CRABP1: Difference between revisions

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Latest revision as of 12:44, 9 January 2019

Cellular retinoic acid-binding protein 1 is a protein that in humans is encoded by the CRABP1 gene.^[1]^[2]

CRABP1 is assumed to play an important role in retinoic acid-mediated differentiation and proliferation processes. It is structurally similar to the cellular retinol-binding proteins, but binds only retinoic acid. CRABP1 is constitutively expressed and is believed to have different functions in the cell than the related CRABP2.^[2]

Function

File:Retinoid Transfer by CRABP1.png

Figure 1. An overview of retinoid transfer by CRABP. R = Retinoic acid, RAR = retinoic acid receptor, RXR = Retinoic X receptor, RRE = retinoid response element. CRABP binds to retinoic acid and transports it to the nucleus where binding with RAR or RXR homodimers or heterodimers further regulates RREs to regulate transcription events on DNA.^[3]

File:Cellular Effects of CRABP1.png

Figure 2. Retinoic acid (RA) is processed from vitamin A to bind to fatty acid binding protein (FABP5) along with CRABP to associate with the binding to DNA to mediate pathways. RA binds with CRABP to mediate further action with retinoic acid receptor (RAR) on DNA for pathway mediation as well.^[4]

File:Domains of CRABP1.png

Figure 3. Image of the domain locations for CRABP1. The nuclear localization signal (NLS) is at position 21-31 and the retinoic acid binding site (RBS) is at position 132-134.^[5]

CRABP1 binds to retinoid acid and helps to transport it into cells (Figure 1). Both CRABP1 and CRABP2 perform this activity. The retinoic acid molecule is then released and further bound to retinoic acid receptor (RAR) and the retinoid X receptor (RXR) as homodimers or heterodimers. This complex then further binds to retinoic acid response elements (RARE) on DNA that regulates transcription of retinoid acid dependent null genes.^[6] The domains for the nuclear localization and the retinoic acid binding are shown in Figure 3.

CRABP1 has been found to be involved in multiple cancer proliferation pathways. CRABP1 activates the extracellular signal-regulated kinase, ERK1 and ERK2 kinases, which are involved in the cell cycle. CRABP1 activity can thus extend the cell cycle, e.g. in embryonic and neural stem cells. Knockout mice without CRABP1 showed increased neural stem cell proliferation and thus hippocampus neurogenesis. Furthermore, learning and memory were improved in knockout mice, as measured by the Morris water maze test and an object recognition task.^[7]

CRABP1 is also involved in cancer cell apoptosis. trans-retinoic acid was considered a [null therapeutic target for cancer] as a ligand of CRABP1.^[8] It was observed that CRABP1 regulated extracellular signal regulated kinase (ERK1/2) which in turn activates the protein phosphatase 2A (PP2A) that induces apoptosis of cancer cells and lengthens the cell cycle of embryonic stem cells. PP2A activity promotes the stem cells renewal ability during the differentiation process. When CRABP1 was knocked down the apoptotic induction ability was also removed and allowed for cell proliferation. The re-expression of CRABP1 in CRABP1 null cells brought back the induced apoptotic activity. Thus CRABP1 may be used as a therapeutic target along with trans-retinoic acid for apoptotic activity within cancer cells.^[8] Figure 2 illustrates both pathways of retinoic acid binding to CRABP for cell proliferation and apoptotic activity.

