scholarly journals What Molecular Recognition Systems Do Mesenchymal Stem Cells/Medicinal Signaling Cells (MSC) Use to Facilitate Cell-Cell and Cell Matrix Interactions? A Review of Evidence and Options

2021 ◽  
Vol 22 (16) ◽  
pp. 8637
Author(s):  
David A. Hart
Keyword(s):  
Stem Cells ◽  
Mesenchymal Stem Cells ◽  
Molecular Recognition ◽  
Tissue Repair ◽  
Bone Cells ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Recognition Systems ◽  
Cell Matrix Interactions

Mesenchymal stem cells, also called medicinal signaling cells (MSC), have been studied regarding their potential to facilitate tissue repair for >30 years. Such cells, derived from multiple tissues and species, are capable of differentiation to a number of lineages (chondrocytes, adipocytes, bone cells). However, MSC are believed to be quite heterogeneous with regard to several characteristics, and the large number of studies performed thus far have met with limited or restricted success. Thus, there is more to understand about these cells, including the molecular recognition systems that are used by these cells to perform their functions, to enhance the realization of their potential to effect tissue repair. This perspective article reviews what is known regarding the recognition systems available to MSC, the possible systems that could be looked for, and alternatives to enhance their localization to specific injury sites and increase their subsequent facilitation of tissue repair. MSC are reported to express recognition molecules of the integrin family. However, there are a number of other recognition molecules that also could be involved such as lectins, inducible lectins, or even a MSC-specific family of molecules unique to these cells. Finally, it may be possible to engineer expression of recognition molecules on the surface of MSC to enhance their function in vivo artificially. Thus, improved understanding of recognition molecules on MSC could further their success in fostering tissue repair.

Cell-Matrix Interactions Modulate Mesenchymal Stem Cell Response to Dynamic Compression

2011 ◽  
Author(s):  
Stephen D. Thorpe ◽  
Conor T. Buckley ◽  
Andrew J. Steward ◽  
Daniel J. Kelly
Keyword(s):  
Stem Cells ◽  
Mesenchymal Stem Cells ◽  
Stem Cell ◽  
Growth Factors ◽  
Chondrogenic Differentiation ◽  
Dynamic Compression ◽  
Compressive Loading ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Cell Matrix Interactions

Unconfined cyclic compressive loading has been shown to promote the chondrogenic differentiation of agarose encapsulated mesenchymal stem cells (MSCs) in the absence of chondrogenic growth factors [1, 2]. However, in general robust chondrogenesis has not been reported as a result of mechanical stimulation alone; with biochemical stimulation through TGF-β supplementation yielding a more potent pro-chondrogenic effect [2, 3].

Collagen structure regulates MSCs behavior by MMPs involved cell–matrix interactions

2018 ◽  
Vol 6 (2) ◽  
pp. 312-326 ◽  
Author(s):  
Yilu Ni ◽  
Zhurong Tang ◽  
Jirong Yang ◽  
Yongli Gao ◽  
Hai Lin ◽  
...  
Keyword(s):  
Stem Cells ◽  
Mesenchymal Stem Cells ◽  
Collagen Structure ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Cell Matrix Interactions

Various scaffolds have been studied in the formation of cell niches and regulation of mesenchymal stem cells (MSCs) behaviors.

Different mechanisms in the attachment of cells to native and denatured collagen

1979 ◽  
Vol 38 (1) ◽  
pp. 267-281
Author(s):  
S.L. Schor ◽  
J. Court
Keyword(s):  
Cell Attachment ◽  
Experimental Conditions ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Independent Mechanism ◽  
Cell Matrix Interactions ◽  
Serum Dependent ◽  
Kinetics Of ◽  
Dependent Mechanism

