scholarly journals Cell Adhesion by Integrins

2019 ◽  
Vol 99 (4) ◽  
pp. 1655-1699 ◽  
Author(s):  
Michael Bachmann ◽  
Sampo Kukkurainen ◽  
Vesa P. Hytönen ◽  
Bernhard Wehrle-Haller
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Intracellular Signaling ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Center Stage ◽  
Pathological Conditions ◽  
Mechanical Connection ◽  
New Generation

Integrins are heterodimeric cell surface receptors ensuring the mechanical connection between cells and the extracellular matrix. In addition to the anchorage of cells to the extracellular matrix, these receptors have critical functions in intracellular signaling, but are also taking center stage in many physiological and pathological conditions. In this review, we provide some historical, structural, and physiological notes so that the diverse functions of these receptors can be appreciated and put into the context of the emerging field of mechanobiology. We propose that the exciting journey of the exploration of these receptors will continue for at least another new generation of researchers.

Biological specificity and measurable physical properties of cell surface receptors and their possible role in signal transduction through the cytoskeleton

1995 ◽  
Vol 73 (7-8) ◽  
pp. 317-326 ◽  
Author(s):  
G. Forgacs
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Physical Properties ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Intracellular Signaling ◽  
Genetically Engineered ◽  
Cell Surface Receptors ◽  
Adhesive Properties ◽  
Surface Receptors

It is proposed that the binding specificities of cell adhesion molecules are manifested in their measurable physical properties. A method specifically designed to measure the interfacial tension of cell aggregates is described. With the introduction of a statistical mechanical model, the measured values of tensions for aggregates consisting of genetically engineered cells with controlled adhesive properties are used to obtain information on the strength of individual receptor–ligand bonds. The strength of binding must depend on the receptor and its ligand and reflects the amino acid sequence of the binding proteins. Many of the cell surface receptors, being transmembrane proteins, are attached to the various macromolecular networks of the cytoskeleton; therefore, it is suggested that their ligation and ensuing conformational change may substantially affect the mechanical state of the cytoskeletal assemblies. Since these assemblies are believed to actively participate in intracellular signaling by transmitting signals from the cell membrane into the nucleus, the cell adhesion molecules may influence signaling in a predictable way through their measurable physical characteristics. In particular, varying bond strength at the cell surface may lead to differential gene regulation.Key words: cell adhesion, surface tension, signaling, network, filament.

scholarly journals Interplay between Cell-Surface Receptors and Extracellular Matrix in Skin

Biomolecules ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 1170
Author(s):  
Svenja Kleiser ◽  
Alexander Nyström
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Cell Surface ◽  
Skin Diseases ◽  
Biochemical Properties ◽  
Dermal Fibroblasts ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Dermal Cell ◽  
Epidermal Basement Membrane

Skin consists of the epidermis and dermis, which are connected by a specialized basement membrane—the epidermal basement membrane. Both the epidermal basement membrane and the underlying interstitial extracellular matrix (ECM) created by dermal fibroblasts contain distinct network-forming macromolecules. These matrices play various roles in order to maintain skin homeostasis and integrity. Within this complex interplay of cells and matrices, cell surface receptors play essential roles not only for inside-out and outside-in signaling, but also for establishing mechanical and biochemical properties of skin. Already minor modulations of this multifactorial cross-talk can lead to severe and systemic diseases. In this review, major epidermal and dermal cell surface receptors will be addressed with respect to their interactions with matrix components as well as their roles in fibrotic, inflammatory or tumorigenic skin diseases.

scholarly journals Integrins as architects of cell behavior

2016 ◽  
Vol 27 (19) ◽  
pp. 2885-2888 ◽  
Author(s):  
Charles H. Streuli
Keyword(s):  
Extracellular Matrix ◽  
Mammary Gland ◽  
Cell Surface ◽  
Cell Function ◽  
External Environment ◽  
Cell Behavior ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Mammary Gland Differentiation