References

↑ Flagiello D, Apiou F, Gibaud A, Poupon MF, Dutrillaux B, Malfoy B (Jun 1997). "Assignment of the genes for cellular retinoic acid binding protein 1 (CRABP1) and 2 (CRABP2) to human chromosome band 15q24 and 1q21.3, respectively, by in situ hybridization". Cytogenetics and Cell Genetics. 76 (1–2): 17–8. doi:10.1159/000134502. PMID 9154115.
↑ ^2.0 ^2.1 "Entrez Gene: CRABP1 cellular retinoic acid binding protein 1".
↑ Redrawn from Lee K (April 2017). "Retinol for all". The Regime.
↑ Redrawn from Michalik L, Wahli W (May 2007). "Guiding ligands to nuclear receptors". Cell. 129 (4): 649–51. doi:10.1016/j.cell.2007.05.001. PMID 17512397.
↑ Adapted from Universal protein resource accession number P29762 for "RABP1_HUMAN" at UniProt.
↑ Liu RZ, Garcia E, Glubrecht DD, Poon HY, Mackey JR, Godbout R (July 2015). "CRABP1 is associated with a poor prognosis in breast cancer: adding to the complexity of breast cancer cell response to retinoic acid". Molecular Cancer. 14: 129. doi:10.1186/s12943-015-0380-7. PMC 4491424. PMID 26142905.
↑ Lin YL, Persaud SD, Nhieu J, Wei LN (September 2017). "Cellular Retinoic Acid-Binding Protein 1 Modulates Stem Cell Proliferation to Affect Learning and Memory in Male Mice". Endocrinology. 158 (9): 3004–3014. doi:10.1210/en.2017-00353. PMC 5659671. PMID 28911165.
↑ ^8.0 ^8.1 Persaud SD, Park SW, Ishigami-Yuasa M, Koyano-Nakagawa N, Kagechika H, Wei LN (March 2016). "All trans-retinoic acid analogs promote cancer cell apoptosis through non-genomic Crabp1 mediating ERK1/2 phosphorylation". Scientific Reports. 6: 22396. doi:10.1038/srep22396. PMC 4776112. PMID 26935534.

External links

Human CRABP1 genome location and CRABP1 gene details page in the UCSC Genome Browser.
Human RBP5 genome location and RBP5 gene details page in the UCSC Genome Browser.

[pmid9154115-1] Flagiello D, Apiou F, Gibaud A, Poupon MF, Dutrillaux B, Malfoy B (Jun 1997). "Assignment of the genes for cellular retinoic acid binding protein 1 (CRABP1) and 2 (CRABP2) to human chromosome band 15q24 and 1q21.3, respectively, by in situ hybridization". Cytogenetics and Cell Genetics. 76 (1–2): 17–8. doi:10.1159/000134502. PMID 9154115.

[entrez-2] 2.0 ^2.1 "Entrez Gene: CRABP1 cellular retinoic acid binding protein 1".

[3] Redrawn from Lee K (April 2017). "Retinol for all". The Regime.

[Michalik_2007-4] Redrawn from Michalik L, Wahli W (May 2007). "Guiding ligands to nuclear receptors". Cell. 129 (4): 649–51. doi:10.1016/j.cell.2007.05.001. PMID 17512397.

[5] Adapted from Universal protein resource accession number P29762 for "RABP1_HUMAN" at UniProt.

[Liu_2015-6] Liu RZ, Garcia E, Glubrecht DD, Poon HY, Mackey JR, Godbout R (July 2015). "CRABP1 is associated with a poor prognosis in breast cancer: adding to the complexity of breast cancer cell response to retinoic acid". Molecular Cancer. 14: 129. doi:10.1186/s12943-015-0380-7. PMC 4491424. PMID 26142905.

[Lin_2017-7] Lin YL, Persaud SD, Nhieu J, Wei LN (September 2017). "Cellular Retinoic Acid-Binding Protein 1 Modulates Stem Cell Proliferation to Affect Learning and Memory in Male Mice". Endocrinology. 158 (9): 3004–3014. doi:10.1210/en.2017-00353. PMC 5659671. PMID 28911165.

[Persaud_2016-8] 8.0 ^8.1 Persaud SD, Park SW, Ishigami-Yuasa M, Koyano-Nakagawa N, Kagechika H, Wei LN (March 2016). "All trans-retinoic acid analogs promote cancer cell apoptosis through non-genomic Crabp1 mediating ERK1/2 phosphorylation". Scientific Reports. 6: 22396. doi:10.1038/srep22396. PMC 4776112. PMID 26935534.

