl = ENSG00000104763
    | Hs_RefseqProtein = NP_004306
    | Hs_RefseqmRNA = NM_004315
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 17958214
    | Hs_GenLoc_end = 17986757
    | Hs_Uniprot = Q13510
    | Mm_EntrezGene = 11886
    | Mm_Ensembl = ENSMUSG00000031591
    | Mm_RefseqmRNA = NM_019734
    | Mm_RefseqProtein = NP_062708
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 42839468
    | Mm_GenLoc_end = 42873466
    | Mm_Uniprot = Q3TWT5
  }}
}}
'''N-acylsphingosine amidohydrolase (acid ceramidase) 1''', also known as '''ASAH1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ASAH1 N-acylsphingosine amidohydrolase (acid ceramidase) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=427| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a [[Heterodimeric#Biochemistry|heterodimeric]] protein consisting of a nonglycosylated alpha subunit and a [[Glycosylation|glycosylated]] beta subunit that is cleaved to the mature enzyme [[Posttranslational modification|posttranslationally]]. The encoded protein catalyzes the synthesis and degradation of [[ceramide]] into [[sphingosine]] and fatty acid. Mutations in this gene have been associated with a [[lysosomal storage disorder]] known as [[Farber disease]] and, recently, with a rare neurodegenerative condition known as [[spinal muscular atrophy with progressive myoclonic epilepsy]].<ref>{{cite journal | vauthors = Zhou J, Tawk M, Tiziano FD, Veillet J, Bayes M, Nolent F, Garcia V, Servidei S, Bertini E, Castro-Giner F, Renda Y, Carpentier S, Andrieu-Abadie N, Gut I, Levade T, Topaloglu H, Melki J | title = Spinal muscular atrophy associated with progressive myoclonic epilepsy is caused by mutations in ASAH1 | journal = American Journal of Human Genetics | volume = 91 | issue = 1 | pages = 5–14 | date = July 2012 | pmid = 22703880 | pmc = 3397266 | doi = 10.1016/j.ajhg.2012.05.001 }}</ref> Two transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez"/> In [[Melanocyte|melanocytic cells]] ASAH1 gene expression may be regulated by [[Microphthalmia-associated transcription factor|MITF]].<ref name="pmid19067971">{{cite journal | vauthors = Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E | title = Novel MITF targets identified using a two-step DNA microarray strategy | journal = Pigment Cell & Melanoma Research | volume = 21 | issue = 6 | pages = 665–76 | date = December 2008 | pmid = 19067971 | doi = 10.1111/j.1755-148X.2008.00505.x }}</ref>
{{PBB_Summary
 
| section_title =
== As a glioblastoma drug target ==
| summary_text = This gene encodes a heterodimeric protein consisting of a nonglycosylated alpha subunit and a glycosylated beta subunit that is cleaved to the mature enzyme posttranslationally. The encoded protein catalyzes the synthesis and degradation of ceramide into sphingosine and fatty acid. Mutations in this gene have been associated with a lysosomal storage disorder known as [[Farber disease]]. Two transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ASAH1 N-acylsphingosine amidohydrolase (acid ceramidase) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=427| accessdate = }}</ref>
 
