DOCSLIB.ORG

Renal Ischemia/Reperfusion Injury: Functional Tissue Preservation by Anti-Activated ␤1 Integrin Therapy

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Renal Ischemia/Reperfusion Injury: Functional Tissue Preservation by Anti-Activated ␤1 Integrin Therapy Renal Ischemia/Reperfusion Injury: Functional Tissue Preservation by Anti-Activated ␤1 Integrin Therapy Ana Molina,* Marı´a Ubeda,* Marı´a M. Escribese,* Laura Garcı´a-Bermejo,* David Sancho,† ʈ Guillermo Pe´rez de Lema,‡ Fernando Lian˜o,§ Carlos Caban˜as, Francisco Sa´nchez-Madrid,† and Francisco Mampaso* *Department of Pathology, Hospital Ramo´n y Cajal, Universidad de Alcala´, Madrid, Spain; †Department of Immunology, Hospital de la Princesa, Universidad Auto´noma de Madrid, Madrid, Spain; ‡Medizinische Poliklinic der Ludwig Maximillians-Universitat, Munich, Germany; §Department of Nephrology, Hospital Ramo´n y Cajal, ʈ Universidad de Alcala´, Madrid, Spain; and Institute of Pharmacology and Toxicology (Centro Mixto CSIC-UCM), Facultad de Medicina, Universidad Complutense, Madrid, Spain Renal ischemia/reperfusion injury (IRI) is an important cause of acute renal failure. Cellular and molecular responses of the kidney to IRI are complex and not fully understood. ␤1 integrins localize to the basal surface of tubular epithelium interacting with extracellular matrix components of the basal membrane, including collagen IV. Whether preservation of tubular epithelium integrity could be a therapeutic approach for IRI was assessed. The effects of HUTS-21 mAb administration, which recognizes an activation-dependent epitope of ␤1 integrins, in a rat model of IRI were investigated. Preischemic HUTS-21 administration resulted in the preservation of renal functional and histopathologic parameters. Analyses of activated ␤1 integrins expression and focal adhesion kinase phosphorylation suggest that its deactivation after IRI was prevented by HUTS-21 treatment. Moreover, HUTS-21 impaired the inflammatory response in vivo, as indicated by inhibition of proin- flammatory mediators and the absence of infiltrating cells. Ex vivo adhesion assays using reperfused kidneys revealed that HUTS-21 induced a significant increase of epithelial cell attachment to collagen IV. In conclusion, the data provide evidence that HUTS-21 has a protective effect in renal IRI, preventing tubular epithelial cell detachment by preserving activated ␤1 integrins functions. J Am Soc Nephrol 16: 374–382, 2005. doi: 10.1681/ASN.2004070528 schemia/reperfusion injury (IRI) is an important cause of the basement membrane (BM) (15). Recently, attention has fo- acute renal failure in native kidneys and allografts (1). cused on the role of ␤1 integrins in the loss of tubular cells and I Cellular and molecular responses of the kidney to acute tubular lumen occlusion by cellular debris during acute IRI (2). ischemic injury are complex and not fully understood (2–4). Using an in vitro model of renal epithelial cells that were Several studies have examined the role of leukocytes and their exposed to oxidative stress, it was demonstrated redistribution surface adhesion molecules in the pathogenesis of postischemic of the ␣3␤1 integrin-subunit from the basolateral to apical cell renal damage. Leukocyte adhesion molecules seem to facilitate membranes (16). Also, in an in vivo model of IRI, it has been polymorphonuclear neutrophils recruitment during reperfu- proposed that the decrease of ␤1 integrins on basal surfaces sion, being implicated as mediators of renal IRI (5,6). Comple- contributes to tubular epithelia detachment into the lumen. mentary studies using mAb, antisense oligonucleotides, or Such observations provide a potential mechanism to explain ␤ gene “knockout” indicate that blockade of 2 integrins and/or tubular obstruction and backleak of glomerular filtrate after intercellular adhesion molecule-1 attenuates IRI in some exper- acute IRI (17). Administration of synthetic arginine-glycine- imental models (7–13). Furthermore, it was proposed recently aspartic acid peptides that block integrins ameliorates renal IRI, that T cells might also mediate IRI through the interaction with suggesting that arginine-glycine-aspartic acid peptides inhibit renal tubular epithelial cells (14). cell–cell adhesion in the tubular lumen, thus reducing intratu- ␤ In adult kidney, members of the 1 integrin subfamily are the bular obstruction (18–20). most common and localize to basal surfaces of tubular epithe- Integrin activation and deactivation are not fully understood lia, interacting with extracellular matrix (ECM) components of in in vivo processes. It is conceivable that after IR, ␤1 integrins, which are basally localized in the stressed tubular cells, are ␤ Received July 6, 2004. Accepted October 15, 2004. deactivated. Conversely, as a new epithelium reforms, 1 inte- grins again become activated and return to an exclusively basal Published online ahead of print. Publication date available at www.jasn.org. location. The state of integrin activation can be assessed by a Address correspondence to: Dr. Francisco Mampaso, Hospital Ramo´n y Cajal, group of mAb (HUTS) that selectively recognize ␤1 integrins in Departamento de Patologı´a, Carretera de Colmenar, Km 9.1, 28034 Madrid, Spain. Phone: 34-91-3368052; Fax: 34-91-3369016; E-mail: fmampaso.hrc@salud. their active form (21). In fact, an activated epitope has been madrid.org defined in the rat using the anti-human HUTS-21 mAb, which Copyright © 2005 by the American Society of Nephrology ISSN: 1046-6673/1602-0374 J Am Soc Nephrol 16: 374–382, 2005 ␤1 Integrin in Ischemia/Reperfusion Injury 375 recognizes ␤1 integrins on rat lymphocytes after activation with concentration was quantified by Bradford colorimetric assay (24). Equal ϩ ϩ divalent cations Mn2 and Hg2 . This mAb confers protective amount of proteins (30 ␮g) were separated by 10% SDS-PAGE and effects in an in vivo autoimmune nephritis model (22). immunoblotted onto polyvinylidene difluoride membranes (Bio-Rad, ␤ ␤ We assessed herein the effects of HUTS-21 systemic admin- Hercules, CA). 1 integrin expression was detected using anti- 1 anti- body (M-106; Santa Cruz) and ECL Western blotting detection system istration, infused before the renal artery clamp in an IRI rat (Amersham Pharmacia Biotech., Buckinghamshire, UK). Results were model. A single administration of this anti-activated ␤1 mAb expressed as percentage of ␤1 integrin expression of sham-operated rat resulted in the preservation of renal function and prevention of kidneys. tissue damage after ischemic insult. Quantitative Reverse Transcriptase–PCR Materials and Methods Total RNA was obtained from snap-frozen kidney tissue using the Animals Ultraspec RNA isolation system (Biotecx, Houston, TX). Two micro- Male Sprague-Dawley rats (IFFA-Credo, Paris, France) that weighed grams of DNaseI-treated RNA were reverse-transcribed with MuLV 180 to 200 g were used throughout the experiments. Animals were reverse transcriptase (Roche, Indianapolis, IN). mRNA expression was treated according to the institutional guidelines that are in compliance quantified by real-time PCR following the manufacturer’s instructions with the National Institutes of Health Guide for the Care and Use of (Lightcycler rapid thermal cycler; Roche) using the primers specific for Laboratory Animals. exon sequences (5Ј33Ј): ATG CCA TCC TGC GTC TGG ACC TGG C (␤-actin, sense), AGC ATT TGC GGT GCA CGA TGG C (␤-actin, Surgery and Experimental Protocol antisense), CAC CTC TCA AGC AGA GCA CAG (IL-1␤, sense), GGG Rats were anesthetized with an inhaled anesthesia mixture of isoflu- TTC CAT GGT GAA GTC AAC (IL-1␤, antisense), CCA GGA GAA rane 2% (Abbott Laboratories Ltd., Queenborough, Kent, England) and AGT CAG CCT CCT (TNF-␣, sense), TCA TAC CAG GGC TTG AGC oxygen 1 L/min and placed on a temperature-regulated table (39°C) to TCA (TNF␣, antisense), CCC TTC CGA AGT TTC TGG CAG CAG maintain body temperature. Renal ischemia was induced