Analysis of alpha 1 beta 1, alpha 2 beta 1 and alpha 3 beta 1 integrins in cell--collagen interactions: identification of conformation dependent alpha 1 beta 1 binding sites in collagen type I.

Gullberg, Donald; Gehlsen, Kurt R.; Turner, David C.; Åhlén, Karina; Zijenah, Lynn S.; Barnes, Michael J.; Rubin, Kristofer

doi:10.1002/j.1460-2075.1992.tb05479.x

Cited by 211 publications

(147 citation statements)

References 46 publications

(60 reference statements)

Supporting

Mentioning

134

Contrasting

Unclassified

Order By: Relevance

“…2A, lanes 1 and 2), as well as a more slowly migrating band, which presumably represents ␣ 1 . 33 Upon culturing the hepatocytes for 3 days, the cell-surface ␤ 1 -integrin profile of the hepatocytes appeared virtually identical to that of H2.35 cells, with the major immunoprecipitated proteins comigrating with ␣ 3 -and ␤ 1 -subunits (Fig. 2B, lanes A B (lanes 2 and 3).…”

Section: The Integrin Profile Of H235 Cells Resembles That Of Primarymentioning

confidence: 75%

“…Thus, the apparent expression of ␣ 3 -integrin subunits on cultured mouse hepatocytes is similar to biochemical findings on the rat. 33 …”

Section: The Integrin Profile Of H235 Cells Resembles That Of Primarymentioning

confidence: 99%

“…34 Although ␣ 3 ␤ 1 -integrin was originally considered to be most important for cell attachment to collagen, more recent studies suggest that it has a higher affinity for laminin. 33,[35][36][37][38][39] Direct biochemical evidence exists showing that adult rat hepatocytes express ␣ 3 ␤ 1 -integrin, 33 yet immunohistochemical analysis of normal adult human hepatocytes …”

mentioning

confidence: 99%

“…3,[6][7][8][26][27][28][29][30][31] Freshly isolated rat hepatocytes can bind to collagen via ␣ 1 ␤ 1 -integrin, 32 as shown by the ability of a monoclonal antibody to the ␣ 1 subunit to block binding to native type I collagen. 33 Hepatocyte binding to fibronectin, specifically at the amino acid sequence RGD, is mediated by ␣ 5 ␤ 1 -integrin. 34 Although ␣ 3 ␤ 1 -integrin was originally considered to be most important for cell attachment to collagen, more recent studies suggest that it has a higher affinity for laminin.…”

mentioning

confidence: 99%

See 3 more Smart Citations

?3?1-integrin as a critical mediator of the hepatic differentiation response to the extracellular matrix

et al. 1998

View full text Add to dashboard Cite

The extracellular matrix (ECM) promotes the differentiation of many cell types, and ECM remodeling in the liver has been implicated in embryonic development, tissue injury, and oncogenesis. Integrins are heterodimeric ECM receptors that play critical roles in transducing the composition of the ECM in the cell environment. We previously showed that mouse H2.35 cells, a conditionally transformed, liver-derived cell line, assume a more differentiated hepatocyte morphology and enhanced liver-specific gene expression when the cells are cultured on gelatinous ECM substrata. Here we show that H2.35 cells express relatively high levels of ␣ 3 ␤ 1 -integrins, similar to that previously shown for immature hepatocytes, transformed hepatocytes, and biliary cells. However, the cell morphological responses that depend on ␣ 3 ␤ 1 -integrin have not been defined. We found that transfecting H2.35 cells with antisense RNA construct directed to ␣ 3 -subunit messenger RNA perturbs the initial cell attachment to laminin and collagen, and strongly inhibits cell morphological, proliferative, and gene expression responses to a collagen gel substratum. In situ hybridization to mouse embryo tissues demonstrates the presence of ␣ 3 -subunit messenger RNAs in newly formed hepatocytes. We suggest that ␣ 3 ␤ 1 -integrins are important for immature and transformed hepatocytes to respond morphologically to the extracellular matrix. (HEPATOLOGY 1998;28:1095-1104.)Tissue-specific gene expression, morphogenesis, and cell migration are promoted by interactions between cells and the surrounding extracellular matrix (ECM). For example, early hepatocyte differentiation begins as foregut endodermal cells enter the new collagenous environment of the surrounding mesenchyme, 1 and the role of the ECM in adult hepatocyte differentiation is well established. [2][3][4][5][6][7][8] Other examples of ECMpromoted differentiation include the differentiation of keratinocytes, 9 gastrulation in Pleurodeles embryos, 10 and the epithelial conversion of kidney mesenchyme 11 (for review, see Adams and Watt 12 ). The ECM is present in all animals from the earliest stages of development and is composed of a mixture of proteins and proteoglycans such as collagens, laminin, and fibronectin. An important set of membrane receptors for ECM molecules is the integrin family of proteins. [13][14][15] Integrins are heterodimers of ␣ and ␤ subunits, with each subunit containing an N-terminal extracellular domain, a transmembrane domain, and a C-terminal intracellular domain. Integrins activate common as well as subgroupspecific intracellular signaling pathways in response to the ECM. 16,17 Membrane proximal events triggered by integrin ligation include the activation of the focal adhesion kinase 18 by the ␤ subunit and the recruitment of adapter protein Shc by certain ␣ subunits within heterodimers. 19 More ␣ subunits are known than ␤ subunits, and the particular combination of ␣ and ␤ partners determines the ligand specificity for ECM molecules. An ECM protein can be recognized...