}}
ASAH1 expression is upregulated following radiation, suggesting it plays a role in conferring radioresistance to [[glioblastoma]] and in the development of recurrent glioblastoma.<ref>{{cite journal | vauthors = Doan NB, Nguyen HS, Al-Gizawiy MM, Mueller WM, Sabbadini RA, Rand SD, Connelly JM, Chitambar CR, Schmainda KM, Mirza SP | title = Acid ceramidase confers radioresistance to glioblastoma cells | journal = Oncology Reports | volume = 38 | issue = 4 | pages = 1932–40 | date = October 2017 | pmid = 28765947 | doi = 10.3892/or.2017.5855 }}</ref> Inhibiting the activity of ASAH1 with [[carmofur]], a drug that has been approved for clinical treatment of [[colorectal cancer]]s in several countries, leads to substantial cell deaths and as a result has been proposed as a drug target in the treatment of glioblastoma.<ref>{{cite journal | vauthors = Doan NB, Alhajala H, Al-Gizawiy MM, Mueller WM, Rand SD, Connelly JM, Cochran EJ, Chitambar CR, Clark P, Kuo J, Schmainda KM, Mirza SP | title = Acid ceramidase and its inhibitors: a de novo drug target and a new class of drugs for killing glioblastoma cancer stem cells with high efficiency | journal = Oncotarget | volume = 8 | issue = 68 | pages = 112662–74 | date = December 2017 | pmid = 29348854 | doi = 10.18632/oncotarget.22637 }}</ref> It has also been suggested to be a novel drug target against pediatric brain tumors as well.<ref>{{cite journal | vauthors = Doan NB, Nguyen HS, Montoure A, Al-Gizawiy MM, Mueller WM, Kurpad S, Rand SD, Connelly JM, Chitambar CR, Schmainda KM, Mirza SP | title = Acid ceramidase is a novel drug target for pediatric brain tumors | journal = Oncotarget | volume = 8 | issue = 15 | pages = 24753–61 | date = April 2017 | pmid = 28445970 | doi = 10.18632/oncotarget.15800 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
==Further reading==
 
