Involucrin: Difference between revisions

Jump to navigation Jump to search
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
m (Bot: HTTP→HTTPS)
 
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
{{Infobox protein family
| update_page = yes
| Symbol = Involucrin_N
| require_manual_inspection = no
| Name = Involucrin of squamous epithelia N-terminus
| update_protein_box = yes
| image =
| update_summary = yes
| width =
| update_citations = yes
| caption =
| Pfam = PF10583
| Pfam_clan = 
| InterPro = IPR019571
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =  
| OPM family =  
| OPM protein =  
| CAZy =  
| CDD =  
}}
}}
{{Infobox protein family
| Symbol = Involucrin
| Name = Involucrin repeat
| image =
| width =
| caption =
| Pfam = PF00904
| Pfam_clan = 
| InterPro = IPR000354
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1eu0
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
{{Infobox protein family
| Symbol = Involucrin2
| Name = Involucrin repeat
| image =
| width =
| caption =
| Pfam = PF06994
| Pfam_clan = 
| InterPro = IPR009733
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
'''Involucrin''' is a [[protein]] component of human skin and in humans is encoded by the ''IVL'' [[gene]].<ref name="pmid2873896">{{cite journal | vauthors = Eckert RL, Green H | title = Structure and evolution of the human involucrin gene | journal = Cell | volume = 46 | issue = 4 | pages = 583–9 | date = August 1986 | pmid = 2873896 | doi = 10.1016/0092-8674(86)90884-6 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: IVL involucrin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3713| accessdate = }}</ref> In binding the protein [[loricrin]], involucrin contributes to the formation of a cell envelope that protects [[corneocyte]]s in the skin.
== Gene ==
This gene is mapped to 1q21, among [[S100A10|calpactin]] I light chain, [[TCHH|trichohyalin]], [[profillaggrin]], [[loricrin]], and [[calcyclin]].<ref name="entrez"/>
== Function ==
Involucrin is a highly reactive, soluble, [[transglutaminase]] [[Enzyme substrate|substrate]] [[protein]] present in [[keratinocytes]] of [[Epidermis (skin)|epidermis]] and other [[stratified squamous epithelia]].<ref name="pmid1359382">{{cite journal | vauthors = Green H, Djian P | title = Consecutive actions of different gene-altering mechanisms in the evolution of involucrin | journal = Molecular Biology and Evolution | volume = 9 | issue = 6 | pages = 977–1017 | date = November 1992 | pmid = 1359382 | url = http://mbe.oxfordjournals.org/cgi/pmidlookup?view=long&pmid=1359382 }}</ref><ref name="pmid8277848">{{cite journal | vauthors = Djian P, Phillips M, Easley K, Huang E, Simon M, Rice RH, Green H | title = The involucrin genes of the mouse and the rat: study of their shared repeats | journal = Molecular Biology and Evolution | volume = 10 | issue = 6 | pages = 1136–49 | date = November 1993 | pmid = 8277848 | url = http://mbe.oxfordjournals.org/cgi/pmidlookup?view=long&pmid=8277848 }}</ref> It first appears in the [[Cell (biology)|cell]] [[cytosol]], but ultimately becomes cross-linked to [[membrane proteins]] by transglutaminase thus helping in the formation of an insoluble envelope beneath the [[Cell membrane|plasma membrane]] functioning as a [[glutamyl]] donor during assembly of the cornified envelope.<ref name="pmid8098344">{{cite journal | vauthors = Eckert RL, Yaffe MB, Crish JF, Murthy S, Rorke EA, Welter JF | title = Involucrin--structure and role in envelope assembly | journal = The Journal of Investigative Dermatology | volume = 100 | issue = 5 | pages = 613–7 | date = May 1993 | pmid = 8098344 | doi = 10.1111/1523-1747.ep12472288 }}</ref>
Involucrin is synthesised in the [[stratum spinosum]] and cross linked in the [[stratum granulosum]] by the [[transglutaminase]] enzyme that makes it highly stable. Thus it provides structural support to the cell, thereby allowing the cell to resist invasion by micro-organisms.{{citation needed|date=January 2017}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
[[Apigenin]], a plant-derived [[flavanoid]] that has significant promise as a [[skin cancer]] [[chemopreventive]] agent, has been found to regulate normal [[Homo sapiens|human]] keratinocyte [[differentiation (cellular)|differentiation]] by suppressing involucrin, and this is associated with reduced cell proliferation without [[apoptosis]].<ref name="pmid16982614">{{cite journal | vauthors = Balasubramanian S, Zhu L, Eckert RL | title = Apigenin inhibition of involucrin gene expression is associated with a specific reduction in phosphorylation of protein kinase Cdelta Tyr311 | journal = The Journal of Biological Chemistry | volume = 281 | issue = 47 | pages = 36162–72 | date = November 2006 | pmid = 16982614 | doi = 10.1074/jbc.M605368200 }}</ref>
{{GNF_Protein_box
 
