Role of the α1β1 integrin complex in collagen gel contraction in vitro by fibroblasts

Wayne Carver, Ivan Molano, Titus A. Reaves, Thomas K. Borg, Louis Terracio

Research output: Contribution to journalArticle

Abstract

Matrix remodeling, critical to embryonic morphogenesis and wound healing, is dependent on the expression of matrix components, their receptors, and matrix proteases. The collagen gel assay has provided an effective model for the examination of the functional role(s) of each of these groups of molecules in matrix remodeling. Previous investigations have indicated that collagen gel contraction involves the β1 integrin family of matrix receptors and is stimulated by several growth factors, including TGF-β, PDGF, and angiotensin II. In particular, collagen gel remodeling by human cells involves the α2β1 and, to a lesser extent, the α1β1 integrin complexes. The present studies were undertaken to determine the role of the α1 integrin chain, a collagen/laminin receptor, in collagen gel contraction by rodent and avian fibroblasts. A high degree of correlation was found between the expression of the α1β1 integrin complex and the relative ability of cells to contract collagen gels. Further studies using antibodies and antisense oligonucleotides against the α1 integrin indicated a significant role for this integrin chain in contraction of collagen gels by rat cardiac fibroblasts. In addition, antibodies to the α1 integrin chain inhibited migration of these fibroblasts on a collagen substratum, suggesting that at least one role of this integrin is in migration of cells in collagen gels. These results indicate that the α1β1 integrin complex plays a significant role in cellular interactions with interstitial collagen that are involved in matrix remodeling such as is seen during morphogenesis and wound healing.

Original languageEnglish (US)
Pages (from-to)425-437
Number of pages13
JournalJournal of Cellular Physiology
Volume165
Issue number2
DOIs
StatePublished - Nov 1995

Fingerprint

Fibroblasts
Integrins
Collagen
Gels
Morphogenesis
Wound Healing
Collagen Receptors
Laminin Receptors
Cells
In Vitro Techniques
Antibodies
Antisense Oligonucleotides
Emigration and Immigration
Angiotensin II
Cell Movement
Rodentia
Intercellular Signaling Peptides and Proteins
Peptide Hydrolases
Rats
Assays

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology
  • Physiology

Cite this

Role of the α1β1 integrin complex in collagen gel contraction in vitro by fibroblasts. / Carver, Wayne; Molano, Ivan; Reaves, Titus A.; Borg, Thomas K.; Terracio, Louis.

In: Journal of Cellular Physiology, Vol. 165, No. 2, 11.1995, p. 425-437.

Research output: Contribution to journalArticle

Carver, Wayne ; Molano, Ivan ; Reaves, Titus A. ; Borg, Thomas K. ; Terracio, Louis. / Role of the α1β1 integrin complex in collagen gel contraction in vitro by fibroblasts. In: Journal of Cellular Physiology. 1995 ; Vol. 165, No. 2. pp. 425-437.
@article{ded587f34c7a463baff921eb4a7abc11,
title = "Role of the α1β1 integrin complex in collagen gel contraction in vitro by fibroblasts",
abstract = "Matrix remodeling, critical to embryonic morphogenesis and wound healing, is dependent on the expression of matrix components, their receptors, and matrix proteases. The collagen gel assay has provided an effective model for the examination of the functional role(s) of each of these groups of molecules in matrix remodeling. Previous investigations have indicated that collagen gel contraction involves the β1 integrin family of matrix receptors and is stimulated by several growth factors, including TGF-β, PDGF, and angiotensin II. In particular, collagen gel remodeling by human cells involves the α2β1 and, to a lesser extent, the α1β1 integrin complexes. The present studies were undertaken to determine the role of the α1 integrin chain, a collagen/laminin receptor, in collagen gel contraction by rodent and avian fibroblasts. A high degree of correlation was found between the expression of the α1β1 integrin complex and the relative ability of cells to contract collagen gels. Further studies using antibodies and antisense oligonucleotides against the α1 integrin indicated a significant role for this integrin chain in contraction of collagen gels by rat cardiac fibroblasts. In addition, antibodies to the α1 integrin chain inhibited migration of these fibroblasts on a collagen substratum, suggesting that at least one role of this integrin is in migration of cells in collagen gels. These results indicate that the α1β1 integrin complex plays a significant role in cellular interactions with interstitial collagen that are involved in matrix remodeling such as is seen during morphogenesis and wound healing.",
author = "Wayne Carver and Ivan Molano and Reaves, {Titus A.} and Borg, {Thomas K.} and Louis Terracio",
year = "1995",
month = "11",
doi = "10.1002/jcp.1041650224",
language = "English (US)",
volume = "165",
pages = "425--437",
journal = "Journal of Cellular Physiology",
issn = "0021-9541",
publisher = "Wiley-Liss Inc.",
number = "2",

