Adhesion and Migration, the Diverse Functions of the Laminin α3 Subunit

Kevin J. Hamill; Amy S. Paller; Jonathan C.R. Jones

doi:10.1016/j.det.2009.10.009

Adhesion and Migration, the Diverse Functions of the Laminin α3 Subunit

Kevin J. Hamill^*, Amy S. Paller, Jonathan C.R. Jones

^*Corresponding author for this work

Dermatology

Research output: Contribution to journal › Review article › peer-review

35 Scopus citations

Abstract

The laminins are a secreted family of heterotrimeric molecules essential for basement membrane formation, structure, and function. It is now well established that the α3 subunit of laminins-332, -321, and -311 plays an important role in mediating epidermal-dermal integrity and is essential for the skin to withstand mechanical stresses. These laminins also regulate cell migration and mechanosignal transduction. This article provides an overview of the gene, transcripts, and protein structures of laminin α3. Also discussed are the proposed functions for the α3 subunit-containing laminins.

Original language	English (US)
Pages (from-to)	79-87
Number of pages	9
Journal	Dermatologic clinics
Volume	28
Issue number	1
DOIs	https://doi.org/10.1016/j.det.2009.10.009
State	Published - Jan 2010

Keywords

Basement membrane
Cell adhesion
Cell migration
Laminins

ASJC Scopus subject areas

Dermatology

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10.1016/j.det.2009.10.009

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title = "Adhesion and Migration, the Diverse Functions of the Laminin α3 Subunit",

abstract = "The laminins are a secreted family of heterotrimeric molecules essential for basement membrane formation, structure, and function. It is now well established that the α3 subunit of laminins-332, -321, and -311 plays an important role in mediating epidermal-dermal integrity and is essential for the skin to withstand mechanical stresses. These laminins also regulate cell migration and mechanosignal transduction. This article provides an overview of the gene, transcripts, and protein structures of laminin α3. Also discussed are the proposed functions for the α3 subunit-containing laminins.",

keywords = "Basement membrane, Cell adhesion, Cell migration, Laminins",

author = "Hamill, {Kevin J.} and Paller, {Amy S.} and Jones, {Jonathan C.R.}",

note = "Funding Information: Work in the Jones laboratory is supported by grant RO1 AR054184 (JCRJ) from the National Institutes of Health. ",

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T1 - Adhesion and Migration, the Diverse Functions of the Laminin α3 Subunit

AU - Hamill, Kevin J.

AU - Paller, Amy S.

AU - Jones, Jonathan C.R.

N1 - Funding Information: Work in the Jones laboratory is supported by grant RO1 AR054184 (JCRJ) from the National Institutes of Health.

PY - 2010/1

Y1 - 2010/1

N2 - The laminins are a secreted family of heterotrimeric molecules essential for basement membrane formation, structure, and function. It is now well established that the α3 subunit of laminins-332, -321, and -311 plays an important role in mediating epidermal-dermal integrity and is essential for the skin to withstand mechanical stresses. These laminins also regulate cell migration and mechanosignal transduction. This article provides an overview of the gene, transcripts, and protein structures of laminin α3. Also discussed are the proposed functions for the α3 subunit-containing laminins.

AB - The laminins are a secreted family of heterotrimeric molecules essential for basement membrane formation, structure, and function. It is now well established that the α3 subunit of laminins-332, -321, and -311 plays an important role in mediating epidermal-dermal integrity and is essential for the skin to withstand mechanical stresses. These laminins also regulate cell migration and mechanosignal transduction. This article provides an overview of the gene, transcripts, and protein structures of laminin α3. Also discussed are the proposed functions for the α3 subunit-containing laminins.

KW - Basement membrane

KW - Cell adhesion

KW - Cell migration

KW - Laminins

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DO - 10.1016/j.det.2009.10.009

M3 - Review article

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SN - 0733-8635

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JO - Dermatologic clinics

JF - Dermatologic clinics

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Adhesion and Migration, the Diverse Functions of the Laminin α3 Subunit

Abstract

Keywords

ASJC Scopus subject areas

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