==External links==
* {{UCSC gene info|ASAH1}}
{{clear}}
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Perry DK, Hannun YA | title = The role of ceramide in cell signaling | journal = Biochimica et Biophysica Acta | volume = 1436 | issue = 1–2 | pages = 233–43 | date = December 1998 | pmid = 9838138 | doi = 10.1016/S0005-2760(98)00145-3 }}
| citations =
* {{cite journal | vauthors = Bernardo K, Hurwitz R, Zenk T, Desnick RJ, Ferlinz K, Schuchman EH, Sandhoff K | title = Purification, characterization, and biosynthesis of human acid ceramidase | journal = The Journal of Biological Chemistry | volume = 270 | issue = 19 | pages = 11098–102 | date = May 1995 | pmid = 7744740 | doi = 10.1074/jbc.270.19.11098 }}
*{{cite journal | author=Perry DK, Hannun YA |title=The role of ceramide in cell signaling. |journal=Biochim. Biophys. Acta |volume=1436 |issue= 1-2 |pages= 233-43 |year= 1999 |pmid= 9838138 |doi= }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Bernardo K, Hurwitz R, Zenk T, ''et al.'' |title=Purification, characterization, and biosynthesis of human acid ceramidase. |journal=J. Biol. Chem. |volume=270 |issue= 19 |pages= 11098-102 |year= 1995 |pmid= 7744740 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Seelan RS, Qian C, Yokomizo A, Bostwick DG, Smith DI, Liu W | title = Human acid ceramidase is overexpressed but not mutated in prostate cancer | journal = Genes, Chromosomes & Cancer | volume = 29 | issue = 2 | pages = 137–46 | date = October 2000 | pmid = 10959093 | doi = 10.1002/1098-2264(2000)9999:9999<::AID-GCC1018>3.0.CO;2-E }}
*{{cite journal  | author=Koch J, Gärtner S, Li CM, ''et al.'' |title=Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease. |journal=J. Biol. Chem. |volume=271 |issue= 51 |pages= 33110-5 |year= 1997 |pmid= 8955159 |doi=  }}
* {{cite journal | vauthors = Strelow A, Bernardo K, Adam-Klages S, Linke T, Sandhoff K, Krönke M, Adam D | title = Overexpression of acid ceramidase protects from tumor necrosis factor-induced cell death | journal = The Journal of Experimental Medicine | volume = 192 | issue = 5 | pages = 601–12 | date = September 2000 | pmid = 10974027 | pmc = 2193270 | doi = 10.1084/jem.192.5.601 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Bär J, Linke T, Ferlinz K, Neumann U, Schuchman EH, Sandhoff K | title = Molecular analysis of acid ceramidase deficiency in patients with Farber disease | journal = Human Mutation | volume = 17 | issue = 3 | pages = 199–209 | date = March 2001 | pmid = 11241842 | doi = 10.1002/humu.5 }}
*{{cite journal  | author=Li CM, Park JH, He X, ''et al.'' |title=The human acid ceramidase gene (ASAH): structure, chromosomal location, mutation analysis, and expression. |journal=Genomics |volume=62 |issue= 2 |pages= 223-31 |year= 2000 |pmid= 10610716 |doi= 10.1006/geno.1999.5940 }}
* {{cite journal | vauthors = Ferlinz K, Kopal G, Bernardo K, Linke T, Bar J, Breiden B, Neumann U, Lang F, Schuchman EH, Sandhoff K | title = Human acid ceramidase: processing, glycosylation, and lysosomal targeting | journal = The Journal of Biological Chemistry | volume = 276 | issue = 38 | pages = 35352–60 | date = September 2001 | pmid = 11451951 | doi = 10.1074/jbc.M103066200 }}
*{{cite journal | author=Seelan RS, Qian C, Yokomizo A, ''et al.'' |title=Human acid ceramidase is overexpressed but not mutated in prostate cancer. |journal=Genes Chromosomes Cancer |volume=29 |issue= 2 |pages= 137-46 |year= 2000 |pmid= 10959093 |doi= }}
* {{cite journal | vauthors = Muramatsu T, Sakai N, Yanagihara I, Yamada M, Nishigaki T, Kokubu C, Tsukamoto H, Ito M, Inui K | title = Mutation analysis of the acid ceramidase gene in Japanese patients with Farber disease | journal = Journal of Inherited Metabolic Disease | volume = 25 | issue = 7 | pages = 585–92 | date = November 2002 | pmid = 12638942 | doi = 10.1023/A:1022047408477 }}
*{{cite journal | author=Strelow A, Bernardo K, Adam-Klages S, ''et al.'' |title=Overexpression of acid ceramidase protects from tumor necrosis factor-induced cell death. |journal=J. Exp. Med. |volume=192 |issue= 5 |pages= 601-12 |year= 2000 |pmid= 10974027 |doi= }}
* {{cite journal | vauthors = Zhang H, Li XJ, Martin DB, Aebersold R | title = Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry | journal = Nature Biotechnology | volume = 21 | issue = 6 | pages = 660–6 | date = June 2003 | pmid = 12754519 | doi = 10.1038/nbt827 }}
*{{cite journal | author=Bär J, Linke T, Ferlinz K, ''et al.'' |title=Molecular analysis of acid ceramidase deficiency in patients with Farber disease. |journal=Hum. Mutat. |volume=17 |issue= 3 |pages= 199-209 |year= 2001 |pmid= 11241842 |doi= 10.1002/humu.5 }}
* {{cite journal | vauthors = Okino N, He X, Gatt S, Sandhoff K, Ito M, Schuchman EH | title = The reverse activity of human acid ceramidase | journal = The Journal of Biological Chemistry | volume = 278 | issue = 32 | pages = 29948–53 | date = August 2003 | pmid = 12764132 | doi = 10.1074/jbc.M303310200 }}
*{{cite journal | author=Ferlinz K, Kopal G, Bernardo K, ''et al.'' |title=Human acid ceramidase: processing, glycosylation, and lysosomal targeting. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35352-60 |year= 2001 |pmid= 11451951 |doi= 10.1074/jbc.M103066200 }}
* {{cite journal | vauthors = He X, Okino N, Dhami R, Dagan A, Gatt S, Schulze H, Sandhoff K, Schuchman EH | title = Purification and characterization of recombinant, human acid ceramidase. Catalytic reactions and interactions with acid sphingomyelinase | journal = The Journal of Biological Chemistry | volume = 278 | issue = 35 | pages = 32978–86 | date = August 2003 | pmid = 12815059 | doi = 10.1074/jbc.M301936200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Hara S, Nakashima S, Kiyono T, Sawada M, Yoshimura S, Iwama T, Banno Y, Shinoda J, Sakai N | title = p53-Independent ceramide formation in human glioma cells during gamma-radiation-induced apoptosis | journal = Cell Death and Differentiation | volume = 11 | issue = 8 | pages = 853–61 | date = August 2004 | pmid = 15088070 | doi = 10.1038/sj.cdd.4401428 }}
*{{cite journal  | author=Muramatsu T, Sakai N, Yanagihara I, ''et al.'' |title=Mutation analysis of the acid ceramidase gene in Japanese patients with Farber disease. |journal=J. Inherit. Metab. Dis. |volume=25 |issue= 7 |pages= 585-92 |year= 2003 |pmid= 12638942 |doi= }}
* {{cite journal | vauthors = Lewandrowski U, Moebius J, Walter U, Sickmann A | title = Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach | journal = Molecular & Cellular Proteomics | volume = 5 | issue = 2 | pages = 226–33 | date = February 2006 | pmid = 16263699 | doi = 10.1074/mcp.M500324-MCP200 }}
*{{cite journal | author=Zhang H, Li XJ, Martin DB, Aebersold R |title=Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. |journal=Nat. Biotechnol. |volume=21 |issue= 6 |pages= 660-6 |year= 2003 |pmid= 12754519 |doi= 10.1038/nbt827 }}
*{{cite journal | author=Okino N, He X, Gatt S, ''et al.'' |title=The reverse activity of human acid ceramidase. |journal=J. Biol. Chem. |volume=278 |issue= 32 |pages= 29948-53 |year= 2003 |pmid= 12764132 |doi= 10.1074/jbc.M303310200 }}
*{{cite journal | author=He X, Okino N, Dhami R, ''et al.'' |title=Purification and characterization of recombinant, human acid ceramidase. Catalytic reactions and interactions with acid sphingomyelinase. |journal=J. Biol. Chem. |volume=278 |issue= 35 |pages= 32978-86 |year= 2003 |pmid= 12815059 |doi= 10.1074/jbc.M301936200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Hara S, Nakashima S, Kiyono T, ''et al.'' |title=p53-Independent ceramide formation in human glioma cells during gamma-radiation-induced apoptosis. |journal=Cell Death Differ. |volume=11 |issue= 8 |pages= 853-61 |year= 2005 |pmid= 15088070 |doi= 10.1038/sj.cdd.4401428 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Lewandrowski U, Moebius J, Walter U, Sickmann A |title=Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. |journal=Mol. Cell Proteomics |volume=5 |issue= 2 |pages= 226-33 |year= 2006 |pmid= 16263699 |doi= 10.1074/mcp.M500324-MCP200 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Glycolipid metabolism}}
{{Glycolipid metabolism}}
{{WikiDoc Sources}}
 