The attachment of cells to collagen has been reported previously to require the presence of serum and the particular serum protein involved in this process, variously known as CIG, CAP or fibronectin, has been isolated. This conclusion that cell attachment to collagen requires serum (or more precisely, fibronectin) is based on experiments measuring the kinetics of cell attachment to films of collagen. We have measured the kinetics of attachment of HeLa and attachment to films of collagen-containing substrata under a variety of experimental conditions and present evidence that the serum-dependent mechanism of cell attachment described by others is actually only the case for films of denatured collagen, while cell attachment to native collagen fibres occurs by a different, serum-independent, mechanism. The possible relevance of these findings to cell-matrix interactions in vivo is discussed.

scholarly journals Fatal Bilateral Chylothorax in Mice Lacking the Integrin α9β1

2000 ◽  
Vol 20 (14) ◽  
pp. 5208-5215 ◽  
Author(s):  
X. Z. Huang ◽  
J. F. Wu ◽  
R. Ferrando ◽  
J. H. Lee ◽  
Y. L. Wang ◽  
...  
Keyword(s):  
Respiratory Failure ◽  
Thoracic Duct ◽  
Lymphocytic Infiltration ◽  
Cell Matrix ◽  
Bilateral Chylothorax ◽  
Matrix Interactions ◽  
Congenital Chylothorax ◽  
Cell Matrix Interactions ◽  
Cell Adhesion Molecule 1

ABSTRACT Members of the integrin family of adhesion receptors mediate both cell-cell and cell-matrix interactions and have been shown to play vital roles in embryonic development, wound healing, metastasis, and other biological processes. The integrin α9β1 is a receptor for the extracellular matrix proteins osteopontin and tenacsin C and the cell surface immunoglobulin vascular cell adhesion molecule-1. This receptor is widely expressed in smooth muscle, hepatocytes, and some epithelia. To examine the in vivo function of α9β1, we have generated mice lacking expression of the α9 subunit. Mice homozygous for a null mutation in the α9 subunit gene appear normal at birth but develop respiratory failure and die between 6 and 12 days of age. The respiratory failure is caused by an accumulation of large volumes of pleural fluid which is rich in triglyceride, cholesterol, and lymphocytes. α9 −/− mice also develop edema and lymphocytic infiltration in the chest wall that appears to originate around lymphatics. α9 protein is transiently expressed in the developing thoracic duct at embryonic day 14, but expression is rapidly lost during later stages of development. Our results suggest that the α9 integrin is required for the normal development of the lymphatic system, including the thoracic duct, and that α9 deficiency could be one cause of congenital chylothorax.

Matricellular proteins as modulators of wound healing and the foreign body response

2003 ◽  
Vol 90 (12) ◽  
pp. 986-992 ◽  
Author(s):  
Themis Kyriakides ◽  
Paul Bornstein
Keyword(s):  
Wound Healing ◽  
Foreign Body ◽  
Tissue Repair ◽  
Foreign Body Response ◽  
Matricellular Proteins ◽  
Cell Matrix ◽  
Ecm Proteins ◽  
Matrix Interactions ◽  
Cell Matrix Interactions ◽  
Body Response

SummaryMatricellular proteins form a group of extracellular matrix (ECM) proteins that do not subserve a primary structural role, but rather function as modulators of cell-matrix interactions (1). Members of the group, including thrombospondin (TSP) -1, TSP-2, SPARC, tenascin (TN)-C, and osteopontin (OPN), have been shown to participate in a number of processes related to tissue repair. Specifically, studies in knockout mice have indicated that a deficiency in one or more of these proteins can alter the course of wound healing. More recently, TSP1, TSP2, and SPARC have also been implicated in the foreign body response, an unusual reaction to injury that occurs after the implantation of biomaterials. This review will focus on the roles of these proteins in the response to injury in mice and will show how studies of this pathophysiological process can elucidate some of the intrinsic properties of these matricellular proteins.