| image =
== Clinical significance ==
| image_source =
As one of the precursor proteins of the cornified cell envelope, involucrin is markedly increased in inflammatory skin diseases such as psoriasis<ref>{{cite journal | vauthors = Takahashi H, Hashimoto Y, Ishida-Yamamoto A, Iizuka H | title = Roxithromycin suppresses involucrin expression by modulation of activator protein-1 and nuclear factor-kappaB activities of keratinocytes | journal = Journal of Dermatological Science | volume = 39 | issue = 3 | pages = 175–82 | date = September 2005 | pmid = 16140218 | doi = 10.1016/j.jdermsci.2005.03.006 }}</ref>
| PDB =  
 
| Name = Involucrin
[[Lamellar ichthyosis]] involves a decrease in expression of involucrin. This decrease could contribute to the altered desquamation process seen in the disease, since the clinical improvement associated with retinoid treatment is accompanied by increased expression of involucrin.<ref>{{cite journal | vauthors = Peña-Penabad C, de Unamuno P, García Silva J, Ludeña MD, González Sarmiento R, Pérez-Arellano JL | title = Altered expression of immunoreactive involucrin in lamellar ichthyosis | journal = European Journal of Dermatology | volume = 9 | issue = 3 | pages = 197–201 | year = 1999 | pmid = 10210784 | url = http://www.john-libbey-eurotext.fr/medline.md?issn=1167-1122&vol=9&iss=3&page=197 }}</ref>
| HGNCid = 6187
 
| Symbol = IVL
==Structure==
| AltSymbols =;
 
| OMIM = 147360
Involucrin consists of a [[conserved sequence|conserved]] [[N-terminal]] region of about 75 [[amino acid]] residues followed by two extremely variable length segments that contain [[glutamine]]-rich [[tandem repeats]]. The [[glutamine]] residues in the tandem repeats are the [[Substrate (biochemistry)|substrate]] for the transglutaminase in the cross-linking reaction. The total size of the protein varies from 285 residues (in [[dog]]) to 835 residues (in [[orangutan]]).{{citation needed|date=January 2017}}
| ECnumber =
| Homologene = 86915
| MGIid = 
| GeneAtlas_image1 = PBB_GE_IVL_214599_at_tn.png
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}}
| Component = {{GNF_GO|id=GO:0001533 |text = cornified envelope}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0010224 |text = response to UV-B}} {{GNF_GO|id=GO:0018149 |text = peptide cross-linking}} {{GNF_GO|id=GO:0018153 |text = isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine}} {{GNF_GO|id=GO:0030216 |text = keratinocyte differentiation}} {{GNF_GO|id=GO:0031424 |text = keratinization}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3713
    | Hs_Ensembl = ENSG00000163207
    | Hs_RefseqProtein = XP_001130659
    | Hs_RefseqmRNA = XM_001130659
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 151147645
    | Hs_GenLoc_end = 151150986
    | Hs_Uniprot = P07476
    | Mm_EntrezGene =
    | Mm_Ensembl =
    | Mm_RefseqmRNA =
    | Mm_RefseqProtein =
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr =
    | Mm_GenLoc_start =
    | Mm_GenLoc_end =
    | Mm_Uniprot =
  }}
}}
'''Involucrin''', also known as '''IVL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IVL involucrin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3713| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== References ==
{{PBB_Summary
{{reflist}}
| section_title =  
| summary_text = Involucrin, a component of the keratinocyte crosslinked envelope, is found in the cytoplasm and crosslinked to membrane proteins by transglutaminase.  This gene is mapped to 1q21, among calpactin I light chain, trichohyalin, profillaggrin, loricrin, and calcyclin.<ref name="entrez">{{cite web | title = Entrez Gene: IVL involucrin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3713| accessdate = }}</ref>
}}


