scholarly journals Integrins: An Important Link between Angiogenesis, Inflammation and Eye Diseases

Cells ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1703
Author(s):  
Małgorzata Mrugacz ◽  
Anna Bryl ◽  
Mariusz Falkowski ◽  
Katarzyna Zorena
Keyword(s):  
Cell Adhesion ◽  
Tissue Repair ◽  
Normal Development ◽  
Cell Attachment ◽  
Biological Activities ◽  
Integrin Receptors ◽  
Cytokine Activation ◽  
Eye Disorders ◽  
Membrane Bound ◽  
Cell To Cell Adhesion

Integrins belong to a group of cell adhesion molecules (CAMs) which is a large group of membrane-bound proteins. They are responsible for cell attachment to the extracellular matrix (ECM) and signal transduction from the ECM to the cells. Integrins take part in many other biological activities, such as extravasation, cell-to-cell adhesion, migration, cytokine activation and release, and act as receptors for some viruses, including severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2). They play a pivotal role in cell proliferation, migration, apoptosis, tissue repair and are involved in the processes that are crucial to infection, inflammation and angiogenesis. Integrins have an important part in normal development and tissue homeostasis, and also in the development of pathological processes in the eye. This review presents the available evidence from human and animal research into integrin structure, classification, function and their role in inflammation, infection and angiogenesis in ocular diseases. Integrin receptors and ligands are clinically interesting and may be promising as new therapeutic targets in the treatment of some eye disorders.

Imatinib Mesilate Modifies Genes Involved in Hematopoiesis in Non Clonal Bone Marrow Cells from CML Patients in Complete Cytogenetic Response.

Blood ◽  
2007 ◽  
Vol 110 (11) ◽  
pp. 2947-2947
Author(s):  
Fermin M. Sanchez-Guijo ◽  
Eva Lumbreras ◽  
Patricia Morais ◽  
Juan-Luis Garcia ◽  
Norma C. Gutierrez ◽  
...  
Keyword(s):  
Gene Expression ◽  
Bone Marrow ◽  
Cell Adhesion ◽  
Mapk Pathway ◽  
Biological Activities ◽  
Chronic Phase ◽  
Long Term Treatment ◽  
Wide Range ◽  
Cell To Cell Adhesion ◽  
Imatinib Mesilate

Abstract Imatinib mesilate (IM) is the standard treatment for newly diagnosed patients with chronic phase (CP) CML. Bcr-Abl signaling has a wide range of biological activities, mainly mediated through activation of Ras/mitogen-activated protein kinase (MAPK) pathways, with broad effects on changes in cell adhesion (through Rho), proliferation (MAPK pathway) and apoptosis (through Akt). IM’s efficacy results from a blockade of these effects. Extensive work on the gene-expression profiling of CML cell lines under IM therapy has been published in order to predict disease transformation or IM resistance. Nevertheless, information on the effects of IM on the residual non clonal bone marrow (BM) hematopoietic compartment is scarce, and this is an important issue, since most responding patients will require long term treatment with IM. Therefore, in the present work we have assessed the gene expression profile (GEP) of whole BM hematopoietic cells from 20 patients with CP-CML in CCR after 6 to 12 months on IM therapy and compared it with that of 6 normal BM donors. Total RNA (100-500 ng) was amplified and labeled using the “GeneChip Two-Cycle cDNA Synthesis Kit” and hybridized to “Human Genome U133A” microarray (Affymetrix). Processing of genechip data was carried out using the Robust Multi-chip Average (RMA) and the Affymetrix Microarray Suite v.5 (MAS5) gene expression algorithms. The Significance Analysis of Microarrays (SAM) algorithm identified gene expression changes in a total of 490 genes (125 up and 365 down-regulated) when samples from CCR CML patients were compared to normal BM samples. Differential genes were grouped in 4 different areas, based on their function: proliferation, apoptosis, ubiquitination and adhesion. In CCR CML samples, there was a lower expression of genes involved in cell proliferation (e.g. C6ORF108, CENPE, CENP5, ESPL1 or GAS6) and cell cycle progression (e.g. PLCB1, ZW10, CUL4A or FOSB). There was an upregulation of genes involved in the induction of apoptosis (e.g. CDC2L2, FOXO3A, ING2, ING3, RYBP or TNFRSF1B) and in the ubiquitination of proteins (e.g. ARIH1, FBXW7, RKHD2, RNF7, SUMO1, UBA2 or UBE2W). Regarding cell-to-cell adhesion, several genes involved in this processes were downregulated (e.g. ITGBL1, CTNNA1, PCDHGA1, TROAP, FLOT2, IGSF4B, SELP, SIGLEC6, ADAM22 and STAB1). In addition, in all CML samples the erythropoietin receptor (Epo-R) gene was downregulated. This is of interest since many patients on IM therapy display a slightly low Hb level, regardless of circulating Epo levels. In summary, IM induces a decrease in proliferation and increase in apoptosis and ubiquitination in residual non clonal BM cells from CCR CML patients. In addition, IM diminishes cell-to-cell adhesion and downregulates the expression of the Epo receptor in the hematopoietic compartment of these patients.