 
 
{{gene-8-stub}}

Latest revision as of 08:39, 10 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

The ASAH1 gene encodes in humans the acid ceramidase enzyme.[1][2][3]

Function

This gene encodes a heterodimeric protein consisting of a nonglycosylated alpha subunit and a glycosylated beta subunit that is cleaved to the mature enzyme posttranslationally. The encoded protein catalyzes the synthesis and degradation of ceramide into sphingosine and fatty acid. Mutations in this gene have been associated with a lysosomal storage disorder known as Farber disease and, recently, with a rare neurodegenerative condition known as spinal muscular atrophy with progressive myoclonic epilepsy.[4] Two transcript variants encoding distinct isoforms have been identified for this gene.[3] In melanocytic cells ASAH1 gene expression may be regulated by MITF.[5]

As a glioblastoma drug target

ASAH1 expression is upregulated following radiation, suggesting it plays a role in conferring radioresistance to glioblastoma and in the development of recurrent glioblastoma.[6] Inhibiting the activity of ASAH1 with carmofur, a drug that has been approved for clinical treatment of colorectal cancers in several countries, leads to substantial cell deaths and as a result has been proposed as a drug target in the treatment of glioblastoma.[7] It has also been suggested to be a novel drug target against pediatric brain tumors as well.[8]