==References==
== Further reading ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Eckert RL, Crish JF, Efimova T, Dashti SR, Deucher A, Bone F, Adhikary G, Huang G, Gopalakrishnan R, Balasubramanian S | title = Regulation of involucrin gene expression | journal = The Journal of Investigative Dermatology | volume = 123 | issue = 1 | pages = 13–22 | date = July 2004 | pmid = 15191537 | doi = 10.1111/j.0022-202X.2004.22723.x }}
| citations =
* {{cite journal | vauthors = Rice RH, Green H | title = Presence in human epidermal cells of a soluble protein precursor of the cross-linked envelope: activation of the cross-linking by calcium ions | journal = Cell | volume = 18 | issue = 3 | pages = 681–94 | date = November 1979 | pmid = 42494 | doi = 10.1016/0092-8674(79)90123-5 }}
*{{cite journal | author=Eckert RL, Crish JF, Efimova T, ''et al.'' |title=Regulation of involucrin gene expression. |journal=J. Invest. Dermatol. |volume=123 |issue= 1 |pages= 13-22 |year= 2004 |pmid= 15191537 |doi= 10.1111/j.0022-202X.2004.22723.x }}
* {{cite journal | vauthors = Yaffe MB, Beegen H, Eckert RL | title = Biophysical characterization of involucrin reveals a molecule ideally suited to function as an intermolecular cross-bridge of the keratinocyte cornified envelope | journal = The Journal of Biological Chemistry | volume = 267 | issue = 17 | pages = 12233–8 | date = June 1992 | pmid = 1601889 | url = http://www.jbc.org/cgi/pmidlookup?view=long&pmid=1601889 }}
*{{cite journal | author=Rice RH, Green H |title=Presence in human epidermal cells of a soluble protein precursor of the cross-linked envelope: activation of the cross-linking by calcium ions. |journal=Cell |volume=18 |issue= 3 |pages= 681-94 |year= 1980 |pmid= 42494 |doi= }}
* {{cite journal | vauthors = Simon M, Green H | title = The glutamine residues reactive in transglutaminase-catalyzed cross-linking of involucrin | journal = The Journal of Biological Chemistry | volume = 263 | issue = 34 | pages = 18093–8 | date = December 1988 | pmid = 2461365 | url = http://www.jbc.org/cgi/pmidlookup?view=long&pmid=2461365 }}
*{{cite journal | author=Yaffe MB, Beegen H, Eckert RL |title=Biophysical characterization of involucrin reveals a molecule ideally suited to function as an intermolecular cross-bridge of the keratinocyte cornified envelope. |journal=J. Biol. Chem. |volume=267 |issue= 17 |pages= 12233-8 |year= 1992 |pmid= 1601889 |doi= }}
* {{cite journal | vauthors = Heller M, Flemington E, Kieff E, Deininger P | title = Repeat arrays in cellular DNA related to the Epstein-Barr virus IR3 repeat | journal = Molecular and Cellular Biology | volume = 5 | issue = 3 | pages = 457–65 | date = March 1985 | pmid = 2985954 | pmc = 366737 | url = http://mcb.asm.org/cgi/pmidlookup?view=long&pmid=2985954 | doi=10.1128/mcb.5.3.457}}
*{{cite journal | author=Simon M, Green H |title=The glutamine residues reactive in transglutaminase-catalyzed cross-linking of involucrin. |journal=J. Biol. Chem. |volume=263 |issue= 34 |pages= 18093-8 |year= 1989 |pmid= 2461365 |doi= }}