}

TY - JOUR

T1 - Role of the α1β1 integrin complex in collagen gel contraction in vitro by fibroblasts

AU - Carver, Wayne

AU - Molano, Ivan

AU - Reaves, Titus A.

AU - Borg, Thomas K.

AU - Terracio, Louis

PY - 1995/11

Y1 - 1995/11

N2 - Matrix remodeling, critical to embryonic morphogenesis and wound healing, is dependent on the expression of matrix components, their receptors, and matrix proteases. The collagen gel assay has provided an effective model for the examination of the functional role(s) of each of these groups of molecules in matrix remodeling. Previous investigations have indicated that collagen gel contraction involves the β1 integrin family of matrix receptors and is stimulated by several growth factors, including TGF-β, PDGF, and angiotensin II. In particular, collagen gel remodeling by human cells involves the α2β1 and, to a lesser extent, the α1β1 integrin complexes. The present studies were undertaken to determine the role of the α1 integrin chain, a collagen/laminin receptor, in collagen gel contraction by rodent and avian fibroblasts. A high degree of correlation was found between the expression of the α1β1 integrin complex and the relative ability of cells to contract collagen gels. Further studies using antibodies and antisense oligonucleotides against the α1 integrin indicated a significant role for this integrin chain in contraction of collagen gels by rat cardiac fibroblasts. In addition, antibodies to the α1 integrin chain inhibited migration of these fibroblasts on a collagen substratum, suggesting that at least one role of this integrin is in migration of cells in collagen gels. These results indicate that the α1β1 integrin complex plays a significant role in cellular interactions with interstitial collagen that are involved in matrix remodeling such as is seen during morphogenesis and wound healing.

AB - Matrix remodeling, critical to embryonic morphogenesis and wound healing, is dependent on the expression of matrix components, their receptors, and matrix proteases. The collagen gel assay has provided an effective model for the examination of the functional role(s) of each of these groups of molecules in matrix remodeling. Previous investigations have indicated that collagen gel contraction involves the β1 integrin family of matrix receptors and is stimulated by several growth factors, including TGF-β, PDGF, and angiotensin II. In particular, collagen gel remodeling by human cells involves the α2β1 and, to a lesser extent, the α1β1 integrin complexes. The present studies were undertaken to determine the role of the α1 integrin chain, a collagen/laminin receptor, in collagen gel contraction by rodent and avian fibroblasts. A high degree of correlation was found between the expression of the α1β1 integrin complex and the relative ability of cells to contract collagen gels. Further studies using antibodies and antisense oligonucleotides against the α1 integrin indicated a significant role for this integrin chain in contraction of collagen gels by rat cardiac fibroblasts. In addition, antibodies to the α1 integrin chain inhibited migration of these fibroblasts on a collagen substratum, suggesting that at least one role of this integrin is in migration of cells in collagen gels. These results indicate that the α1β1 integrin complex plays a significant role in cellular interactions with interstitial collagen that are involved in matrix remodeling such as is seen during morphogenesis and wound healing.

UR - http://www.scopus.com/inward/record.url?scp=0028972023&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028972023&partnerID=8YFLogxK

U2 - 10.1002/jcp.1041650224

DO - 10.1002/jcp.1041650224

M3 - Article

C2 - 7593221

AN - SCOPUS:0028972023

VL - 165

SP - 425

EP - 437

JO - Journal of Cellular Physiology

JF - Journal of Cellular Physiology

SN - 0021-9541

IS - 2

ER -