Role of integrins in cell adhesion and polarity in normal keratinocytes and human skin pathologies - PubMed (original) (raw)

Review

Role of integrins in cell adhesion and polarity in normal keratinocytes and human skin pathologies

M De Luca et al. J Dermatol. 1994 Nov.

Abstract

In vitro, normal human keratinocytes reconstitute a differentiated stratified epidermis, maintaining the same gene expression pattern as its in vivo counterpart and are suitable for permanent grafting onto patients. Keratinocyte adhesion to basal lamina and lateral interactions among basal epidermal cells are also mediated by integrin receptors that are sorted to defined plasma membrane domains. The hemidesmosome-associated integrin alpha 6 beta 4 is sharply localized at the basal surface of basal cells and codistributes with laminin and nicein/kalinin; the alpha 2 beta 1 and alpha 3 beta 1 integrins are enriched laterally and play crucial roles in cell-cell interaction and proper colony morphology. During wound healing, proliferating and migrating keratinocytes express on their plasma membrane alpha v beta 5 and alpha 5 beta 1, which allow keratinocyte attachment and migration over the provisional matrix present in the wound. TGF beta, which is an autocrine and paracrine mediator in wound healing, specifically increases the synthesis and expression of alpha v beta 5 and alpha 5 beta 1, induces the de novo expression of alpha v beta 6, and determines the loss of integrin polarization. In hyperproliferative skin diseases, such as skin cancer or psoriasis vulgaris, and in normal keratinocytes forced into more frequent cell cycles, the polarized expression of integrins is lost, and alpha 5 beta 1 becomes costitutively expressed on the plasma membrane. In addition, the alpha 6 beta 4 integrin becomes associated with focal contacts. Nerve growth factor (NGF) is a potent autocrine stimulator of keratinocyte growth and induces melanocyte migration toward the leading edge of a healing wound.(ABSTRACT TRUNCATED AT 250 WORDS)

PubMed Disclaimer

Cited by

Low-frequency low-intensity ultrasounds do not influence the survival and immune functions of cultured keratinocytes and dendritic cells.
Scarponi C, Nasorri F, Pavani F, Madonna S, Sestito R, Simonacci M, De Pità O, Cavani A, Albanesi C. Scarponi C, et al. J Biomed Biotechnol. 2009;2009:193260. doi: 10.1155/2009/193260. Epub 2010 Jan 19. J Biomed Biotechnol. 2009. PMID: 20145702 Free PMC article.
Regulation of wound healing and fibrosis by hypoxia and hypoxia-inducible factor-1.
Ruthenborg RJ, Ban JJ, Wazir A, Takeda N, Kim JW. Ruthenborg RJ, et al. Mol Cells. 2014 Sep;37(9):637-43. doi: 10.14348/molcells.2014.0150. Epub 2014 Jun 24. Mol Cells. 2014. PMID: 24957212 Free PMC article. Review.
Reversion of the malignant phenotype of human breast cells in three-dimensional culture and in vivo by integrin blocking antibodies.
Weaver VM, Petersen OW, Wang F, Larabell CA, Briand P, Damsky C, Bissell MJ. Weaver VM, et al. J Cell Biol. 1997 Apr 7;137(1):231-45. doi: 10.1083/jcb.137.1.231. J Cell Biol. 1997. PMID: 9105051 Free PMC article.
Gpnmb is a melanosome-associated glycoprotein that contributes to melanocyte/keratinocyte adhesion in a RGD-dependent fashion.
Tomihari M, Hwang SH, Chung JS, Cruz PD Jr, Ariizumi K. Tomihari M, et al. Exp Dermatol. 2009 Jul;18(7):586-95. doi: 10.1111/j.1600-0625.2008.00830.x. Epub 2009 Mar 6. Exp Dermatol. 2009. PMID: 19320736 Free PMC article.
Collagenase promotes the cellular responses to injury and wound healing in vivo.
Riley KN, Herman IM. Riley KN, et al. J Burns Wounds. 2005 May 17;4:e8. J Burns Wounds. 2005. PMID: 16921413 Free PMC article.

Role of integrins in cell adhesion and polarity in normal keratinocytes and human skin pathologies - PubMed (original) (raw)