by clamping (inducible nitric oxide synthase [iNOS], sense), GGG CTC CTC CAA both renal pedicles during 45 min. Vehicle group (n ϭ 36), received an GGT GTT GCC C (iNOS-antisense). intravenous injection of phosphate buffer (pH 7.4) 5 min before clamp- ϭ ing. The HUTS-treated group (n 36) received a single intravenous Isolation of Proximal Tubular Epithelial Cells ␤ injection of 0.28 g/100 g body wt anti-activated 1 integrin HUTS-21 Proximal tubular epithelial cells (PTEC) were obtained from rat ϭ mAb (19) 5 min before clamping. The sham-operated group (n 8) kidney cortices that were subjected to 45 min of ischemia and3hof underwent the same surgical procedure, except that the clamp was not reperfusion or sham operation, following the process described by applied. Blood samples and kidneys were collected at different reper- Vinay et al. (25) with some modifications. Briefly, renal cortices were fusion times and processed for different studies. incubated in gassed Krebs-Henseleit saline (pH 7.4) that contained 0.1 mg/ml collagenase type I (Sigma, St. Louis, MO) at 37°C for1hand Functional and Histopathologic Studies sieved throughout 0.250- to 0.035-mm mesh. Cell populations were Serum creatinine was determined using a modified Jaffe’s reaction, separated by gradient centrifugation in 50% Percoll (Sigma) solution and blood urea nitrogen (BUN) was measured on the AEROSET System (Krebs-Henseleit saline:Percoll, 1:1, gassed for1honice). PTEC that (Abbott Laboratories, Abbott Park, IL). Kidneys were processed for were obtained from the appropriate band were immediately used for light microscopy examination according to standard procedures, and cell adhesion experiments. sections were stained with hematoxylin and eosin and periodic acid- Schiff. Histopathologic changes were analyzed for tubular epithelial Cell Adhesion Assay cell necrosis, tubular
Load more

Recommended publications
  • Hemidesmosomes and Focal Adhesions Treadmill As Separate but Linked Entities During Keratinocyte Migration Anne Pora1, Sungjun Yoon1, Reinhard Windoffer1 and Rudolf E
    ORIGINAL ARTICLE See related commentary on pg 1854 Hemidesmosomes and Focal Adhesions Treadmill as Separate but Linked Entities during Keratinocyte Migration Anne Pora1, Sungjun Yoon1, Reinhard Windoffer1 and Rudolf E. Leube1 Hemidesmosomes anchor the epidermal keratin filament cytoskeleton to the extracellular matrix. They are crucial for the mechanical integrity of skin. Their role in keratinocyte migration, however, remains unclear. Examining migrating primary human keratinocytes, we find that hemidesmosomes cluster as ordered arrays consisting of multiple chevrons that are flanked by actin-associated focal adhesions. These hemidesmosomal arrays with intercalated focal adhesions extend from the cell rear to the cell front. New hemidesmosomal chevrons form subsequent to focal adhesion assembly at the cell’s leading front, whereas chevrons and associated focal adhesions disassemble at the cell rear in reverse order. The bulk of the hemidesmosome-focal adhesion composite, however, remains attached to the substratum during cell translocation. Similar hemidesmosome-focal adhesion patterns emerge on X-shaped fibronectin-coated micropatterns, during cell spreading and in leader cells during collective cell migration. We further find that hemidesmosomes and focal adhesions affect each other’s distribution. We propose that both junctions are separate but linked entities, which treadmill coordinately to support efficient directed cell migration and cooperate to coordinate the dy- namic interplay between the keratin and actin cytoskeleton. Journal of Investigative Dermatology (2019) 139, 1876e1888; doi:10.1016/j.jid.2019.03.1139 INTRODUCTION are characterized by HD-specific a6/b4 integrin hetero- Epithelial cell migration is a key process in physiological dimers, which are connected through plakins to keratins situations, such as tissue morphogenesis, and in pathological (Nahidiazar et al., 2015).