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@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox_gene}}
-{{PBB_Controls
+'''Cellular retinoic acid-binding protein 1''' is a [[protein]] that in humans is encoded by the ''CRABP1'' [[gene]].<ref name="pmid9154115">{{cite journal | vauthors = Flagiello D, Apiou F, Gibaud A, Poupon MF, Dutrillaux B, Malfoy B | title = Assignment of the genes for cellular retinoic acid binding protein 1 (CRABP1) and 2 (CRABP2) to human chromosome band 15q24 and 1q21.3, respectively, by in situ hybridization | journal = Cytogenetics and Cell Genetics | volume = 76 | issue = 1–2 | pages = 17–8 | date = Jun 1997 | pmid = 9154115 | pmc =  | doi = 10.1159/000134502 }}</ref><ref name="entrez"/>
-| update_page = yes
-| require_manual_inspection = no
+CRABP1 is assumed to play an important role in [[retinoic acid]]-mediated differentiation and proliferation processes. It is structurally similar to the cellular retinol-binding proteins, but binds only retinoic acid. CRABP1 is constitutively expressed and is believed to have different functions in the cell than the related CRABP2.<ref name="entrez">{{cite web | title = Entrez Gene: CRABP1 cellular retinoic acid binding protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1381 }}</ref>
-| update_protein_box = yes
-| update_summary = yes
+== Function ==
-| update_citations = yes
+[[File:Retinoid Transfer by CRABP1.png|left|thumb|Figure 1. An overview of retinoid transfer by CRABP. R = Retinoic acid, RAR = retinoic acid receptor, RXR = Retinoic X receptor, RRE = retinoid response element. CRABP binds to retinoic acid and transports it to the nucleus where binding with RAR or RXR homodimers or heterodimers further regulates RREs to regulate transcription events on DNA.<ref>Redrawn from {{cite web | title = Retinol for all | date = April 2017 | work = The Regime | url = http://www.the-regimen.com/new-blog/2017/4/17/retinol-for-all | first = Kate | last = Lee | name-list-format = vanc }}</ref>]]
-}}
+[[File:Cellular Effects of CRABP1.png|left|thumb|Figure 2. Retinoic acid (RA) is processed from vitamin A to bind to fatty acid binding protein (FABP5) along with CRABP to associate with the binding to DNA to mediate pathways. RA binds with CRABP to mediate further action with retinoic acid receptor (RAR) on DNA for pathway mediation as well.<ref name = "Michalik_2007"/>]]
+[[File:Domains of CRABP1.png|left|thumb|Figure 3. Image of the domain locations for CRABP1. The nuclear localization signal (NLS)  is at position 21-31 and the retinoic acid binding site (RBS) is at position 132-134.<ref>Adapted from {{UniProt Full|P29762|RABP1_HUMAN}}</ref>]]
+CRABP1 binds to retinoid acid and helps to transport it into cells (Figure 1). Both CRABP1 and [[CRABP2]] perform this activity. The retinoic acid molecule is then released and further bound to [[Retinoic acid receptor|retinoic acid receptor (RAR)]] and the [[Retinoid X receptor|retinoid X receptor (RXR)]] as homodimers or heterodimers. This complex then further binds to retinoic acid response elements (RARE) on [[DNA]] that regulates transcription of retinoid acid dependent null genes.<ref name = "Liu_2015" /> The domains for the nuclear localization and the retinoic acid binding are shown in Figure 3.
+CRABP1 has been found to be involved in multiple cancer proliferation pathways. CRABP1 activates the [[Extracellular signal–regulated kinases|extracellular signal-regulated kinase]], ERK1 and ERK2 kinases, which are involved in the cell cycle. CRABP1 activity can thus extend the cell cycle, e.g. in embryonic and neural stem cells. Knockout mice without CRABP1 showed increased neural stem cell proliferation and thus hippocampus neurogenesis. Furthermore, learning and memory were improved in knockout mice, as measured by the [[Morris water navigation task|Morris water maze test]] and an object recognition task.<ref name = "Lin_2017" />
