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Introduction to Oral and Craniofacial Tissue Engineering
Published in Vincenzo Guarino, Marco Antonio Alvarez-Pérez, Current Advances in Oral and Craniofacial Tissue Engineering, 2020
María Verónica Cuevas González, Eduardo Villarreal-Ramírez, Adriana Pérez-Soria, Pedro Alberto López Reynoso, Vincenzo Guarino, Marco Antonio Alvarez-Pérez
Another essential fibrous protein in the matrix for playing a crucial role in the organization of the interstitial of the extracellular matrix and for interactions with cells is fibronectin. Fibronectin is directly related to central cellular events related to the matrix, such as cell adhesion, migration, growth and differentiation. Fibronectin is a protein made up of a dimer that is held together by a pair of disulfide linkages in the carboxyl terminus, and each monomer has a molecular weight around of ~250 kDa. Similar to elastin, fibronectin is a protein encoded by a single gene. However, fibronectin may occur in different versions due to alternative splicing, generating up to 20 known isoforms. Fibronectin can be stretched several times over its resting length by a neighboring cellular traction force. Owing to the tensile strength over fibronectin, it undergoes to conformational changes to expose integrin-binding sites recognized by integrins on the cellular surface. Consequently, the adhesion of integrins to fibronectin is allowed and promotes fibronectin-fibril assembly, which implies that fibronectin is also a mechano-regulator of the extracellular matrix (Frantz et al. 2010; Pankov and Yamada 2002; Xu and Mosher 2011).
Positional information in the extracellular matrix
Published in David M. Gardiner, Regenerative Engineering and Developmental Biology, 2017
Anne Q. Phan, Md. Ferdous Anower-E-Khuda
Fibronectin is a multifunctional molecule that is ubiquitously expressed in the ECM. Fibronectin has a key role in cell adhesion, embryonic development, and wound healing. The molecule exists in two forms: the circulating form is present in plasma and the cellular form is expressed by fibroblasts. Fibronectin binds to cells through integrin receptors and forms binding domains for a variety of proteins and carbohydrates. The integrin-α5β1 is the primary fibronectin receptor that mediates cell adhesion, migration, and signaling. Cell signaling through fibronectin involves two mechanisms: integrin–ligand interaction and integrin clustering or aggregation. Syndecans, a family of HS PG (HSPG) cell surface receptors, bind to fibronectin through their GAG chains and induce intracellular cell signaling.
Enzyme Catalysis
Published in Harvey W. Blanch, Douglas S. Clark, Biochemical Engineering, 1997
Harvey W. Blanch, Douglas S. Clark
The site of adhesion of cells to surfaces has a morphological pattern that is known as a tight junction. When several cells attach around a locus, points of contact may develop between cells; these are known as gap junctions. Both types of junctions (around 50Å apart) play an important role in allowing coordination and metabolic exchange to occur, resulting in metabolic cooperativity. The type of attachment material, known as the "substrate" or "substratum" in the cell culture literature, is important. As cells are negatively charged, the best substrata are positively charged, holding cells by electrostatic forces. An excellent material is fibronectin, a cold-insoluble globular glycoprotein. Fibronectin promotes cell cell and cell-substrate adhesion and cell spreading. The type of substrata used for cultivation of anchorage-dependant cells is thus quite important and we shall briefly discuss both natural and artificial substrata.
PEGylated TiO2 nanoparticles mediated inhibition of cell migration via integrin beta 1
Published in Science and Technology of Advanced Materials, 2018
Qingqing Sun, Koki Kanehira, Akiyoshi Taniguchi
Integrin beta 1, as the major fibronectin receptor on most cells, transmits cellular signaling across cell membrane to modulate cell adhesion, survival, and migration. Its endocytic trafficking is divided into two parts based on the trafficking time: one is long loop trafficking during which integrin beta 1 is recycled to the plasma membrane for new focal adhesions formation and cell migration; the other one is short loop trafficking during which integrin beta 1 is sorted and translocated to the late endosome or lysosome for degradation [45]. The equilibrium between recycling and degradation of integrin beta 1 maintains the normal cell migration, which plays a crucial part in embryo development, histogenesis, and wound healing [46].