show abstract

Section: The Integrin Profile Of H235 Cells Resembles That Of Primarymentioning

confidence: 75%

“…Thus, the apparent expression of ␣ 3 -integrin subunits on cultured mouse hepatocytes is similar to biochemical findings on the rat. 33 …”

Section: The Integrin Profile Of H235 Cells Resembles That Of Primarymentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

?3?1-integrin as a critical mediator of the hepatic differentiation response to the extracellular matrix

et al. 1998

View full text Add to dashboard Cite

show abstract

“…Particularly, the globular organization of collagen upon immobilization on this surface likely presents binding sites for the main collagen integrins of dermal fibroblasts (α 1 β 1 , α 2 β 1 ) 69 in a conformation that allows integrin clustering and focal adhesion formation even at low protein concentrations. Interestingly, the distance between the globular clusters on PL-GP-col samples is in range of 70 nm, which has been indicated as the critical local inter-ligand spacing for integrin clustering and cell adhesion.…”

Section: Focal Points Formation and Fibronectin Fibrillogenesismentioning

confidence: 99%

Different Organization of Type I Collagen Immobilized on Silanized and Nonsilanized Titanium Surfaces Affects Fibroblast Adhesion and Fibronectin Secretion

Marín-Pareja

Cantini

González-García

et al. 2015

ACS Appl. Mater. Interfaces

View full text Add to dashboard Cite

ABSTRACT:Silanization has emerged in recent years as a way to obtain a stronger and more stable attachment of biomolecules to metallic substrates. However, its impact on protein conformation, a key aspect that influences cell response, has hardly been studied. In this work we analyzed by AFM the distribution and conformation of type I collagen on plasma treated surfaces before and after silanization. Subsequently, we investigated the effect of the different collagen conformations on fibroblasts adhesion and fibronectin secretion by immunofluorescence analyses. Two different organosilanes were used on plasma-treated titanium surfaces, either 3-chloropropyl-triethoxy-silane (CPTES), or 3-Glycidyloxypropyl-triethoxy-silane (GPTES). The properties and amount of the adsorbed collagen was assessed by contact angle, XPS, OWLS and AFM.AFM studies revealed different conformations of type I collagen depending on the silane employed. Collagen was organized in fibrillar networks over very hydrophilic (plasma treated titanium) or hydrophobic (silanized with CPTES) surfaces, the latter forming little globules with a beads-on-a-string appearance, whereas over surfaces presenting an intermediate hydrophobic character (silanized with GPTES), collagen was organized into clusters with a size increasing at higher protein concentration in solution.Cell response was strongly affected by collagen conformation, especially at low collagen density. The samples exhibiting collagen organized in globular clusters (GPTES-functionalized samples) favored a faster and better fibroblast adhesion, as well as better cell spreading, focal adhesions formation and more pronounced fibronectin fibrillogenesis. In contrast, when a certain protein concentration was reached at the material surface the effect of collagen conformation was masked, and similar fibroblast response was observed in all samples.

show abstract

Adhesion-guided in vitro morphogenesis in pure and mixed cell cultures

Powers

Griffith

1998

Microsc. Res. Tech.

View full text Add to dashboard Cite

Analysis of alpha 1 beta 1, alpha 2 beta 1 and alpha 3 beta 1 integrins in cell--collagen interactions: identification of conformation dependent alpha 1 beta 1 binding sites in collagen type I.

Cited by 211 publications

References 46 publications

?3?1-integrin as a critical mediator of the hepatic differentiation response to the extracellular matrix

?3?1-integrin as a critical mediator of the hepatic differentiation response to the extracellular matrix

Different Organization of Type I Collagen Immobilized on Silanized and Nonsilanized Titanium Surfaces Affects Fibroblast Adhesion and Fibronectin Secretion

Adhesion-guided in vitro morphogenesis in pure and mixed cell cultures

Contact Info

Product

Resources

About