+CRABP1 is also involved in cancer cell [[apoptosis]]. [[Tretinoin|trans-retinoic acid]] was considered a [null therapeutic target for cancer]  as a ligand of CRABP1.<ref name = "Persaud_2016" /> It was observed that CRABP1 regulated [[Extracellular signal–regulated kinases|extracellular signal regulated kinase (ERK1/2)]] which in turn activates the [[Protein phosphatase 2|protein phosphatase 2A (PP2A)]] that induces [[apoptosis]] of cancer cells and lengthens the cell cycle of embryonic stem cells. PP2A activity promotes the stem cells renewal ability during the differentiation process. When CRABP1 was knocked down the apoptotic induction  ability was also removed and allowed for cell proliferation. The re-expression of CRABP1 in CRABP1 null cells brought back the induced apoptotic activity. Thus CRABP1 may be used as a therapeutic target along with [[Tretinoin|trans-retinoic acid]] for apoptotic activity within cancer cells.<ref name = "Persaud_2016" /> Figure 2 illustrates both pathways of [[retinoic acid]] binding to CRABP for cell proliferation and apoptotic activity.{{clear}}
+== References ==
+{{reflist|33em|refs=
+<ref name = "Lin_2017">{{cite journal | vauthors = Lin YL, Persaud SD, Nhieu J, Wei LN | title = Cellular Retinoic Acid-Binding Protein 1 Modulates Stem Cell Proliferation to Affect Learning and Memory in Male Mice | journal = Endocrinology | volume = 158 | issue = 9 | pages = 3004–3014 | date = September 2017 | pmid = 28911165 | doi = 10.1210/en.2017-00353 | pmc=5659671}}</ref>
+<ref name = "Liu_2015">{{cite journal | vauthors = Liu RZ, Garcia E, Glubrecht DD, Poon HY, Mackey JR, Godbout R | title = CRABP1 is associated with a poor prognosis in breast cancer: adding to the complexity of breast cancer cell response to retinoic acid | journal = Molecular Cancer | volume = 14 | pages = 129 | date = July 2015 | pmid = 26142905 | doi = 10.1186/s12943-015-0380-7 | pmc=4491424}}</ref>
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+<ref name = "Michalik_2007">Redrawn from {{cite journal | vauthors = Michalik L, Wahli W | title = Guiding ligands to nuclear receptors | journal = Cell | volume = 129 | issue = 4 | pages = 649–51 | date = May 2007 | pmid = 17512397 | doi = 10.1016/j.cell.2007.05.001 }}</ref>
-{{GNF_Protein_box
- | image = PBB_Protein_CRABP1_image.jpg
+<ref name = "Persaud_2016">{{cite journal | vauthors = Persaud SD, Park SW, Ishigami-Yuasa M, Koyano-Nakagawa N, Kagechika H, Wei LN | title = All trans-retinoic acid analogs promote cancer cell apoptosis through non-genomic Crabp1 mediating ERK1/2 phosphorylation | journal = Scientific Reports | volume = 6 | pages = 22396 | date = March 2016 | pmid = 26935534 | doi = 10.1038/srep22396 | pmc=4776112}}</ref>
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cbi.
- | PDB = {{PDB2|1cbi}}, {{PDB2|1cbr}}, {{PDB2|2cbr}}
- | Name = Cellular retinoic acid binding protein 1
- | HGNCid = 2338
- | Symbol = CRABP1
- | AltSymbols =; CRABP; CRABP-I; CRABPI; RBP5
- | OMIM = 180230
- | ECnumber =
- | Homologene = 3222
- | MGIid = 88490
- | GeneAtlas_image1 = PBB_GE_CRABP1_205350_at_tn.png
- | Function = {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0016918 |text = retinal binding}}
-  | Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
- | Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 1381
-    | Hs_Ensembl = ENSG00000166426
-    | Hs_RefseqProtein = NP_004369
-    | Hs_RefseqmRNA = NM_004378
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 15
-    | Hs_GenLoc_start = 76419744
-    | Hs_GenLoc_end = 76427620
-    | Hs_Uniprot = P29762
-    | Mm_EntrezGene = 12903
-    | Mm_Ensembl = ENSMUSG00000032291
-    | Mm_RefseqmRNA = NM_013496
-    | Mm_RefseqProtein = NP_038524
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 9
-    | Mm_GenLoc_start = 54562944
-    | Mm_GenLoc_end = 54571246
-    | Mm_Uniprot = Q6P071
-  }}
-}}
-'''Cellular retinoic acid binding protein 1''', also known as '''CRABP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CRABP1 cellular retinoic acid binding protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1381| accessdate = }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{PBB_Summary