    [Show full text]
  • Universidade Estadual De Campinas Faculdade De Ciências Médicas Carlos Vinícius Buarque De Gusmão Efeito Do Ultrassom, Ondas
    UNIVERSIDADE ESTADUAL DE CAMPINAS FACULDADE DE CIÊNCIAS MÉDICAS CARLOS VINÍCIUS BUARQUE DE GUSMÃO EFEITO DO ULTRASSOM, ONDAS DE CHOQUE E DE PRESSÃO RADIAL NO REPARO DE DEFEITOS ÓSSEOS NAS TÍBIAS DE RATOS AVALIADO PELA EXPRESSÃO E ATIVIDADE DE AKT, BMP-2, ERK-2, FAK E TGF-β1 EFFECT OF ULTRASOUND, EXTRACORPOREAL SHOCKWAVES AND RADIAL PRESSURE WAVES ON AKT, BMP-2, ERK-2, FAK AND TGF-β1 DURING BONE HEALING IN RAT TIBIAL DEFECTS CAMPINAS 2018 CARLOS VINÍCIUS BUARQUE DE GUSMÃO EFEITO DO ULTRASSOM, ONDAS DE CHOQUE E DE PRESSÃO RADIAL NO REPARO DE DEFEITOS ÓSSEOS NAS TÍBIAS DE RATOS AVALIADO PELA EXPRESSÃO E ATIVIDADE DE AKT, BMP-2, ERK-2, FAK E TGF-β1 EFFECT OF ULTRASOUND, EXTRACORPOREAL SHOCKWAVES AND RADIAL PRESSURE WAVES ON AKT, BMP-2, ERK-2, FAK AND TGF-β1 DURING BONE HEALING IN RAT TIBIAL DEFECTS Tese apresentada à Faculdade de Ciências Médicas da Universidade Estadual de Campinas como parte dos requisitos exigidos para a obtenção do título de Doutor em Ciências. Thesis presented to the Faculty of Medical Sciences of the State University of Campinas as part of the requirements to obtain the title of Doctor in Sciences. ORIENTADOR: PROF. DR. WILLIAM DIAS BELANGERO ESTE EXEMPLAR CORRESPONDE À VERSÃO FINAL DA TESE DEFENDIDA PELO ALUNO CARLOS VINÍCIUS BUARQUE DE GUSMÃO, E ORIENTADO PELO PROF. DR. WILLIAM DIAS BELANGERO. CAMPINAS 2018 Agência(s) de fomento e nº(s) de processo(s): CAPES, 02-P-3369/2017; FAPESP, 2014/26729-0 Ficha catalográfica Universidade Estadual de Campinas Biblioteca da Faculdade de Ciências Médicas Maristella Soares dos Santos - CRB 8/8402 Gusmão, Carlos Vinícius Buarque de, 1986- G972e Efeito do ultrassom, ondas de choque e de pressão radial no reparo de defeitos ósseos nas tíbias de ratos avaliado pela expressão e atividade de Akt, BMP-2, ERK-2, FAK e TGF-b1 / Carlos Vinícius Buarque de Gusmão.
    [Show full text]
  • Nomina Histologica Veterinaria, First Edition
    NOMINA HISTOLOGICA VETERINARIA Submitted by the International Committee on Veterinary Histological Nomenclature (ICVHN) to the World Association of Veterinary Anatomists Published on the website of the World Association of Veterinary Anatomists www.wava-amav.org 2017 CONTENTS Introduction i Principles of term construction in N.H.V. iii Cytologia – Cytology 1 Textus epithelialis – Epithelial tissue 10 Textus connectivus – Connective tissue 13 Sanguis et Lympha – Blood and Lymph 17 Textus muscularis – Muscle tissue 19 Textus nervosus – Nerve tissue 20 Splanchnologia – Viscera 23 Systema digestorium – Digestive system 24 Systema respiratorium – Respiratory system 32 Systema urinarium – Urinary system 35 Organa genitalia masculina – Male genital system 38 Organa genitalia feminina – Female genital system 42 Systema endocrinum – Endocrine system 45 Systema cardiovasculare et lymphaticum [Angiologia] – Cardiovascular and lymphatic system 47 Systema nervosum – Nervous system 52 Receptores sensorii et Organa sensuum – Sensory receptors and Sense organs 58 Integumentum – Integument 64 INTRODUCTION The preparations leading to the publication of the present first edition of the Nomina Histologica Veterinaria has a long history spanning more than 50 years. Under the auspices of the World Association of Veterinary Anatomists (W.A.V.A.), the International Committee on Veterinary Anatomical Nomenclature (I.C.V.A.N.) appointed in Giessen, 1965, a Subcommittee on Histology and Embryology which started a working relation with the Subcommittee on Histology of the former International Anatomical Nomenclature Committee. In Mexico City, 1971, this Subcommittee presented a document entitled Nomina Histologica Veterinaria: A Working Draft as a basis for the continued work of the newly-appointed Subcommittee on Histological Nomenclature. This resulted in the editing of the Nomina Histologica Veterinaria: A Working Draft II (Toulouse, 1974), followed by preparations for publication of a Nomina Histologica Veterinaria.
