β1- and β3-Class Integrins Mediate Fibronectin Binding Activity at the Surface of Developing Mouse Peri-implantation Blastocysts

Schultz, J F; Armant, D. Randall

doi:10.1074/jbc.270.19.11522

Cited by 108 publications

(87 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Outgrowth on laminin requires an integrin of the β1 family, perhaps α7β1 (Sutherland et al, 1993;Stephens et al, 1995;Yelian et al, 1995; Table 1). Schultz and Armant (1995) observed that the binding of fibronectin-coated spheres to hatched mouse blastocysts is confined to the abembryonic pole, that is, the site of initial attachment to the uterus. Furthermore, the expression of fibronectinbinding activity depends on prior exposure of the embryo to ligand in solution or on a surface.…”

Section: Embryonic Integrins and Peri-implantation Events In Micementioning

confidence: 99%

Adhesion molecules in implantation

Aplin

1997

Reviews of Reproduction

201

View full text Add to dashboard Cite

Section: Embryonic Integrins and Peri-implantation Events In Micementioning

confidence: 99%

Adhesion molecules in implantation

Aplin

1997

Reviews of Reproduction

201

View full text Add to dashboard Cite

“…Hamster monoclonal antibodies specific for CD51 (␣v␤3 integrin (Clone H9.2B)) and CD61 (␤3 integrin (Clone 2C9.2G2, HM␤3-1)) were purchased from BD Biosciences. Both these antibodies have been described as function-blocking antibodies for murine integrin subunits (40). Control isotype antibody was used as negative controls.…”

Section: Methodsmentioning

confidence: 99%

Ultrasound Induces Hypoxia-inducible Factor-1 Activation and Inducible Nitric-oxide Synthase Expression through the Integrin/Integrin-linked Kinase/Akt/Mammalian Target of Rapamycin Pathway in Osteoblasts

Tang

Tan

et al. 2007

Journal of Biological Chemistry

View full text Add to dashboard Cite

It has been shown that ultrasound (US) stimulation accelerates fracture healing in the animal models and clinical studies. Nitric oxide (NO) is a crucial early mediator in mechanically induced bone formation. Here we found that US stimulation increased NO formation and the protein level of inducible nitric-oxide synthase (iNOS). US-mediated iNOS expression was attenuated by anti-integrinFracture healing is a complex physiological process comprising the coordinated participation of several cell types. Among all the means to influence fracture healing, ultrasound (US) 3 distinguishes itself by being non-invasive and easy to apply. Low intensity levels are used to accelerate fracture healing and are considered neither thermal nor destructive. It has been shown that low intensity US accelerates fracture healing in animal models (1, 2) and clinical studies (3, 4). It has been demonstrated that low intensity-pulsed US exposure increases nitric oxide (NO) and prostaglandin release (5, 6), stimulates collagen synthesis, and promotes bone formation (7). However, the mechanisms involved in osteoblasts to detect US stress and transduce the signal across the membrane for activating signaling pathways in metabolism, such as the induction of inducible nitric-oxide synthase (iNOS) and release of NO, remain poorly understood.Integrins are cell-surface adhesion receptors that regulate cell viability in response to cues derived from the extracellular matrix (8, 9). In the case of mesenchymal cells, encompassed by the extracellular matrix, matrix-derived mechanical stimuli can regulate their viability. In this latter scenario, integrins function as mechanoreceptors that detect mechanical stimuli originating from the extracellular matrix and convert them to chemical signaling pathways that regulate cell viability (10, 11). Mechanical stimuli can be transmitted through the direct or indirect interaction of integrins with associated lipid or protein-signaling molecules in the focal adhesion complex (12, 13). Integrinlinked kinase (ILK), a potential candidate signaling molecule, has been shown to be capable of regulating integrin-mediated signaling (14). ILK can interact with the cytoplasmic domain of ␤-integrin subunits and is activated by both integrin activation as well as growth factors and is an upstream regulator of Akt (15).Hypoxia-inducible factor-1 (HIF-1) is a heterodimeric transcription factor composed of the basic helix-loop-helix-PerArnt-Sim-domain, containing the proteins HIF-1␣ and arylhydrocarbon receptor nuclear translocator (HIF-1␤) (16). The availability of HIF-1 is determined primarily by HIF-1␣, which is regulated at the protein level in an oxygen-sensitive manner, in contrast to HIF-1␤, which is stably expressed (17,18). During normoxia, HIF-1␣ is efficiently degraded through the von HippelLindau-dependent ubiquitin-proteasome pathway (18). Under * This work was supported by the National Science Council of Taiwan (Grant NSC 95-2314-B-039-045) and China Medical University . The costs of publication of this arti...