Integrins are cell surface receptors that bind cells to their physical external environment, linking the extracellular matrix to cell function. They are essential in the biology of all animals. In the late 1980s, we discovered that integrins are required for the ability of breast epithelia to do what they are programmed to do, which is to differentiate and make milk. Since then, integrins have been shown to control most other aspects of phenotype: to stay alive, to divide, and to move about. Integrins also provide part of the mechanism that allows cells to form tissues. Here I discuss how we discovered that integrins control mammary gland differentiation and explore the role of integrins as central architects of other aspects of cell behavior.

scholarly journals Impaired chemotaxis and cell adhesion due to decrease in several cell-surface receptors in cathepsin E-deficient macrophages

2009 ◽  
Vol 145 (5) ◽  
pp. 565-573 ◽  
Author(s):  
T. Tsukuba ◽  
M. Yanagawa ◽  
K. Okamoto ◽  
Y. Okamoto ◽  
Y. Yasuda ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Cathepsin E

scholarly journals Dynamic Monitoring of Cell Adhesion and Spreading on Microelectronic Sensor Arrays

2005 ◽  
Vol 10 (8) ◽  
pp. 795-805 ◽  
Author(s):  
Josephine M. Atienza ◽  
Jenny Zhu ◽  
Xiaobo Wang ◽  
Xiao Xu ◽  
Yama Abassi
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Real Time ◽  
Specific Interaction ◽  
Sensor Arrays ◽  
Dynamic Monitoring ◽  
Cellular Interaction ◽  
Cell Surface Receptors ◽  
Label Free ◽  
Surface Receptors

Cellular interaction with and adhesion on different biological surfaces is a dynamic and integrated process requiring the participation of specialized cell surface receptors, structural proteins, signaling proteins, and the cellular cytoskeleton. In this report, the authors describe a label-free and real-time method for measuring and monitoring cell adhesion on special microplates integrated with electronic cell sensor arrays. These plates were used in conjunction with the real-time cell electronic sensing (RT-CES™) system to dynamically and quantitatively monitor the specific interaction of fibroblasts with extracellular matrix (ECM) proteins and compared with standard adhesion techniques. Cell adhesion on ECM-coated cell sensor arrays is dependent on the concentration of ECMproteins coated and is inhibited by agents that disrupt the interaction of ECM with cell surface receptors. Furthermore, the authors demonstrate that the integrity of the actin cytoskeleton is required for productive cell adhesion and spreading on ECM-coated microelectronic sensors. Confirming earlier results, it is shown that interfering with Src expression or activity, via siRNA or small molecule, results in the disruption of adhesion and spreading of Bx PC3cells. The results indicate that the RT-CES system offers a convenient and quantitative means of assessing the kinetics of cell adhesion in a high-throughput manner.

scholarly journals The Ig Superfamily Cell Adhesion Molecule, apCAM, Mediates Growth Cone Steering by Substrate–Cytoskeletal Coupling

1998 ◽  
Vol 141 (1) ◽  
pp. 227-240 ◽  
Author(s):  
Daniel M. Suter ◽  
Laura D. Errante ◽  
Victoria Belotserkovsky ◽  
Paul Forscher
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Adhesion Molecule ◽  
Growth Cone ◽  
Cell Adhesion Molecule ◽  
Latency Period ◽  
Cytoplasmic Domain ◽  
Cell Surface Receptors ◽  
Vitro Assay ◽  
Surface Receptors

Dynamic cytoskeletal rearrangements are involved in neuronal growth cone motility and guidance. To investigate how cell surface receptors translate guidance cue recognition into these cytoskeletal changes, we developed a novel in vitro assay where beads, coated with antibodies to the immunoglobulin superfamily cell adhesion molecule apCAM or with purified native apCAM, replaced cellular substrates. These beads associated with retrograde F-actin flow, but in contrast to previous studies, were then physically restrained with a microneedle to simulate interactions with noncompliant cellular substrates. After a latency period of ∼10 min, we observed an abrupt increase in bead-restraining tension accompanied by direct extension of the microtubule-rich central domain toward sites of apCAM bead binding. Most importantly, we found that retrograde F-actin flow was attenuated only after restraining tension had increased and only in the bead interaction axis where preferential microtubule extension occurred. These cytoskeletal and structural changes are very similar to those reported for growth cone interactions with physiological targets. Immunolocalization using an antibody against the cytoplasmic domain of apCAM revealed accumulation of the transmembrane isoform of apCAM around bead-binding sites. Our results provide direct evidence for a mechanical continuum from apCAM bead substrates through the peripheral domain to the central cytoplasmic domain. By modulating functional linkage to the underlying actin cytoskeleton, cell surface receptors such as apCAM appear to enable the application of tensioning forces to extracellular substrates, providing a mechanism for transducing retrograde flow into guided growth cone movement.