-| section_title =
-| summary_text = A number of specific carrier proteins for members of the vitamin A family have been discovered. Cellular retinoic acid-binding protein is assumed to play an important role in retinoic acid-mediated differentiation and proliferation processes.  CRABP1 is structurally similar to the cellular retinol-binding proteins, but binds only retinoic acid. CRABP1 is constitutively expressed and is believed to have different functions in the cell than the related CRABP2.<ref name="entrez">{{cite web | title = Entrez Gene: CRABP1 cellular retinoic acid binding protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1381| accessdate = }}</ref>
 }}
-==References==
+== Further reading ==
-{{reflist|2}}
+{{refbegin|33em}}
-==Further reading==
+* {{cite journal | vauthors = Eller MS, Oleksiak MF, McQuaid TJ, McAfee SG, Gilchrest BA | title = The molecular cloning and expression of two CRABP cDNAs from human skin | journal = Experimental Cell Research | volume = 198 | issue = 2 | pages = 328–36 | date = February 1992 | pmid = 1309505 | doi = 10.1016/0014-4827(92)90387-N }}
-{{refbegin | 2}}
+* {{cite journal | vauthors = Aström A, Tavakkol A, Pettersson U, Cromie M, Elder JT, Voorhees JJ | title = Molecular cloning of two human cellular retinoic acid-binding proteins (CRABP). Retinoic acid-induced expression of CRABP-II but not CRABP-I in adult human skin in vivo and in skin fibroblasts in vitro | journal = The Journal of Biological Chemistry | volume = 266 | issue = 26 | pages = 17662–6 | date = September 1991 | pmid = 1654334 | doi =  }}
-{{PBB_Further_reading
+* {{cite journal | vauthors = Ong DE | title = Cellular retinoid-binding proteins | journal = Archives of Dermatology | volume = 123 | issue = 12 | pages = 1693–1695a | date = December 1987 | pmid = 2825608 | doi = 10.1001/archderm.123.12.1693 }}
-| citations =
+* {{cite journal | vauthors = Wang L, Li Y, Yan H | title = Structure-function relationships of cellular retinoic acid-binding proteins. Quantitative analysis of the ligand binding properties of the wild-type proteins and site-directed mutants | journal = The Journal of Biological Chemistry | volume = 272 | issue = 3 | pages = 1541–7 | date = January 1997 | pmid = 8999826 | doi = 10.1074/jbc.272.3.1541 }}
-*{{cite journal  | author=Eller MS, Oleksiak MF, McQuaid TJ, ''et al.'' |title=The molecular cloning and expression of two CRABP cDNAs from human skin. |journal=Exp. Cell Res. |volume=198 |issue= 2 |pages= 328-36 |year= 1992 |pmid= 1309505 |doi=  }}
+* {{cite journal | vauthors = Liu W, Hellman P, Li Q, Yu WR, Juhlin C, Nordlinder H, Rollman O, Akerström G, Törmä H, Melhus H | title = Biosynthesis and function of all-trans- and 9-cis-retinoic acid in parathyroid cells | journal = Biochemical and Biophysical Research Communications | volume = 229 | issue = 3 | pages = 922–9 | date = December 1996 | pmid = 9005841 | doi = 10.1006/bbrc.1996.1903 }}
-*{{cite journal  | author=Aström A, Tavakkol A, Pettersson U, ''et al.'' |title=Molecular cloning of two human cellular retinoic acid-binding proteins (CRABP). Retinoic acid-induced expression of CRABP-II but not CRABP-I in adult human skin in vivo and in skin fibroblasts in vitro. |journal=J. Biol. Chem. |volume=266 |issue= 26 |pages= 17662-6 |year= 1991 |pmid= 1654334 |doi=  }}
+* {{cite journal | vauthors = Kreutz M, Fritsche J, Andreesen R, Krause SW | title = Regulation of cellular retinoic acid binding protein (CRABP II) during human monocyte differentiation in vitro | journal = Biochemical and Biophysical Research Communications | volume = 248 | issue = 3 | pages = 830–4 | date = July 1998 | pmid = 9704013 | doi = 10.1006/bbrc.1998.9058 }}
-*{{cite journal  | author=Ong DE |title=Cellular retinoid-binding proteins. |journal=Archives of dermatology |volume=123 |issue= 12 |pages= 1693-1695a |year= 1987 |pmid= 2825608 |doi=  }}