scholarly journals Laminin-6 Is Activated by Proteolytic Processing and Regulates Cellular Adhesion and Migration Differently from Laminin-5

2002 ◽  
Vol 277 (51) ◽  
pp. 49287-49295 ◽  
Author(s):  
Tomomi Hirosaki ◽  
Yoshiaki Tsubota ◽  
Yoshinobu Kariya ◽  
Kayano Moriyama ◽  
Hiroto Mizushima ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Attachment ◽  
Biological Activities ◽  
Cell Spreading ◽  
Cellular Adhesion ◽  
Binding Domain ◽  
Proteolytic Processing ◽  
Heparin Binding ◽  
Laminin 5 ◽  
Ht1080 Cells

Laminin-6 (LN6) and laminin-5 (LN5), which share the common integrin-binding domain in the laminin α3 chain, are thought to cooperatively regulate cellular functions, but the former has poorly been characterized. Human fibrosarcoma HT1080 cells expressing an exogenous α3 chain were found to secrete LN6 with the full-length α3 chain and a smaller amount of its processed form lacking the carboxyl-terminal G4-5 domain, besides mature LN5 without G4-5 (mat-LN5). We prepared the unprocessed LN6 and mat-LN5, as well as LN6 mutants without G4-5 (LN6ΔG4-5) or G5 (LN6ΔG5). These laminins supported attachment of HT1080 cells and human keratinocytes (HaCaT) through integrins α3β1and/or α6β1. LN6ΔG4-5, LN6ΔG5, and mat-LN5 promoted rapid cell spreading, whereas LN6 did hardly. A purified G4-5 fragment of the laminin α3 chain supported cell attachment through interaction with heparan sulfate proteoglycans and promoted cell spreading in combination with mat-LN5 or LN6ΔG4-5. These results imply that the G4-5 domain within the LN6 molecule suppresses cell adhesion, while the released G4-5 promotes it. The presence of G5 rather than the heparin-binding domain G4 was responsible for the impaired cell spreading activity of LN6. However, the unprocessed LN6 promoted cell spreading in the presence of mat-LN5. Unlike mat-LN5, both LN6ΔG4-5 and LN6 did weakly or did not stimulate cell motility. These findings demonstrate that LN6 and LN5 have distinct biological activities, but they may cooperatively support cell adhesion. The proteolytic processing of the α3 chain seems to regulate the physiological functions of LN6.

ROCK2 Regulates the Expression of Cell Adhesion Molecules and Cell-to-Cell Adhesion in Vascular Endothelial Cells

Diabetes ◽  
2018 ◽  
Vol 67 (Supplement 1) ◽  
pp. 476-P
Author(s):  
YUSUKE TAKEDA ◽  
KEIICHIRO MATOBA ◽  
DAIJI KAWANAMI ◽  
YOSUKE NAGAI ◽  
TOMOYO AKAMINE ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Adhesion ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Cell To Cell Adhesion

scholarly journals Differences in a Single Extracellular Residue Underlie Adhesive Functions of Two Zebrafish Aqp0s

Cells ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 2005
Author(s):  
Irene Vorontsova ◽  
James E. Hall ◽  
Thomas F. Schilling ◽  
Noriaki Nagai ◽  
Yosuke Nakazawa
Keyword(s):  
Cell Adhesion ◽  
Single Amino Acid ◽  
Amino Acid Difference ◽  
Adhesion Assay ◽  
Loss Of Function ◽  
Adhesive Properties ◽  
The Difference ◽  
In Vitro Adhesion ◽  
Cell To Cell Adhesion

