Wikipedia

Involucrin

Involucrin is a protein component of human skin and in humans is encoded by the IVL gene.[5][6] In binding the protein loricrin, involucrin contributes to the formation of a cell envelope that protects corneocytes in the skin.

IVL
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesIVL, involucrin
External IDsOMIM: 147360; MGI: 96626; HomoloGene: 136793; GeneCards: IVL; OMA:IVL - orthologs
Orthologs
SpeciesHumanMouse
Entrez

3713

16447

Ensembl

ENSG00000163207

ENSMUSG00000049128

UniProt

P07476

P48997

RefSeq (mRNA)

NM_005547

NM_008412

RefSeq (protein)

NP_005538

NP_032438

Location (UCSC)Chr 1: 152.91 – 152.91 MbChr 3: 92.48 – 92.48 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
Involucrin of squamous epithelia N-terminus
Identifiers
SymbolInvolucrin_N
PfamPF10583
InterProIPR019571
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Involucrin repeat
Identifiers
SymbolInvolucrin
PfamPF00904
InterProIPR000354
SCOP21eu0 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Involucrin repeat
Identifiers
SymbolInvolucrin2
PfamPF06994
InterProIPR009733
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Gene

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This gene is mapped to 1q21, among calpactin I light chain, trichohyalin, profillaggrin, loricrin, and calcyclin.[6]

Function

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Involucrin is a highly reactive, soluble, transglutaminase substrate protein present in keratinocytes of epidermis and other stratified squamous epithelia.[7][8] 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.[9]

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.[10]

Clinical significance

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As one of the precursor proteins of the cornified cell envelope, involucrin is markedly increased in inflammatory skin diseases such as psoriasis[11]

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.[12]

Structure

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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

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163207 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000049128 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. S2CID 39293076.583-9&rft.date=1986-08&rft_id=https://api.semanticscholar.org/CorpusID:39293076#id-name=S2CID&rft_id=info:pmid/2873896&rft_id=info:doi/10.1016/0092-8674(86)90884-6&rft.aulast=Eckert&rft.aufirst=RL&rft.au=Green, H&rfr_id=info:sid/en.wikipedia.org:Involucrin" class="Z3988">
  6. ^ a b "Entrez Gene: IVL involucrin".
  7. ^ 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. doi:10.1093/oxfordjournals.molbev.a040775. PMID 1359382.977-1017&rft.date=1992-11&rft_id=info:doi/10.1093/oxfordjournals.molbev.a040775&rft_id=info:pmid/1359382&rft.aulast=Green&rft.aufirst=H&rft.au=Djian, P&rft_id=https://doi.org/10.1093%2Foxfordjournals.molbev.a040775&rfr_id=info:sid/en.wikipedia.org:Involucrin" class="Z3988">
  8. ^ 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. doi:10.1093/oxfordjournals.molbev.a040069. PMID 8277848.1136-49&rft.date=1993-11&rft_id=info:doi/10.1093/oxfordjournals.molbev.a040069&rft_id=info:pmid/8277848&rft.aulast=Djian&rft.aufirst=P&rft.au=Phillips, M&rft.au=Easley, K&rft.au=Huang, E&rft.au=Simon, M&rft.au=Rice, RH&rft.au=Green, H&rft_id=https://doi.org/10.1093%2Foxfordjournals.molbev.a040069&rfr_id=info:sid/en.wikipedia.org:Involucrin" class="Z3988">
  9. ^ 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 8098344.613-7&rft.date=1993-05&rft_id=info:doi/10.1111/1523-1747.ep12472288&rft_id=info:pmid/8098344&rft.aulast=Eckert&rft.aufirst=RL&rft.au=Yaffe, MB&rft.au=Crish, JF&rft.au=Murthy, S&rft.au=Rorke, EA&rft.au=Welter, JF&rft_id=https://doi.org/10.1111%2F1523-1747.ep12472288&rfr_id=info:sid/en.wikipedia.org:Involucrin" class="Z3988">
  10. ^ 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 16982614.36162-72&rft.date=2006-11&rft_id=info:doi/10.1074/jbc.M605368200&rft_id=info:pmid/16982614&rft.aulast=Balasubramanian&rft.aufirst=S&rft.au=Zhu, L&rft.au=Eckert, RL&rft_id=https://doi.org/10.1074%2Fjbc.M605368200&rfr_id=info:sid/en.wikipedia.org:Involucrin" class="Z3988">
  11. ^ 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 16140218.175-82&rft.date=2005-09&rft_id=info:doi/10.1016/j.jdermsci.2005.03.006&rft_id=info:pmid/16140218&rft.aulast=Takahashi&rft.aufirst=H&rft.au=Hashimoto, Y&rft.au=Ishida-Yamamoto, A&rft.au=Iizuka, H&rfr_id=info:sid/en.wikipedia.org:Involucrin" class="Z3988">
  12. ^ 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 10210784.197-201&rft.date=1999&rft_id=info:pmid/10210784&rft.aulast=Peña-Penabad&rft.aufirst=C&rft.au=de Unamuno, P&rft.au=García Silva, J&rft.au=Ludeña, MD&rft.au=González Sarmiento, R&rft.au=Pérez-Arellano, JL&rft_id=http://www.john-libbey-eurotext.fr/medline.md?issn=1167-1122&vol=9&iss=3&page=197&rfr_id=info:sid/en.wikipedia.org:Involucrin" class="Z3988">

Further reading

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