* {{cite journal | vauthors = Welter JF, Crish JF, Agarwal C, Eckert RL | title = Fos-related antigen (Fra-1), junB, and junD activate human involucrin promoter transcription by binding to proximal and distal AP1 sites to mediate phorbol ester effects on promoter activity | journal = The Journal of Biological Chemistry | volume = 270 | issue = 21 | pages = 12614–22 | date = May 1995 | pmid = 7759510 | doi = 10.1074/jbc.270.21.12614 }}
*{{cite journal | author=Eckert RL, Green H |title=Structure and evolution of the human involucrin gene. |journal=Cell |volume=46 |issue= 4 |pages= 583-9 |year= 1986 |pmid= 2873896 |doi= }}
* {{cite journal | vauthors = Volz A, Korge BP, Compton JG, Ziegler A, Steinert PM, Mischke D | title = Physical mapping of a functional cluster of epidermal differentiation genes on chromosome 1q21 | journal = Genomics | volume = 18 | issue = 1 | pages = 92–9 | date = October 1993 | pmid = 8276421 | doi = 10.1006/geno.1993.1430 }}
*{{cite journal | author=Heller M, Flemington E, Kieff E, Deininger P |title=Repeat arrays in cellular DNA related to the Epstein-Barr virus IR3 repeat. |journal=Mol. Cell. Biol. |volume=5 |issue= 3 |pages= 457-65 |year= 1985 |pmid= 2985954 |doi= }}
* {{cite journal | vauthors = Takahashi H, Iizuka H | title = Analysis of the 5'-upstream promoter region of human involucrin gene: activation by 12-O-tetradecanoylphorbol-13-acetate | journal = The Journal of Investigative Dermatology | volume = 100 | issue = 1 | pages = 10–5 | date = January 1993 | pmid = 8380829 | doi = 10.1111/1523-1747.ep12349867 }}
*{{cite journal | author=Welter JF, Crish JF, Agarwal C, Eckert RL |title=Fos-related antigen (Fra-1), junB, and junD activate human involucrin promoter transcription by binding to proximal and distal AP1 sites to mediate phorbol ester effects on promoter activity. |journal=J. Biol. Chem. |volume=270 |issue= 21 |pages= 12614-22 |year= 1995 |pmid= 7759510 |doi= }}
* {{cite journal | vauthors = Lopez-Bayghen E, Vega A, Cadena A, Granados SE, Jave LF, Gariglio P, Alvarez-Salas LM | title = Transcriptional analysis of the 5'-noncoding region of the human involucrin gene | journal = The Journal of Biological Chemistry | volume = 271 | issue = 1 | pages = 512–20 | date = January 1996 | pmid = 8550612 | doi = 10.1074/jbc.271.1.512 }}
*{{cite journal  | author=Volz A, Korge BP, Compton JG, ''et al.'' |title=Physical mapping of a functional cluster of epidermal differentiation genes on chromosome 1q21. |journal=Genomics |volume=18 |issue= 1 |pages= 92-9 |year= 1994 |pmid= 8276421 |doi= 10.1006/geno.1993.1430 }}
* {{cite journal | vauthors = Takahashi H, Kobayashi H, Matsuo S, Iizuka H | title = Repression of involucrin gene expression by transcriptional enhancer factor 1 (TEF-1) | journal = Archives of Dermatological Research | volume = 287 | issue = 8 | pages = 740–6 | year = 1995 | pmid = 8554386 | doi = 10.1007/BF01105799 }}
*{{cite journal | author=Takahashi H, Iizuka H |title=Analysis of the 5'-upstream promoter region of human involucrin gene: activation by 12-O-tetradecanoylphorbol-13-acetate. |journal=J. Invest. Dermatol. |volume=100 |issue= 1 |pages= 10-5 |year= 1993 |pmid= 8380829 |doi= }}
