Surface relocation of alpha 6 beta 4 integrins and assembly of hemidesmosomes in an in vitro model of wound healing.

Kurpakus, Michelle A.; Quaranta, Vito; Jones, Jonathan

doi:10.1083/jcb.115.6.1737

Cited by 152 publications

(73 citation statements)

References 33 publications

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“…receptor for laminin (35,54,55 We have extended previous studies (19)(20)(21)(22) by demonstrating that HER-2/neu and HER-3 are both expressed in skin and dermal adnexa. We have also shown that HER-2/neu expression is markedly decreased in the migrating new epidermis, while neoepidermal HER-3 expression is markedly increased.…”

Section: Discussionmentioning

confidence: 51%

Neu differentiation factor upregulates epidermal migration and integrin expression in excisional wounds.

Danilenko

Ring²,

Lü³

et al. 1995

J. Clin. Invest.

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Neu differentiation factor (NDF) is a 44-kD glycoprotein which was isolated from ras-transformed rat , applied once at the time of wounding, induced a highly significant increase in both epidermal migration and epidermal thickness at doses ranging from 4 to 40 ,ug/cm2. In contrast, rhNDF-al, rhNDF-pl, and rhNDF-132 had no apparent biologic effects in this model. rhNDF-a2 also induced increased neoepidermal expression of as and a6 integrins, two of the earliest integrins to appear during epidermal migration. In addition, rhNDF-a2-treated wounds exhibited increased neoepidermal expression of cytokeratin 10 and filaggrin, both epidermal differentiation markers. NDF a isoforms were expressed in dermal fibroblasts of wounded and unwounded skin, while both HER-2/neu and HER-3 were expressed in unwounded epidermis and dermal adnexa. In wounds, HER-2/neu expression was markedly decreased in the wound neoepidermis while neoepidermal HER-3 expression was markedly upregulated.

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Section: Discussionmentioning

confidence: 51%

Neu differentiation factor upregulates epidermal migration and integrin expression in excisional wounds.

Danilenko

Ring²,

Lü³

et al. 1995

J. Clin. Invest.

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“…The a6134-integrin localizes in hemidesmosomes (20-23) but it is not restricted to that location. It was recently shown that in an in vitro model ofwound healing, a614 appears along the entire cell surface of migrating keratinocytes in which the hemidesmosomes are absent (21 ). Epiligrin serves as a good candidate for a ligand for a614 in migrating keratinocytes.…”

Section: Discussionmentioning

confidence: 99%

“…The a331-integrin has been reported to bind several ligands, namely fibronectin, collagen, laminin, and epiligrin (5,14,15,19). The a6134-integrin localizes in hemidesmosome structures (20)(21)(22)(23), probably binding to epiligrin (24) or kalinin (25) present in the anchoring filaments. Finally, the acv#5-integrin mediates keratinocyte adhesion on vitronectin ( 14).…”

Section: Introductionmentioning

confidence: 99%

Expression of integrins and basement membrane components by wound keratinocytes.

Larjava¹,

Salo²,

Haapasalmi³

et al. 1993

J. Clin. Invest.

368

309

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Extracellular matrix proteins and their cellular receptors, integrins, play a fundamental role in keratinocyte adhesion and migration. During wound healing, keratinocytes detach, migrate until the two epithelial sheets confront, and then regenerate the basement membrane. We examined the expression of different integrins and their putative ligands in keratinocytes during human mucosal wound healing. Migrating keratinocytes continuously expressed kalinin but not the other typical components of the basement membrane zone: type IV collagen, laminin, and type VII collagen. When the epithelial sheets confronted each other, these missing basement membrane components started to appear gradually through the entire wound area. The expression of integrin 81 subunit was increased in keratinocytes during migration. The #,B-associated a2 and a3 subunits were expressed constantly by wound keratinocytes whereas the a5 subunit was present only in keratinocytes during reepithelialization. Furthermore, migrating cells started to express a,-integrins which were not present in the nonaffected epithelium. All keratinocytes also expressed the a684 integrin during migration. In the migrating cells, the distribution of integrins was altered. In normal mucosa, ,61-integrins were located mainly on the lateral plasma membrane and aQ84 at the basal surface of basal keratinocytes in the nonaffected tissue. In wounds, integrins were found in filopodia of migrating keratinocytes, and also surrounding cells in several cell layers of the migrating sheet. The results indicate that migrating keratinocytes in deep human wounds enlarge their integrin repertoire. The changes in integrin expression take place concomitantly with changes in the basement membrane composition, suggesting a close interplay of these two groups of molecules during wound healing. (J. Clin. Invest. 1993. 92:1425-1435

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“…α6β4 integrin has generally been viewed as a mediator of attachment and HD formation at sites more distal from the wound edge (Kurpakus et al, 1991;Nguyen et al, 2000a) or even as an inhibitor of keratinocyte motility (Hintermann et al, 2001). However, several lines of evidence suggest α6β4 integrin may play a more direct and active role in keratinocyte migration.…”

Section: Introductionmentioning

confidence: 99%

“…We believe that it is unlikely that keratinocytes make isolated contact between collagen I and α2β1 integrin at the front edge of a wound. Indeed, leading cells highly express unprocessed laminin-5, and upregulate expression of many integrins including α2β1, α3β1 and α6β4 (Kainulainen et al, 1998;Kurpakus et al, 1991;Larjava et al, 1993). Therefore, growth factor-induced chemotactic signals must be translated from several of these inputs into a functionally coordinated response.…”

Section: Direct Activation Of α3β1 Integrin Though β4(ad)mentioning

confidence: 99%

α6β4 integrin regulates keratinocyte chemotaxis through differential GTPase activation and antagonism of α3β1 integrin

Russell

Fincher

Millman

et al. 2003

Journal of Cell Science

126

112

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Surface relocation of alpha 6 beta 4 integrins and assembly of hemidesmosomes in an in vitro model of wound healing.

Abstract: Abstract. A transmembrane extracellular matrix receptor of the integrin family, a684, is a component of the hemidesmosome, an adhesion complex of importance in epithelial cell-connective tissue attachment

Cited by 152 publications

References 33 publications

Neu differentiation factor upregulates epidermal migration and integrin expression in excisional wounds.

Neu differentiation factor upregulates epidermal migration and integrin expression in excisional wounds.

Expression of integrins and basement membrane components by wound keratinocytes.

α6β4 integrin regulates keratinocyte chemotaxis through differential GTPase activation and antagonism of α3β1 integrin

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