    [Show full text]
  • Molecular Organization of the Desmosome As Revealed by Direct Stochastic Optical Reconstruction Microscopy Sara N
    © 2016. Published by The Company of Biologists Ltd | Journal of Cell Science (2016) 129, 2897-2904 doi:10.1242/jcs.185785 SHORT REPORT Molecular organization of the desmosome as revealed by direct stochastic optical reconstruction microscopy Sara N. Stahley1, Emily I. Bartle1, Claire E. Atkinson2, Andrew P. Kowalczyk1,3 and Alexa L. Mattheyses1,* ABSTRACT plakoglobin and plakophilin, and the plakin family member Desmosomes are macromolecular junctions responsible for providing desmoplakin contribute to the intracellular plaque (Fig. 1A). strong cell–cell adhesion. Because of their size and molecular Plaque ultrastructure is characterized by two electron-dense complexity, the precise ultrastructural organization of desmosomes regions: the plasma-membrane-proximal outer dense plaque and is challenging to study. Here, we used direct stochastic optical the inner dense plaque (Desai et al., 2009; Farquhar and Palade, reconstruction microscopy (dSTORM) to resolve individual plaque 1963; Stokes, 2007). The cadherin cytoplasmic tails bind to proteins pairs for inner and outer dense plaque proteins. Analysis methods in the outer dense plaque whereas the C-terminus of desmoplakin based on desmosomal mirror symmetry were developed to measure binds to intermediate filaments in the inner dense plaque. This plaque-to-plaque distances and create an integrated map. We tethers the desmosome to the intermediate filament cytoskeleton, quantified the organization of desmoglein 3, plakoglobin and establishing an integrated adhesive network (Bornslaeger et al., desmoplakin (N-terminal, rod and C-terminal domains) in primary 1996; Harmon and Green, 2013). human keratinocytes. Longer desmosome lengths correlated with Many desmosomal protein interactions have been characterized increasing plaque-to-plaque distance, suggesting that desmoplakin is by biochemical studies (Bass-Zubek and Green, 2007; Green and arranged with its long axis at an angle within the plaque.
    [Show full text]
  • Loss of Mouse Cardiomyocyte Talin-1 and Talin-2 Leads to Β-1 Integrin
    Loss of mouse cardiomyocyte talin-1 and talin-2 leads PNAS PLUS to β-1 integrin reduction, costameric instability, and dilated cardiomyopathy Ana Maria Mansoa,b,1, Hideshi Okadaa,b, Francesca M. Sakamotoa, Emily Morenoa, Susan J. Monkleyc, Ruixia Lia, David R. Critchleyc, and Robert S. Rossa,b,1 aDivision of Cardiology, Department of Medicine, University of California at San Diego School of Medicine, La Jolla, CA 92093; bCardiology Section, Department of Medicine, Veterans Administration Healthcare, San Diego, CA 92161; and cDepartment of Molecular Cell Biology, University of Leicester, Leicester LE1 9HN, United Kingdom Edited by Kevin P. Campbell, Howard Hughes Medical Institute, University of Iowa, Iowa City, IA, and approved May 30, 2017 (received for review January 26, 2017) Continuous contraction–relaxation cycles of the heart require ognized as key mechanotransducers, converting mechanical per- strong and stable connections of cardiac myocytes (CMs) with turbations to biochemical signals (5, 6). the extracellular matrix (ECM) to preserve sarcolemmal integrity. The complex of proteins organized by integrins has been most CM attachment to the ECM is mediated by integrin complexes commonly termed focal adhesions (FA) by studies performed in localized at the muscle adhesion sites termed costameres. The cells such as fibroblasts in a 2D environment. It is recognized that ubiquitously expressed cytoskeletal protein talin (Tln) is a compo- this structure is important for organizing and regulating the me- nent of muscle costameres that links integrins ultimately to the chanical and signaling events that occur upon cellular adhesion to sarcomere. There are two talin genes, Tln1 and Tln2. Here, we ECM (7, 8).