Interactions of VEGF isoforms with VEGFR-1, VEGFR-2, and neuropilin in vivo: a computational model of human skeletal muscle

2007 ◽  
Vol 292 (1) ◽  
pp. H459-H474 ◽  
Author(s):  
Feilim Mac Gabhann ◽  
Aleksander S. Popel
Keyword(s):  
Skeletal Muscle ◽  
Extracellular Matrix ◽  
Cell Surface ◽  
Computational Model ◽  
Receptor Activation ◽  
Cell Surface Receptors ◽  
Vastus Lateralis Muscle ◽  
Surface Receptors ◽  
Vegf Isoforms

The vascular endothelial growth factor (VEGF) family of cytokines is involved in the maintenance of existing adult blood vessels as well as in angiogenesis, the sprouting of new vessels. To study the proangiogenic activation of VEGF receptors (VEGFRs) by VEGF family members in skeletal muscle, we develop a computational model of VEGF isoforms (VEGF121, VEGF165), their cell surface receptors, and the extracellular matrix in in vivo tissue. We build upon our validated model of the biochemical interactions between VEGF isoforms and receptor tyrosine kinases (VEGFR-1 and VEGFR-2) and nonsignaling neuropilin-1 coreceptors in vitro. The model is general and could be applied to any tissue; here we apply the model to simulate the transport of VEGF isoforms in human vastus lateralis muscle, which is extensively studied in physiological experiments. The simulations predict the distribution of VEGF isoforms in resting (nonexercising) muscle and the activation of VEGFR signaling. Little of the VEGF protein in muscle is present as free, unbound extracellular cytokine; the majority is bound to the cell surface receptors or to the extracellular matrix. However, interstitial sequestration of VEGF165 does not affect steady-state receptor binding. In the absence of neuropilin, VEGF121 and VEGF165 behave similarly, but neuropilin enhances the binding of VEGF165 to VEGFR-2. This model is the first to study VEGF tissue distribution and receptor activation in human muscle, and it provides a platform for the design and evaluation of therapeutic approaches.

scholarly journals Tyrosine phosphorylation of CD6 by stimulation of CD3: augmentation by the CD4 and CD2 coreceptors.

1993 ◽  
Vol 177 (1) ◽  
pp. 219-223 ◽  
Author(s):  
S Wee ◽  
G L Schieven ◽  
J M Kirihara ◽  
T T Tsu ◽  
J A Ledbetter ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Cell Surface ◽  
T Cell Activation ◽  
Intracellular Signaling ◽  
Cell Activation ◽  
Cell Receptor ◽  
Surface Proteins ◽  
Cell Surface Receptors ◽  
Surface Receptors

When T cells are activated via the T cell receptor (TCR) complex a number of cellular substrates, including some cell surface proteins, become phosphorylated on tyrosine (Tyr) residues. Phosphorylation of cytoplasmic Tyr renders these cell surface receptors competent to interact with proteins that link cell surface receptors to protein in the intracellular signaling pathways. Here we show that Tyr residues in the cytoplasmic domain of CD6 become phosphorylated upon T cell activation via the TCR complex. Tyr phosphorylation was observed when the T cells were activated by crosslinking CD3 or by cocrosslinking CD3 with CD2 or CD4, but not when the cells were stimulated by crosslinking CD2, CD4, or CD28 alone. Unlike other Tyr kinase substrates, such as the phospholipase C gamma 1-associated pp35/36 protein, whose level of Tyr phosphorylation is highest when T cells are activated by cocrosslinking CD3 with CD2, the levels of CD6 Tyr phosphorylation are highest when T cells were activated by cocrosslinking CD3 with CD4.

Sign in / Sign up

Export Citation Format

Share Document