show abstract

“…Blocking antibodies against ␤ 1 and ␤ 3 integrins (Schultz and Armant, 1995;Ridger et al, 2001) were purchased from Biolegend (San Diego, CA) (CD29, CD61). All other reagents and chemicals were purchased from Roth (Karlsruhe, Germany), Invitrogen (Carlsbad, CA), or Sigma-Aldrich (St. Louis, MO).…”

Section: Methodsmentioning

confidence: 99%

Cyclic Guanosine Monophosphate-dependent Protein Kinase I Promotes Adhesion of Primary Vascular Smooth Muscle Cells

Weinmeister¹,

Łukowski²,

Linder

et al. 2008

MBoC

View full text Add to dashboard Cite

The cyclic guanosine monophosphate (cGMP)/cGMP-dependent protein kinase type I (cGKI) pathway regulates many cellular functions. The current study shows that 8-Br-cGMP stimulates the number of attached primary but not that of subcultured murine vascular smooth muscle cells (VSMCs). These effects of 8-Br-cGMP require the presence of cGKI. In agreement with previous studies, cGKI inhibited the number of cells in repeatedly passaged murine VSMCs. Activation of the cGMP/cGKI pathway in freshly isolated primary VSMCs slightly decreased apoptosis and strongly increased cell adhesion. The stimulation of cell adhesion by cGKI involves an inhibition of the RhoA/Rho kinase pathway and increased exposure of ␤ 1 and ␤ 3 integrins on the cell surface. Together, these results identify a novel proadhesive function of cGMP/cGKI signaling in primary VSMCs and suggest that the opposing effects of this pathway on VSMC number depend on the phenotypic context of the cells. INTRODUCTIONThe nitric oxide (NO)/cyclic guanosine monophosphate (cGMP)/cGMP-dependent protein kinase type I (cGKI) pathway regulates important functions in many cell types, including vascular smooth muscle cells (VSMCs) Lohmann and Walter, 2005;Hofmann et al., 2006;Lincoln et al., 2006). In addition to its potent vasorelaxant properties, it has been associated with vascular proliferative diseases, such as atherosclerosis and restenosis (von der Leyen et al., 1995;Janssens et al., 1998;Varenne et al., 1998;von der Thusen et al., 2004). Several studies (an excellent summary is given in Lincoln et al., 2006) suggested that activation of cGKI-dependent pathways has antimitogenic effects in smooth muscle cells (SMCs) in culture (Garg and Hassid, 1989;Boerth et al., 1997;Chiche et al., 1998;Brophy et al., 2002) and might be vasculoprotective in the intact animal (Anderson et al., 2000;Sinnaeve et al., 2002). Despite a large body of evidence that active cGKI acts antiproliferative, Hassid and coworkers reported that NO/ cGMP amplified the proliferative response of fibroblast growth factor-2 in primary VSMCs (Hassid et al., 1994). These results were supported by a report that NO and cGMP analogues activated rather than inhibited the mitogen-activated protein (MAP) kinase pathway in freshly isolated rat aortic VSMCs (Komalavilas et al., 1999). An increased MAP kinase activity has been associated with an increase in cell proliferation. The antiproliferative effect of cGMP/cGKI signaling could not be confirmed by a study on atherosclerosis in an in vivo mouse model (Wolfsgruber et al., 2003). This study suggested a proatherogenic role of VSMC cGKI. Furthermore, the recent analysis of several murine models for restenosis did not show significant effects of the presence or absence of cGKI in VSMCs on restenosis (Lukowski et al., 2008).Previous in vitro and in vivo studies led to the hypothesis that cGKI may affect different functions in primary and cultured VSMCs. A loss or reduction of cGKI, as it may occur during passage of VSMCs, is associated with the development of a syn...

show abstract

β1- and β3-Class Integrins Mediate Fibronectin Binding Activity at the Surface of Developing Mouse Peri-implantation Blastocysts

Cited by 108 publications

References 51 publications

Adhesion molecules in implantation

Adhesion molecules in implantation

Ultrasound Induces Hypoxia-inducible Factor-1 Activation and Inducible Nitric-oxide Synthase Expression through the Integrin/Integrin-linked Kinase/Akt/Mammalian Target of Rapamycin Pathway in Osteoblasts

Cyclic Guanosine Monophosphate-dependent Protein Kinase I Promotes Adhesion of Primary Vascular Smooth Muscle Cells

Contact Info

Product

Resources

About