    [Show full text]
  • Regulation of Keratin Filament Network Dynamics
    Regulation of keratin filament network dynamics Von der Fakultät für Mathematik, Informatik und Naturwissenschaften der RWTH Aachen University zur Erlangung des akademischen Grades eines Doktors der Naturwissenschaften genehmigte Dissertation vorgelegt von Diplom Biologe Marcin Maciej Moch aus Dzierżoniów (früher Reichenbach, NS), Polen Berichter: Universitätsprofessor Dr. med. Rudolf E. Leube Universitätsprofessor Dr. phil. nat. Gabriele Pradel Tag der mündlichen Prüfung: 19. Juni 2015 Diese Dissertation ist auf den Internetseiten der Hochschulbibliothek online verfügbar. This work was performed at the Institute for Molecular and Cellular Anatomy at University Hospital RWTH Aachen by the mentorship of Prof. Dr. med. Rudolf E. Leube. It was exclusively performed by myself, unless otherwise stated in the text. 1. Reviewer: Univ.-Prof. Dr. med. Rudolf E. Leube 2. Reviewer: Univ.-Prof. Dr. phil. nat. Gabriele Pradel Ulm, 15.02.2015 2 Publications Publications Measuring the regulation of keratin filament network dynamics. Moch M, and Herberich G, Aach T, Leube RE, Windoffer R. 2013. Proc Natl Acad Sci U S A. 110:10664-10669. Intermediate filaments and the regulation of focal adhesion. Leube RE, Moch M, Windoffer R. 2015. Current Opinion in Cell Biology. 32:13–20. "Panta rhei": Perpetual cycling of the keratin cytoskeleton. Leube RE, Moch M, Kölsch A, Windoffer R. 2011. Bioarchitecture. 1:39-44. Intracellular motility of intermediate filaments. Leube RE, Moch M, Windoffer R. Under review in: The Cytoskeleton. Editors: Pollard T., Dutcher S., Goldman R. Cold Springer Harbor Laboratory Press, Cold Spring Harbor. Multidimensional monitoring of keratin filaments in cultured cells and in tissues. Schwarz N, and Moch M, Windoffer R, Leube RE.
    [Show full text]
  • Limits of Extracellular Matrix Geometry for Spreading and Adhesion
    Research Article 41 Cell behaviour on micropatterned substrata: limits of extracellular matrix geometry for spreading and adhesion Dirk Lehnert1, Bernhard Wehrle-Haller2, Christian David3, Ulrich Weiland1, Christoph Ballestrem2, Beat A. Imhof2 and Martin Bastmeyer1,* 1 Department of Biology, University of Konstanz, Universitaetstrasse 10, 78457 Konstanz, Germany 2Department of Pathology, Centre Medical Universitaire, Geneva, Switzerland 3Laboratory for Micro- and Nanotechnology, Paul Scherrer Institut, Villigen-PSI, Switzerland *Author for correspondence at present address: Friedrich-Schiller-Universität, Institut für Allgemeine Zoologie, Erbertstrasse 1, 07743 Jena, Germany (e-mail: [email protected]) Accepted 18 August 2003 Journal of Cell Science 117, 41-52 Published by The Company of Biologists 2004 doi:10.1242/jcs.00836 Summary Cell adhesion, spreading and migration require the migrate on dots ≥1 µm2 ceases when the dot separation is dynamic formation and dispersal of contacts with the ≥30 µm. The extent of cell spreading is directly correlated extracellular matrix (ECM). In vivo, the number, to the total substratum coverage with ECM-proteins, but availability and distribution of ECM binding sites dictate irrespective of the geometrical pattern. An optimal the shape of a cell and determine its mobility. To analyse spreading extent is reached at a surface coating above 15%. the geometrical limits of ECM binding sites required for Knowledge of these geometrical limits is essential for an cell attachment and spreading, we used microcontact understanding of cell adhesion and migration, and for the printing to produce regular patterns of ECM protein dots design of artificial surfaces that optimally interact with of defined size separated by nonadhesive regions.