* {{cite journal | vauthors = Steinert PM, Marekov LN | title = Direct evidence that involucrin is a major early isopeptide cross-linked component of the keratinocyte cornified cell envelope | journal = The Journal of Biological Chemistry | volume = 272 | issue = 3 | pages = 2021–30 | date = January 1997 | pmid = 8999895 | doi = 10.1074/jbc.272.3.2021 }}
*{{cite journal | author=Lopez-Bayghen E, Vega A, Cadena A, ''et al.'' |title=Transcriptional analysis of the 5'-noncoding region of the human involucrin gene. |journal=J. Biol. Chem. |volume=271 |issue= 1 |pages= 512-20 |year= 1996 |pmid= 8550612 |doi= }}
* {{cite journal | vauthors = Robinson NA, Lapic S, Welter JF, Eckert RL | title = S100A11, S100A10, annexin I, desmosomal proteins, small proline-rich proteins, plasminogen activator inhibitor-2, and involucrin are components of the cornified envelope of cultured human epidermal keratinocytes | journal = The Journal of Biological Chemistry | volume = 272 | issue = 18 | pages = 12035–46 | date = May 1997 | pmid = 9115270 | doi = 10.1074/jbc.272.18.12035 }}
*{{cite journal | author=Takahashi H, Kobayashi H, Matsuo S, Iizuka H |title=Repression of involucrin gene expression by transcriptional enhancer factor 1 (TEF-1). |journal=Arch. Dermatol. Res. |volume=287 |issue= 8 |pages= 740-6 |year= 1996 |pmid= 8554386 |doi= }}
* {{cite journal | vauthors = Ng DC, Su MJ, Kim R, Bikle DD | title = Regulation of involucrin gene expression by calcium in normal human keratinocytes | journal = Frontiers in Bioscience | volume = 1 | pages = a16-24 | date = January 1996 | pmid = 9159190 | doi = 10.2741/A101 }}
*{{cite journal | author=Steinert PM, Marekov LN |title=Direct evidence that involucrin is a major early isopeptide cross-linked component of the keratinocyte cornified cell envelope. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 2021-30 |year= 1997 |pmid= 8999895 |doi= }}
* {{cite journal | vauthors = Banks EB, Crish JF, Welter JF, Eckert RL | title = Characterization of human involucrin promoter distal regulatory region transcriptional activator elements-a role for Sp1 and AP1 binding sites | journal = The Biochemical Journal | volume = 331 | issue = 1 | pages = 61–8 | date = April 1998 | pmid = 9512462 | pmc = 1219321 | url = http://www.biochemj.org/cgi/pmidlookup?view=long&pmid=9512462 | doi=10.1042/bj3310061}}
*{{cite journal | author=Robinson NA, Lapic S, Welter JF, Eckert RL |title=S100A11, S100A10, annexin I, desmosomal proteins, small proline-rich proteins, plasminogen activator inhibitor-2, and involucrin are components of the cornified envelope of cultured human epidermal keratinocytes. |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 12035-46 |year= 1997 |pmid= 9115270 |doi= }}
* {{cite journal | vauthors = Marekov LN, Steinert PM | title = Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope | journal = The Journal of Biological Chemistry | volume = 273 | issue = 28 | pages = 17763–70 | date = July 1998 | pmid = 9651377 | doi = 10.1074/jbc.273.28.17763 }}
*{{cite journal  | author=Ng DC, Su MJ, Kim R, Bikle DD |title=Regulation of involucrin gene expression by calcium in normal human keratinocytes. |journal=Front. Biosci. |volume=1 |issue= |pages= a16-24 |year= 2004 |pmid= 9159190 |doi= }}