Modulation of myelin formation by combined high affinity with extracellular matrix structure of electrospun silk fibroin nanoscaffolds
Published in Journal of Biomaterials Science, Polymer Edition, 2019
Sha Liu, Changmei Niu, Ziqi Xu, Yingyu Wang, Yunyun Liang, Ying Zhao, Yahong Zhao, Yumin Yang
To investigate why electrospun silk fibroin affected adhesion of DRG neurons, quantitative real-time PCR analysis was used to determine the expression of adhesion-related genes in cultured DRG neurons. The expression levels of β-caterin, fibronectin, laminin and N-cadherin were analyzed. Fibronectin is an important extracellular matrix protein. It interacts with cell surface receptors to regulate various cellular processes, involving cell adhesion, cell motility and tissue repair [23]. Laminin is a component of all basement membranes. It also affects a variety of functions of adjacent cells, including cell adhesion, proliferation and differentiation [24]. Cadherins are Ca2+ dependent cell adhesion molecules (CAM), which play an important role in the tissue construction and morphogenesis of multicellular organisms [25]. Classification according to the organization patterns of expression, type N is nerve-derived. N-cadherin is widely distributed in neurons and glial cells [26]. Myelination is formed by the complex interaction between Schwann cells and DRG neurons. Electrospun silk fibroin promotes the attachment of DRG through the secretion of related adhesion factors. Schwann cells, the principal glial cells of the PNS, play a crucial role in the survival and function of neurons, and wrap around axons to form dense myelin sheaths [27]. Previous studies have shown that electrospun fibers topography can induce Schwann cells to be myelinating state, and that the electrospun scaffold has the potential to promote Schwann cell maturation [28]. Therefore, the electrospun silk fibroin may be used as an ideal biological scaffold material to optimally mediate cell-cell and cell-matrix interaction.
Development of a three dimensional (3D) knitted scaffold for myocardial tissue engineering. Part II: biological performance of the knitted scaffolds
Published in The Journal of The Textile Institute, 2025
Derya Haroglu, Ahmet Eken, Zeynep Burçin Gönen, Dilek Bahar
The absorbance has strong negative correlation with the thickness (r= −0.94), and positive strong correlation with the porosity (r = 0.94). The early continuity of cell growth inside the scaffold is dominated through diffusion by transporting nutrients and oxygen to and waste products from the cells until angiogenesis (vascularization) is completed to a great extent after implantation (Harley & Yannas, 2006; Rouwkema et al., 2010). Therefore, thickness and pore structure of scaffolds become critical in terms of the initial migration of cells both during cell culture in vitro, and after implantation of the cell seeded structure in vivo. Here, slow supply of metabolites by diffusion would be questionable for cells that are far from the scaffold surface on the order of several hundreds of microns (Harley & Yannas, 2006; Rouwkema et al., 2010). On the other hand, a high degree of porosity with interconnectivity between adjacent pores contributes the migration of cells, and the total number of cells binding to the scaffold, facilitating the diffusion of metabolites (Yannas, 2001). In addition, t-test showed that the absorbance values of the half pile loop structures were higher than those of the full pile loop structures (Figure 5(c)) at statistically significant level (p-value < 0.01). Furthermore, in case of the scaffolds coated with fibronectin, the absorbance values of the full pile loop structures were higher than those of the half pile loop structures (Figure 2(b)) (p-value < 0.05). Here, the 144H sample has higher porosity, and lower thickness when compared with the 144 F sample. However, the higher specific surface of the 144 F sample due to its full scale pile loops together with fibronectin have promoted the cell attachment and penetration. Fibronectin is an extracellular matrix fibrous protein that plays a pivotal role in cell adhesion through binding to the major cell surface responsive sites and coordinating cell behavior (Grinnell, 1978; Parisi et al., 2020). The coating of scaffolds with fibronectin is a promissing approach for improving cell adhesion and spreading that is crucial for cell viability with following cell migration and proliferation (Grinnell, 1978; Jacobsen et al., 2017).