+* {{cite journal | vauthors = Huang Y, de la Chapelle A, Pellegata NS | title = Hypermethylation, but not LOH, is associated with the low expression of MT1G and CRABP1 in papillary thyroid carcinoma | journal = International Journal of Cancer | volume = 104 | issue = 6 | pages = 735–44 | date = May 2003 | pmid = 12640681 | doi = 10.1002/ijc.11006 }}
-*{{cite journal  | author=Wang L, Li Y, Yan H |title=Structure-function relationships of cellular retinoic acid-binding proteins. Quantitative analysis of the ligand binding properties of the wild-type proteins and site-directed mutants. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1541-7 |year= 1997 |pmid= 8999826 |doi=  }}
+* {{cite journal | vauthors = Kim SK, Yoo JI, Cho BK, Hong SJ, Kim YK, Moon JA, Kim JH, Chung YN, Wang KC | title = Elevation of CRABP-I in the cerebrospinal fluid of patients with Moyamoya disease | journal = Stroke | volume = 34 | issue = 12 | pages = 2835–41 | date = December 2003 | pmid = 14605320 | doi = 10.1161/01.STR.0000100159.43123.D7 }}
-*{{cite journal  | author=Liu W, Hellman P, Li Q, ''et al.'' |title=Biosynthesis and function of all-trans- and 9-cis-retinoic acid in parathyroid cells. |journal=Biochem. Biophys. Res. Commun. |volume=229 |issue= 3 |pages= 922-9 |year= 1997 |pmid= 9005841 |doi= 10.1006/bbrc.1996.1903 }}
+* {{cite journal | vauthors = Blaese MA, Santo-Hoeltje L, Rodemann HP | title = CRABP I expression and the mediation of the sensitivity of human tumour cells to retinoic acid and irradiation | journal = International Journal of Radiation Biology | volume = 79 | issue = 12 | pages = 981–91 | date = December 2003 | pmid = 14713576 | doi = 10.1080/09553000310001632949 }}
-*{{cite journal  | author=Flagiello D, Apiou F, Gibaud A, ''et al.'' |title=Assignment of the genes for cellular retinoic acid binding protein 1 (CRABP1) and 2 (CRABP2) to human chromosome band 15q24 and 1q21.3, respectively, by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=76 |issue= 1-2 |pages= 17-8 |year= 1997 |pmid= 9154115 |doi=  }}
+* {{cite journal | vauthors = Won JY, Nam EC, Yoo SJ, Kwon HJ, Um SJ, Han HS, Kim SH, Byun Y, Kim SY | title = The effect of cellular retinoic acid binding protein-I expression on the CYP26-mediated catabolism of all-trans retinoic acid and cell proliferation in head and neck squamous cell carcinoma | journal = Metabolism | volume = 53 | issue = 8 | pages = 1007–12 | date = August 2004 | pmid = 15281009 | doi = 10.1016/j.metabol.2003.12.015 }}
-*{{cite journal  | author=Kreutz M, Fritsche J, Andreesen R, Krause SW |title=Regulation of cellular retinoic acid binding protein (CRABP II) during human monocyte differentiation in vitro. |journal=Biochem. Biophys. Res. Commun. |volume=248 |issue= 3 |pages= 830-4 |year= 1998 |pmid= 9704013 |doi= 10.1006/bbrc.1998.9058 }}
+* {{cite journal | vauthors = Ahn J, Chung KS, Kim DU, Won M, Kim L, Kim KS, Nam M, Choi SJ, Kim HC, Yoon M, Chae SK, Hoe KL | title = Systematic identification of hepatocellular proteins interacting with NS5A of the hepatitis C virus | journal = Journal of Biochemistry and Molecular Biology | volume = 37 | issue = 6 | pages = 741–8 | date = November 2004 | pmid = 15607035 | doi =  10.5483/bmbrep.2004.37.6.741}}
-*{{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 = Pfoertner S, Goelden U, Hansen W, Toepfer T, Geffers R, Ukena SN, von Knobloch R, Hofmann R, Buer J, Schrader AJ | title = Cellular retinoic acid binding protein I: expression and functional influence in renal cell carcinoma | journal = Tumour Biology | volume = 26 | issue = 6 | pages = 313–23 | year = 2005 | pmid = 16254461 | doi = 10.1159/000089262 }}
-*{{cite journal  | author=Huang Y, de la Chapelle A, Pellegata NS |title=Hypermethylation, but not LOH, is associated with the low expression of MT1G and CRABP1 in papillary thyroid carcinoma. |journal=Int. J. Cancer |volume=104 |issue= 6 |pages= 735-44 |year= 2003 |pmid= 12640681 |doi= 10.1002/ijc.11006 }}