Aquaporin 0 (AQP0) is the most abundant lens membrane protein, and loss of function in human and animal models leads to cataract formation. AQP0 has several functions in the lens including water transport and adhesion. Since lens optics rely on strict tissue architecture achieved by compact cell-to-cell adhesion between lens fiber cells, understanding how AQP0 contributes to adhesion would shed light on normal lens physiology and pathophysiology. We show in an in vitro adhesion assay that one of two closely related zebrafish Aqp0s, Aqp0b, has strong auto-adhesive properties while Aqp0a does not. The difference appears to be largely due to a single amino acid difference at residue 110 in the extracellular C-loop, which is T in Aqp0a and N in Aqp0b. Similarly, P110 is the key residue required for adhesion in mammalian AQP0, highlighting the importance of residue 110 in AQP0 cell-to-cell adhesion in vertebrate lenses as well as the divergence of adhesive and water permeability functions in zebrafish duplicates.

Quantitative Studies of Fibronectin Adsorption on Submicron Scaffolds

2012 ◽  
Author(s):  
Shawn Regis ◽  
Manisha Jassal ◽  
Sina Youssefian ◽  
Nima Rahbar ◽  
Sankha Bhowmick
Keyword(s):  
Surface Functionalization ◽  
Cultured Cells ◽  
Cell Attachment ◽  
Md Simulations ◽  
Cell Types ◽  
Biological Processes ◽  
Integrin Receptors ◽  
Tissue Engineering Scaffolds ◽  
Quantitative Studies

Fibronectin plays a crucial role in adhesion of several cell types, mainly due to the fact that it is recognized by at least ten different integrin receptors. Since most cell types can bind to fibronectin, it becomes involved in many various biological processes. The interaction of cells with ECM proteins such as fibronectin provides the signals affecting morphology, motility, gene expression, and survival of cells [1]. Fibronectin exists in both soluble and insoluble forms; soluble fibronectin is secreted by cells and exits in cell media or body fluids, whereas insoluble fibronectin exists in tissues or the extracellular matrix of cultured cells [2]. The ability to control adsorption of fibronectin on tissue engineering scaffolds would therefore play a huge role in controlling cell attachment and survival in vivo. This can be achieved through surface functionalization of the scaffolds. The goal of these studies is to use molecular dynamics (MD) simulations to mechanistically understand how fibronectin adsorption is enhanced by surface functionalization of submicron scaffolds.

Regulation of epithelial and lymphocyte cell adhesion by adenosine deaminase–CD26 interaction

2002 ◽  
Vol 361 (2) ◽  
pp. 203-209 ◽  
Author(s):  
Silvia GINÉS ◽  
Marta MARIÑO ◽  
Josefa MALLOL ◽  
Enric I. CANELA ◽  
Chikao MORIMOTO ◽  
...  
Keyword(s):  
T Cells ◽  
Cell Adhesion ◽  
T Cell ◽  
B Cells ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Cell Surface ◽  
Adenosine Deaminase ◽  
Cell To Cell Adhesion ◽  
Lymphocyte Cell

The extra-enzymic function of cell-surface adenosine deaminase (ADA), an enzyme mainly localized in the cytosol but also found on the cell surface of monocytes, B cells and T cells, has lately been the subject of numerous studies. Cell-surface ADA is able to transduce co-stimulatory signals in T cells via its interaction with CD26, an integral membrane protein that acts as ADA-binding protein. The aim of the present study was to explore whether ADA—CD26 interaction plays a role in the adhesion of lymphocyte cells to human epithelial cells. To meet this aim, different lymphocyte cell lines (Jurkat and CEM T) expressing endogenous, or overexpressing human, CD26 protein were tested in adhesion assays to monolayers of colon adenocarcinoma human epithelial cells, Caco-2, which express high levels of cell-surface ADA. Interestingly, the adhesion of Jurkat and CEM T cells to a monolayer of Caco-2 cells was greatly dependent on CD26. An increase by 50% in the cell-to-cell adhesion was found in cells containing higher levels of CD26. Incubation with an anti-CD26 antibody raised against the ADA-binding site or with exogenous ADA resulted in a significant reduction (50–70%) of T-cell adhesion to monolayers of epithelial cells. The role of ADA—CD26 interaction in the lymphocyte—epithelial cell adhesion appears to be mediated by CD26 molecules that are not interacting with endogenous ADA (ADA-free CD26), since SKW6.4 (B cells) that express more cell-surface ADA showed lower adhesion than T cells. Adhesion stimulated by CD26 and ADA is mediated by T cell lymphocyte function-associated antigen. A role for ADA—CD26 interaction in cell-to-cell adhesion was confirmed further in integrin activation assays. FACS analysis revealed a higher expression of activated integrins on T cell lines in the presence of increasing amounts of exogenous ADA. Taken together, these results suggest that the ADA—CD26 interaction on the cell surface has a role in lymphocyte—epithelial cell adhesion.