* {{cite journal | vauthors = Crish JF, Zaim TM, Eckert RL | title = The distal regulatory region of the human involucrin promoter is required for expression in epidermis | journal = The Journal of Biological Chemistry | volume = 273 | issue = 46 | pages = 30460–5 | date = November 1998 | pmid = 9804813 | doi = 10.1074/jbc.273.46.30460 }}
*{{cite journal | author=Banks EB, Crish JF, Welter JF, Eckert RL |title=Characterization of human involucrin promoter distal regulatory region transcriptional activator elements-a role for Sp1 and AP1 binding sites. |journal=Biochem. J. |volume=331 ( Pt 1) |issue= |pages= 61-8 |year= 1998 |pmid= 9512462 |doi= }}
* {{cite journal | vauthors = Lee CH, Marekov LN, Kim S, Brahim JS, Park MH, Steinert PM | title = Small proline-rich protein 1 is the major component of the cell envelope of normal human oral keratinocytes | journal = FEBS Letters | volume = 477 | issue = 3 | pages = 268–72 | date = July 2000 | pmid = 10908733 | doi = 10.1016/S0014-5793(00)01806-8 }}
*{{cite journal | author=Marekov LN, Steinert PM |title=Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope. |journal=J. Biol. Chem. |volume=273 |issue= 28 |pages= 17763-70 |year= 1998 |pmid= 9651377 |doi= }}
* {{cite journal | vauthors = Candi E, Oddi S, Terrinoni A, Paradisi A, Ranalli M, Finazzi-Agró A, Melino G | title = Transglutaminase 5 cross-links loricrin, involucrin, and small proline-rich proteins in vitro | journal = The Journal of Biological Chemistry | volume = 276 | issue = 37 | pages = 35014–23 | date = September 2001 | pmid = 11443109 | doi = 10.1074/jbc.M010157200 }}
*{{cite journal | author=Crish JF, Zaim TM, Eckert RL |title=The distal regulatory region of the human involucrin promoter is required for expression in epidermis. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30460-5 |year= 1998 |pmid= 9804813 |doi= }}
* {{cite journal | vauthors = Crish JF, Bone F, Banks EB, Eckert RL | title = The human involucrin gene contains spatially distinct regulatory elements that regulate expression during early versus late epidermal differentiation | journal = Oncogene | volume = 21 | issue = 5 | pages = 738–47 | date = January 2002 | pmid = 11850802 | doi = 10.1038/sj.onc.1205038 }}
*{{cite journal | author=Lee CH, Marekov LN, Kim S, ''et al.'' |title=Small proline-rich protein 1 is the major component of the cell envelope of normal human oral keratinocytes. |journal=FEBS Lett. |volume=477 |issue= 3 |pages= 268-72 |year= 2000 |pmid= 10908733 |doi=  }}
*{{cite journal  | author=Candi E, Oddi S, Terrinoni A, ''et al.'' |title=Transglutaminase 5 cross-links loricrin, involucrin, and small proline-rich proteins in vitro. |journal=J. Biol. Chem. |volume=276 |issue= 37 |pages= 35014-23 |year= 2001 |pmid= 11443109 |doi= 10.1074/jbc.M010157200 }}
*{{cite journal | author=Crish JF, Bone F, Banks EB, Eckert RL |title=The human involucrin gene contains spatially distinct regulatory elements that regulate expression during early versus late epidermal differentiation. |journal=Oncogene |volume=21 |issue= 5 |pages= 738-47 |year= 2002 |pmid= 11850802 |doi= 10.1038/sj.onc.1205038 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{InterPro content|IPR019571}}
{{WikiDoc Sources}}
 