Substrates of Factor XIII-A: roles in thrombosis and wound healing

2012 ◽  
Vol 124 (3) ◽  
pp. 123-137 ◽  
Author(s):  
Victoria R. Richardson ◽  
Paul Cordell ◽  
Kristina F. Standeven ◽  
Angela M. Carter
Keyword(s):  
Wound Healing ◽  
Factor Xiii ◽  
Tissue Repair ◽  
Cross Linking ◽  
Clot Retraction ◽  
Matrix Deposition ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Cell Matrix Interactions

FXIII (Factor XIII) is a Ca2+-dependent enzyme which forms covalent ϵ-(γ-glutamyl)lysine cross-links between the γ-carboxy-amine group of a glutamine residue and the ϵ-amino group of a lysine residue. FXIII was originally identified as a protein involved in fibrin clot stabilization; however, additional extracellular and intracellular roles for FXIII have been identified which influence thrombus resolution and tissue repair. The present review discusses the substrates of FXIIIa (activated FXIII) involved in thrombosis and wound healing with a particular focus on: (i) the influence of plasma FXIIIa on the formation of stable fibrin clots able to withstand mechanical and enzymatic breakdown through fibrin–fibrin cross-linking and cross-linking of fibrinolysis inhibitors, in particular α2-antiplasmin; (ii) the role of intracellular FXIIIa in clot retraction through cross-linking of platelet cytoskeleton proteins, including actin, myosin, filamin and vinculin; (iii) the role of intracellular FXIIIa in cross-linking the cytoplasmic tails of monocyte AT1Rs (angiotensin type 1 receptors) and potential effects on the development of atherosclerosis; and (iv) the role of FXIIIa on matrix deposition and tissue repair, including cross-linking of extracellular matrix proteins, such as fibronectin, collagen and von Willebrand factor, and the effects on matrix deposition and cell–matrix interactions. The review highlights the central role of FXIIIa in the regulation of thrombus stability, thrombus regulation, cell–matrix interactions and wound healing, which is supported by observations in FXIII-deficient humans and animals.

scholarly journals IMT504, the Prototype of the Immunostimulatory Oligonucleotides of the PyNTTTTGT Class, Increases the Number of Progenitors of Mesenchymal Stem Cells Both In Vitro and In Vivo: Potential Use in Tissue Repair Therapy

Stem Cells ◽  
2007 ◽  
Vol 25 (4) ◽  
pp. 1047-1054 ◽  
Author(s):  
Andrés Hernando Insúa ◽  
Alejandro D. Montaner ◽  
Juan M. Rodriguez ◽  
Fernanda Elías ◽  
Juan Fló ◽  
...  
Keyword(s):  
Stem Cells ◽  
Mesenchymal Stem Cells ◽  
Tissue Repair ◽  
Potential Use

scholarly journals Integrin phosphorylation is modulated during the differentiation of F-9 teratocarcinoma stem cells.

1989 ◽  
Vol 108 (1) ◽  
pp. 183-190 ◽  
Author(s):  
S C Dahl ◽  
L B Grabel
Keyword(s):  
Stem Cells ◽  
Monolayer Culture ◽  
Developmentally Regulated ◽  
Fibronectin Receptor ◽  
Phosphorylation State ◽  
Cell Matrix ◽  
Teratocarcinoma Cells ◽  
Matrix Interactions ◽  
Before And After ◽  
Cell Matrix Interactions

The retinoic acid-induced differentiation of F-9 teratocarcinoma cells in monolayer culture is accompanied by the accumulation of fibrillar fibronectin deposits, the appearance of a highly structured actin cytoskeleton, and the redistribution of integrin to apparent sites of substrate contact. We have studied the 140-kD fibronectin receptor during this process and report that although the integrin molecule is present in equivalent amounts before and after differentiation, the level of integrin phosphorylation decreases dramatically as the cells differentiate. This loss of phosphorylation coincides temporally with the observed changes in actin, fibronectin, and integrin organization. The phosphorylation state of integrin thus may mediate developmentally regulated cell-matrix interactions.

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