References

  1. ↑ Koch J, Gärtner S, Li CM, Quintern LE, Bernardo K, Levran O, Schnabel D, Desnick RJ, Schuchman EH, Sandhoff K (December 1996). "Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease". The Journal of Biological Chemistry. 271 (51): 33110–5. doi:10.1074/jbc.271.51.33110. PMID 8955159.
  2. ↑ Li CM, Park JH, He X, Levy B, Chen F, Arai K, Adler DA, Disteche CM, Koch J, Sandhoff K, Schuchman EH (December 1999). "The human acid ceramidase gene (ASAH): structure, chromosomal location, mutation analysis, and expression". Genomics. 62 (2): 223–31. doi:10.1006/geno.1999.5940. PMID 10610716.
  3. ↑ 3.0 3.1 "Entrez Gene: ASAH1 N-acylsphingosine amidohydrolase (acid ceramidase) 1".
  4. ↑ Zhou J, Tawk M, Tiziano FD, Veillet J, Bayes M, Nolent F, Garcia V, Servidei S, Bertini E, Castro-Giner F, Renda Y, Carpentier S, Andrieu-Abadie N, Gut I, Levade T, Topaloglu H, Melki J (July 2012). "Spinal muscular atrophy associated with progressive myoclonic epilepsy is caused by mutations in ASAH1". American Journal of Human Genetics. 91 (1): 5–14. doi:10.1016/j.ajhg.2012.05.001. PMC 3397266. PMID 22703880.
  5. ↑ Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E (December 2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell & Melanoma Research. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
  6. ↑ Doan NB, Nguyen HS, Al-Gizawiy MM, Mueller WM, Sabbadini RA, Rand SD, Connelly JM, Chitambar CR, Schmainda KM, Mirza SP (October 2017). "Acid ceramidase confers radioresistance to glioblastoma cells". Oncology Reports. 38 (4): 1932–40. doi:10.3892/or.2017.5855. PMID 28765947.
  7. ↑ Doan NB, Alhajala H, Al-Gizawiy MM, Mueller WM, Rand SD, Connelly JM, Cochran EJ, Chitambar CR, Clark P, Kuo J, Schmainda KM, Mirza SP (December 2017). "Acid ceramidase and its inhibitors: a de novo drug target and a new class of drugs for killing glioblastoma cancer stem cells with high efficiency". Oncotarget. 8 (68): 112662–74. doi:10.18632/oncotarget.22637. PMID 29348854.
  8. ↑ Doan NB, Nguyen HS, Montoure A, Al-Gizawiy MM, Mueller WM, Kurpad S, Rand SD, Connelly JM, Chitambar CR, Schmainda KM, Mirza SP (April 2017). "Acid ceramidase is a novel drug target for pediatric brain tumors". Oncotarget. 8 (15): 24753–61. doi:10.18632/oncotarget.15800. PMID 28445970.

External links

Further reading

  • Perry DK, Hannun YA (December 1998). "The role of ceramide in cell signaling". Biochimica et Biophysica Acta. 1436 (1–2): 233–43. doi:10.1016/S0005-2760(98)00145-3. PMID 9838138.
  • Bernardo K, Hurwitz R, Zenk T, Desnick RJ, Ferlinz K, Schuchman EH, Sandhoff K (May 1995). "Purification, characterization, and biosynthesis of human acid ceramidase". The Journal of Biological Chemistry. 270 (19): 11098–102. doi:10.1074/jbc.270.19.11098. PMID 7744740.
  • Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Seelan RS, Qian C, Yokomizo A, Bostwick DG, Smith DI, Liu W (October 2000). "Human acid ceramidase is overexpressed but not mutated in prostate cancer". Genes, Chromosomes & Cancer. 29 (2): 137–46. doi:10.1002/1098-2264(2000)9999:9999<::AID-GCC1018>3.0.CO;2-E. PMID 10959093.
  • Strelow A, Bernardo K, Adam-Klages S, Linke T, Sandhoff K, Krönke M, Adam D (September 2000). "Overexpression of acid ceramidase protects from tumor necrosis factor-induced cell death". The Journal of Experimental Medicine. 192 (5): 601–12. doi:10.1084/jem.192.5.601. PMC 2193270. PMID 10974027.
  • Bär J, Linke T, Ferlinz K, Neumann U, Schuchman EH, Sandhoff K (March 2001). "Molecular analysis of acid ceramidase deficiency in patients with Farber disease". Human Mutation. 17 (3): 199–209. doi:10.1002/humu.5. PMID 11241842.
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