    [Show full text]
  • A Review of Cell Adhesion Studies for Biomedical and Biological Applications
    Int. J. Mol. Sci. 2015, 16, 18149-18184; doi:10.3390/ijms160818149 OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 www.mdpi.com/journal/ijms Review A Review of Cell Adhesion Studies for Biomedical and Biological Applications Amelia Ahmad Khalili 1 and Mohd Ridzuan Ahmad 1,2,* 1 Department of Control and Mechatronic Engineering, Faculty of Electrical Engineering, Universiti Teknologi Malaysia, Johor 81310, Malaysia; E-Mail: [email protected] 2 Institute of Ibnu Sina, Universiti Teknologi Malaysia, Johor 81310, Malaysia * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +607-553-6333; Fax: +607-556-6272. Academic Editor: Fan-Gang Tseng Received: 10 May 2015 / Accepted: 24 June 2015 / Published: 5 August 2015 Abstract: Cell adhesion is essential in cell communication and regulation, and is of fundamental importance in the development and maintenance of tissues. The mechanical interactions between a cell and its extracellular matrix (ECM) can influence and control cell behavior and function. The essential function of cell adhesion has created tremendous interests in developing methods for measuring and studying cell adhesion properties. The study of cell adhesion could be categorized into cell adhesion attachment and detachment events. The study of cell adhesion has been widely explored via both events for many important purposes in cellular biology, biomedical, and engineering fields. Cell adhesion attachment and detachment events could be further grouped into the cell
    [Show full text]
  • Uterine Focal Adhesions Are Retained at Implantation After Rat Ovarian Hyperstimulation
    REPRODUCTIONRESEARCH PROOF ONLY Uterine focal adhesions are retained at implantation after rat ovarian hyperstimulation Laura A Lindsay, Samson N Dowland and Christopher R Murphy School of Medical Sciences (Anatomy and Histology), The University of Sydney, Sydney, New South Wales, Australia Correspondence should be addressed to L A Lindsay; Email: [email protected] Abstract Controlled ovarian hyperstimulation is an essential component of IVF techniques to ensure proliferation and development of multiple ovarian follicles, but the effects of these hormones on the endometrium are largely unknown. During normal pregnancy in rats, there are significant changes in the basal plasma membrane of uterine epithelial cells (UECs) at the time of receptivity, including loss of focal adhesions. This enables the UECs to be removed from the implantation chamber surrounding the blastocyst, thus allowing invasion into the underlying stroma. This study investigated the influence of ovarian hyperstimulation (OH) on the basal plasma membrane of UECs during early pregnancy in the rat. Immunofluorescence results demonstrate the presence of paxillin, talin, integrin β1 and phosphorylated FAK (Y397FAK) in the basal portion of UECs at the time of implantation in OH pregnancy. TEM analysis demonstrated a flattened basal lamina and the presence of focal adhesions on the basal surface at this time in OH pregnancy. Significantly low full-length paxillin, high paxillinδ and integrin β1 were seen at the time of implantation in OH compared with those in normal pregnancy. The increase in paxillin δ suggests that these cells are less mobile, whereas the increase in integrin β1 and Y397FAK suggests the retention of a stable FA complex.
    [Show full text]
  • Diverse Cell Junctions with Unique Molecular Composition in Tissues of a Sponge (Porifera)
    bioRxiv preprint doi: https://doi.org/10.1101/685875; this version posted June 28, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Diverse cell junctions with unique molecular composition in tissues of a sponge (Porifera) Jennyfer M. Mitchell ab and Scott A. Nichols a1 a Department of Biological Sciences, 2101 E. Wesley Ave. SGM 203, University of Denver, Denver, CO 80208 b Current address: University of Colorado, Anschutz Medical Campus, 12801 E. 17th Ave. RC1S, 11501G, Aurora, CO 80045 1 Correspondence: [email protected] Abstract The integrity and organization of animal tissues depends upon specialized protein complexes that mediate adhesion between cells with each other (cadherin-based adherens junctions), and with the extracellular matrix (integrin-based focal adhesions). Reconstructing how and when these cell junctions evolved is central to understanding early tissue evolution in animals. We examined focal adhesion protein homologs in tissues of the freshwater sponge, Ephydatia muelleri (phylum Porifera). We found that sponge homologs of focal adhesion proteins co- precipitate as a complex and localize to cell junctions in sponge tissues. These data support that the adhesion roles of these proteins evolved early, prior to the divergence of sponges and other animals. However, in contrast to the spatially partitioned distribution of cell junctions in epithelia of other animals, focal adhesion proteins were found to be co-distributed with the adherens junction protein Emβ-catenin in sponge tissues; both at certain cell-cell and cell- extracellular matrix (ECM) adhesions.