[[Category:Protein domains]]

Latest revision as of 06:55, 1 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human
Involucrin of squamous epithelia N-terminus
Identifiers
SymbolInvolucrin_N
PfamPF10583
InterProIPR019571
Involucrin repeat
Identifiers
SymbolInvolucrin
PfamPF00904
InterProIPR000354
SCOP1eu0
SUPERFAMILY1eu0
Involucrin repeat
Identifiers
SymbolInvolucrin2
PfamPF06994
InterProIPR009733

Involucrin is a protein component of human skin and in humans is encoded by the IVL gene.[1][2] In binding the protein loricrin, involucrin contributes to the formation of a cell envelope that protects corneocytes in the skin.

Gene

This gene is mapped to 1q21, among calpactin I light chain, trichohyalin, profillaggrin, loricrin, and calcyclin.[2]

Function

Involucrin is a highly reactive, soluble, transglutaminase substrate protein present in keratinocytes of epidermis and other stratified squamous epithelia.[3][4] It first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase thus helping in the formation of an insoluble envelope beneath the plasma membrane functioning as a glutamyl donor during assembly of the cornified envelope.[5]

Involucrin is synthesised in the stratum spinosum and cross linked in the stratum granulosum by the transglutaminase enzyme that makes it highly stable. Thus it provides structural support to the cell, thereby allowing the cell to resist invasion by micro-organisms.[citation needed]

Apigenin, a plant-derived flavanoid that has significant promise as a skin cancer chemopreventive agent, has been found to regulate normal human keratinocyte differentiation by suppressing involucrin, and this is associated with reduced cell proliferation without apoptosis.[6]

Clinical significance

As one of the precursor proteins of the cornified cell envelope, involucrin is markedly increased in inflammatory skin diseases such as psoriasis[7]

Lamellar ichthyosis involves a decrease in expression of involucrin. This decrease could contribute to the altered desquamation process seen in the disease, since the clinical improvement associated with retinoid treatment is accompanied by increased expression of involucrin.[8]

Structure

Involucrin consists of a conserved N-terminal region of about 75 amino acid residues followed by two extremely variable length segments that contain glutamine-rich tandem repeats. The glutamine residues in the tandem repeats are the substrate for the transglutaminase in the cross-linking reaction. The total size of the protein varies from 285 residues (in dog) to 835 residues (in orangutan).[citation needed]

References

  1. Eckert RL, Green H (August 1986). "Structure and evolution of the human involucrin gene". Cell. 46 (4): 583–9. doi:10.1016/0092-8674(86)90884-6. PMID 2873896.
  2. 2.0 2.1 "Entrez Gene: IVL involucrin".
  3. Green H, Djian P (November 1992). "Consecutive actions of different gene-altering mechanisms in the evolution of involucrin". Molecular Biology and Evolution. 9 (6): 977–1017. PMID 1359382.
  4. Djian P, Phillips M, Easley K, Huang E, Simon M, Rice RH, Green H (November 1993). "The involucrin genes of the mouse and the rat: study of their shared repeats". Molecular Biology and Evolution. 10 (6): 1136–49. PMID 8277848.
  5. Eckert RL, Yaffe MB, Crish JF, Murthy S, Rorke EA, Welter JF (May 1993). "Involucrin--structure and role in envelope assembly". The Journal of Investigative Dermatology. 100 (5): 613–7. doi:10.1111/1523-1747.ep12472288. PMID 8098344.
  6. Balasubramanian S, Zhu L, Eckert RL (November 2006). "Apigenin inhibition of involucrin gene expression is associated with a specific reduction in phosphorylation of protein kinase Cdelta Tyr311". The Journal of Biological Chemistry. 281 (47): 36162–72. doi:10.1074/jbc.M605368200. PMID 16982614.
  7. Takahashi H, Hashimoto Y, Ishida-Yamamoto A, Iizuka H (September 2005). "Roxithromycin suppresses involucrin expression by modulation of activator protein-1 and nuclear factor-kappaB activities of keratinocytes". Journal of Dermatological Science. 39 (3): 175–82. doi:10.1016/j.jdermsci.2005.03.006. PMID 16140218.
  8. Peña-Penabad C, de Unamuno P, García Silva J, Ludeña MD, González Sarmiento R, Pérez-Arellano JL (1999). "Altered expression of immunoreactive involucrin in lamellar ichthyosis". European Journal of Dermatology. 9 (3): 197–201. PMID 10210784.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR019571