Biology:Involucrin
 Generic protein structure example |
| Involucrin of squamous epithelia N-terminus | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Involucrin_N | ||||||||
| Pfam | PF10583 | ||||||||
| InterPro | IPR019571 | ||||||||
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| Involucrin repeat | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Involucrin | ||||||||
| Pfam | PF00904 | ||||||||
| InterPro | IPR000354 | ||||||||
| SCOP2 | 1eu0 / SCOPe / SUPFAM | ||||||||
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| Involucrin repeat | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Involucrin2 | ||||||||
| Pfam | PF06994 | ||||||||
| InterPro | IPR009733 | ||||||||
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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
- ↑ "Structure and evolution of the human involucrin gene". Cell 46 (4): 583–9. August 1986. doi:10.1016/0092-8674(86)90884-6. PMID 2873896.
- ↑ 2.0 2.1 "Entrez Gene: IVL involucrin". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3713.
- ↑ "Consecutive actions of different gene-altering mechanisms in the evolution of involucrin". Molecular Biology and Evolution 9 (6): 977–1017. November 1992. doi:10.1093/oxfordjournals.molbev.a040775. PMID 1359382.
- ↑ "The involucrin genes of the mouse and the rat: study of their shared repeats". Molecular Biology and Evolution 10 (6): 1136–49. November 1993. doi:10.1093/oxfordjournals.molbev.a040069. PMID 8277848.
- ↑ "Involucrin--structure and role in envelope assembly". The Journal of Investigative Dermatology 100 (5): 613–7. May 1993. doi:10.1111/1523-1747.ep12472288. PMID 8098344.
- ↑ "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. November 2006. doi:10.1074/jbc.M605368200. PMID 16982614.
- ↑ "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. September 2005. doi:10.1016/j.jdermsci.2005.03.006. PMID 16140218.
- ↑ "Altered expression of immunoreactive involucrin in lamellar ichthyosis". European Journal of Dermatology 9 (3): 197–201. 1999. PMID 10210784. http://www.john-libbey-eurotext.fr/medline.md?issn=1167-1122&vol=9&iss=3&page=197.
Further reading
- "Regulation of involucrin gene expression". The Journal of Investigative Dermatology 123 (1): 13–22. July 2004. doi:10.1111/j.0022-202X.2004.22723.x. PMID 15191537.
- "Presence in human epidermal cells of a soluble protein precursor of the cross-linked envelope: activation of the cross-linking by calcium ions". Cell 18 (3): 681–94. November 1979. doi:10.1016/0092-8674(79)90123-5. PMID 42494. https://escholarship.org/uc/item/8pc4c9rc.
- "Biophysical characterization of involucrin reveals a molecule ideally suited to function as an intermolecular cross-bridge of the keratinocyte cornified envelope". The Journal of Biological Chemistry 267 (17): 12233–8. June 1992. doi:10.1016/S0021-9258(19)49829-3. PMID 1601889. http://www.jbc.org/cgi/pmidlookup?view=long&pmid=1601889.
- "The glutamine residues reactive in transglutaminase-catalyzed cross-linking of involucrin". The Journal of Biological Chemistry 263 (34): 18093–8. December 1988. doi:10.1016/S0021-9258(19)81327-3. PMID 2461365. http://www.jbc.org/cgi/pmidlookup?view=long&pmid=2461365.
- "Repeat arrays in cellular DNA related to the Epstein-Barr virus IR3 repeat". Molecular and Cellular Biology 5 (3): 457–65. March 1985. doi:10.1128/mcb.5.3.457. PMID 2985954.
- "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". The Journal of Biological Chemistry 270 (21): 12614–22. May 1995. doi:10.1074/jbc.270.21.12614. PMID 7759510.
- "Physical mapping of a functional cluster of epidermal differentiation genes on chromosome 1q21". Genomics 18 (1): 92–9. October 1993. doi:10.1006/geno.1993.1430. PMID 8276421.
- "Analysis of the 5'-upstream promoter region of human involucrin gene: activation by 12-O-tetradecanoylphorbol-13-acetate". The Journal of Investigative Dermatology 100 (1): 10–5. January 1993. doi:10.1111/1523-1747.ep12349867. PMID 8380829.
- "Transcriptional analysis of the 5'-noncoding region of the human involucrin gene". The Journal of Biological Chemistry 271 (1): 512–20. January 1996. doi:10.1074/jbc.271.1.512. PMID 8550612.
- "Repression of involucrin gene expression by transcriptional enhancer factor 1 (TEF-1)". Archives of Dermatological Research 287 (8): 740–6. 1995. doi:10.1007/BF01105799. PMID 8554386.
- "Direct evidence that involucrin is a major early isopeptide cross-linked component of the keratinocyte cornified cell envelope". The Journal of Biological Chemistry 272 (3): 2021–30. January 1997. doi:10.1074/jbc.272.3.2021. PMID 8999895.
- "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". The Journal of Biological Chemistry 272 (18): 12035–46. May 1997. doi:10.1074/jbc.272.18.12035. PMID 9115270.
- "Regulation of involucrin gene expression by calcium in normal human keratinocytes". Frontiers in Bioscience 1: a16-24. January 1996. doi:10.2741/A101. PMID 9159190.
- "Characterization of human involucrin promoter distal regulatory region transcriptional activator elements-a role for Sp1 and AP1 binding sites". The Biochemical Journal 331 (1): 61–8. April 1998. doi:10.1042/bj3310061. PMID 9512462.
- "Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope". The Journal of Biological Chemistry 273 (28): 17763–70. July 1998. doi:10.1074/jbc.273.28.17763. PMID 9651377.
- "The distal regulatory region of the human involucrin promoter is required for expression in epidermis". The Journal of Biological Chemistry 273 (46): 30460–5. November 1998. doi:10.1074/jbc.273.46.30460. PMID 9804813.
- "Small proline-rich protein 1 is the major component of the cell envelope of normal human oral keratinocytes". FEBS Letters 477 (3): 268–72. July 2000. doi:10.1016/S0014-5793(00)01806-8. PMID 10908733.
- "Transglutaminase 5 cross-links loricrin, involucrin, and small proline-rich proteins in vitro". The Journal of Biological Chemistry 276 (37): 35014–23. September 2001. doi:10.1074/jbc.M010157200. PMID 11443109.
- "The human involucrin gene contains spatially distinct regulatory elements that regulate expression during early versus late epidermal differentiation". Oncogene 21 (5): 738–47. January 2002. doi:10.1038/sj.onc.1205038. PMID 11850802.
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