Adhesion of Phytophthora palmivora zoospores: electron microscopy of cell attachment and cyst wall fibril formation

1975 ◽  
Vol 18 (1) ◽  
pp. 123-132
Author(s):  
V.O. Sing ◽  
S. Bartnicki-Garcia
Keyword(s):  
Electron Microscopy ◽  
Cell Adhesion ◽  
Cyst Wall ◽  
Cell Attachment ◽  
Sodium Dodecyl ◽  
Film Surface ◽  
Phytophthora Palmivora ◽  
Thin Sections ◽  
Electron Dense Deposit ◽  
Dense Deposit

Zoospores of Phytophthora palmivora adhered to a plastic film surface were examined by electron microscopy. Three stages of adhesion were compared: (1) non-adhesive, unencysted zoospores, (2) adhered incipient cysts, and (3) adhered mature cysts. Thin sections of incipient cysts revealed cells attached to the film surface through the partially discharged contents of the so-called peripheral vesicles; this seems to be the first step in cell adhesion. In mature cysts, the adhesive appeared to have been compacted into an electron-dense deposit binding the cyst wall to the plastic surface. The adhesion zone was also examined in face view after lysing attached incipient cysts with sodium dodecyl sulphate. Cyst wall microfibrils were seen together with an amorphous substance (presumably the adhesive material). The microfibrils were in various stages of formation. Seemingly, adhesion and microfibril formation take place concurrently. The possibility was considered that the material contained in the peripheral vesicles serves in both cell adhesion and microfibril elaboration.

Contrasting migratory response of astrocytoma cells to tenascin mediated by different integrins

1996 ◽  
Vol 109 (8) ◽  
pp. 2161-2168 ◽  
Author(s):  
A. Giese ◽  
M.A. Loo ◽  
S.A. Norman ◽  
S. Treasurywala ◽  
M.E. Berens
Keyword(s):  
Cell Adhesion ◽  
Matrix Protein ◽  
Glioma Cells ◽  
Extracellular Matrix Protein ◽  
Integrin Receptors ◽  
Migration Assay ◽  
Dose Dependent Fashion ◽  
Beta 1 Integrin

Tenascin, an extracellular matrix protein, is expressed in human gliomas in vitro and in vivo. The distribution of tenascin at the invasive edge of these tumors, even surrounding solitary invading cells, suggests a role for this protein as a regulator of glioma cell migration. We tested whether purified tenascin, passively deposited on surfaces, influenced the adhesion or migration of a human gliomaderived cell line, SF-767. Adhesion of glioma cells to tenascin increased in a dose-dependent fashion up to a coating concentration of 10 micrograms/ml. Higher coating concentrations resulted in progressively fewer cells attaching. Cell adhesion could be blocked to basal levels using anti-beta 1 integrin antibodies. In contrast, when anti-alpha v antibodies were added to the medium of cells on tenascin, cell adhesion was enhanced slightly. Using a microliter scale migration assay, we found that cell motility on tenascin was dose dependently stimulated at coating concentrations of 1 and 3 micrograms/ml, but migration was inhibited below levels of non-specific motility when tested at coating concentrations of 30 and 100 micrograms/ml. Migration on permissive concentrations of tenascin could be reversibly inhibited with anti-beta 1, while treatment with anti-alpha v antibodies increased migration rates. We conclude that SF-767 glioma cells express two separate integrin receptors that mediate contrasting adhesive and migratory responses to tenascin.

Abscission in agriculture

1984 ◽  
Vol 13 (2) ◽  
pp. 97-103 ◽  
Author(s):  
Daphne J. Osborne
Keyword(s):  
Cell Adhesion ◽  
Natural Process ◽  
Citrus Fruits ◽  
Biochemical Mechanisms ◽  
Cell To Cell Adhesion

Abscission—the natural process by which cell-to-cell adhesion is lost at specific points in plants—plays an important role in the maturing and harvesting of many crops. Understanding of the biochemical mechanisms involved makes control of the abscission process possible and this has been put to practical use in agriculture: for example, in harvesting citrus fruits.

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