+* {{cite journal | vauthors = Lind GE, Kleivi K, Meling GI, Teixeira MR, Thiis-Evensen E, Rognum TO, Lothe RA | title = ADAMTS1, CRABP1, and NR3C1 identified as epigenetically deregulated genes in colorectal tumorigenesis | journal = Cellular Oncology | volume = 28 | issue = 5–6 | pages = 259–72 | year = 2007 | pmid = 17167179 | doi =  }}
-*{{cite journal  | author=Kim SK, Yoo JI, Cho BK, ''et al.'' |title=Elevation of CRABP-I in the cerebrospinal fluid of patients with Moyamoya disease. |journal=Stroke |volume=34 |issue= 12 |pages= 2835-41 |year= 2004 |pmid= 14605320 |doi= 10.1161/01.STR.0000100159.43123.D7 }}
+* {{cite journal | vauthors = Tanaka K, Imoto I, Inoue J, Kozaki K, Tsuda H, Shimada Y, Aiko S, Yoshizumi Y, Iwai T, Kawano T, Inazawa J | title = Frequent methylation-associated silencing of a candidate tumor-suppressor, CRABP1, in esophageal squamous-cell carcinoma | journal = Oncogene | volume = 26 | issue = 44 | pages = 6456–68 | date = September 2007 | pmid = 17438526 | doi = 10.1038/sj.onc.1210459 }}
-*{{cite journal  | author=Blaese MA, Santo-Hoeltje L, Rodemann HP |title=CRABP I expression and the mediation of the sensitivity of human tumour cells to retinoic acid and irradiation. |journal=Int. J. Radiat. Biol. |volume=79 |issue= 12 |pages= 981-91 |year= 2004 |pmid= 14713576 |doi= 10.1080/09553000310001632949 }}
+* {{cite journal | vauthors = Wu Q, Lothe RA, Ahlquist T, Silins I, Tropé CG, Micci F, Nesland JM, Suo Z, Lind GE | title = DNA methylation profiling of ovarian carcinomas and their in vitro models identifies HOXA9, HOXB5, SCGB3A1, and CRABP1 as novel targets | journal = Molecular Cancer | volume = 6 | issue =  | pages = 45 | date = July 2007 | pmid = 17623056 | pmc = 1964763 | doi = 10.1186/1476-4598-6-45 }}
-*{{cite journal  | author=Won JY, Nam EC, Yoo SJ, ''et al.'' |title=The effect of cellular retinoic acid binding protein-I expression on the CYP26-mediated catabolism of all-trans retinoic acid and cell proliferation in head and neck squamous cell carcinoma. |journal=Metab. Clin. Exp. |volume=53 |issue= 8 |pages= 1007-12 |year= 2004 |pmid= 15281009 |doi=  }}
-*{{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=Ahn J, Chung KS, Kim DU, ''et al.'' |title=Systematic identification of hepatocellular proteins interacting with NS5A of the hepatitis C virus. |journal=J. Biochem. Mol. Biol. |volume=37 |issue= 6 |pages= 741-8 |year= 2005 |pmid= 15607035 |doi=  }}
-*{{cite journal  | author=Pfoertner S, Goelden U, Hansen W, ''et al.'' |title=Cellular retinoic acid binding protein I: expression and functional influence in renal cell carcinoma. |journal=Tumour Biol. |volume=26 |issue= 6 |pages= 313-23 |year= 2005 |pmid= 16254461 |doi= 10.1159/000089262 }}
-*{{cite journal  | author=Lind GE, Kleivi K, Meling GI, ''et al.'' |title=ADAMTS1, CRABP1, and NR3C1 identified as epigenetically deregulated genes in colorectal tumorigenesis. |journal=Cell. Oncol. |volume=28 |issue= 5-6 |pages= 259-72 |year= 2007 |pmid= 17167179 |doi=  }}
-*{{cite journal  | author=Tanaka K, Imoto I, Inoue J, ''et al.'' |title=Frequent methylation-associated silencing of a candidate tumor-suppressor, CRABP1, in esophageal squamous-cell carcinoma. |journal=Oncogene |volume=26 |issue= 44 |pages= 6456-68 |year= 2007 |pmid= 17438526 |doi= 10.1038/sj.onc.1210459 }}
-*{{cite journal  | author=Wu Q, Lothe RA, Ahlquist T, ''et al.'' |title=DNA methylation profiling of ovarian carcinomas and their in vitro models identifies HOXA9, HOXB5, SCGB3A1, and CRABP1 as novel targets. |journal=Mol. Cancer |volume=6 |issue=  |pages= 45 |year= 2007 |pmid= 17623056 |doi= 10.1186/1476-4598-6-45 }}
-}}
 {{refend}}
-{{protein-stub}}
+== External links ==
-{{WikiDoc Sources}}
+* {{UCSC gene info|CRABP1}}
+* {{UCSC gene info|RBP5}}
+{{PDB Gallery|geneid=1381}}
+[[Category:Lipocalins]]

CRABP1: Difference between revisions

Latest revision as of 12:44, 9 January 2019

Contents

Function

References

Further reading

External links

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