    [Show full text]
  • Cell Adhesion and Its Endocytic Regulation in Cell Migration During Neural Development and Cancer Metastasis
    Int. J. Mol. Sci. 2012, 13, 4564-4590; doi:10.3390/ijms13044564 OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 www.mdpi.com/journal/ijms Review Cell Adhesion and Its Endocytic Regulation in Cell Migration during Neural Development and Cancer Metastasis Takeshi Kawauchi 1,2 1 Precursory Research for Embryonic Science and Technology (PRESTO), Japan Science and Technology Agency (JST), Saitama 332-0012, Japan; E-Mail: [email protected]; Tel.: +81-3-5363-3743; Fax: +81-3-5379-1977 2 Department of Anatomy, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan Received: 7 February 2012; in revised form: 23 March 2012/ Accepted: 26 March 2012 / Published: 11 April 2012 Abstract: Cell migration is a crucial event for tissue organization during development, and its dysregulation leads to several diseases, including cancer. Cells exhibit various types of migration, such as single mesenchymal or amoeboid migration, collective migration and scaffold cell-dependent migration. The migration properties are partly dictated by cell adhesion and its endocytic regulation. While an epithelial-mesenchymal transition (EMT)-mediated mesenchymal cell migration requires the endocytic recycling of integrin-mediated adhesions after the disruption of cell-cell adhesions, an amoeboid migration is not dependent on any adhesions to extracellular matrix (ECM) or neighboring cells. In contrast, a collective migration is mediated by both cell-cell and cell-ECM adhesions, and a scaffold cell-dependent migration is regulated by the endocytosis and recycling of cell-cell adhesion molecules. Although some invasive carcinoma cells exhibit an EMT-mediated mesenchymal or amoeboid migration, other cancer cells are known to maintain cadherin-based cell-cell adhesions and epithelial morphology during metastasis.
    [Show full text]
  • (Cell Junctions). II. Cell-Matrix Adhesion. III.Components of the Extracellular Matrix. Epithelial Cells Trans-Well System
    Outline: Cell-Cell and Cell-ECM Interaction -Integration from cells to tissues- I. Cell-Cell Adhesion (cell Junctions). II. Cell-Matrix Adhesion. III.Components of the extracellular Matrix. Yi-Ping Hsueh 2019 Trans-Well system Epithelial cells 1. Epithelial cells 2. Cell migration 1 Cell junctions: Epithelial cells Cell junctions link to cytoskeletons Tight Junctions Tight junctions and adherens junctions are linked to the actin Freeze-fracture EM cytoskeleton, and desmosomes and hemidesmosomes are linked to intermediate filaments. a major constituent of TJ strands Claudins with molecular masses of ~23 kD comprise a multigene family consisting of 24 members in mice/humans. 2 Tight junctions: 1. To seal off body cavities 2. To restrict diffusion of membrane components. 3. To maintain blood-brain barrier. Capillary Intestinal lumen Epithelial cells Epithelial Basal lamina Current Biology Dec, 2011, Vol. 21, Featured video The composition of tight junctions. Assembly of epithelial tight junctions and regulation of proliferation and differentiation. aPKC, atypical protein kinase C; huASH1, human ZO-1: absent, small or homeotic discs 1; JAMs, junctional adhesion molecules; MAGI, •Tight junction associated Membrane-associated MAGUK guanylate kinase inverted; MUPP1, multi-PDZ domain protein 1; Pals1, Protein •In confluent epithelial associated with Lin-7 1; culture, ZO-1 is restricted PAR, Partitioning defective; PATJ, Pals1- at the junction. In associated tight junction subconfluent culture, ZO1 protein; PP2A, protein is present in the nuclei. phosphatase 2A; PTEN, phosphatase and tensin homologue; ZO, zonula •ZO-1 interacts with a Y- occludens; ZONAB, ZO-1- box transcription factor associated nucleic-acid ZONAB and regulates binding. EGFR member ErbB2, which is critical for regulation of epithelial cell Some of the components that are thought to become recruited to TJs do not localize proliferation.
    [Show full text]