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Biomedical Applications V: Influence of Carbon Nanotubes in Neuronal Living Networks
Published in Giorgia Pastorin, carbon nanotubes, 2019
The CNT-based composite was prepared by in situ polymerisation of acrylic acid onto oxidised CNTs. The neuron differentiation efficiency on poly(acrylic acid)-grafted CNT (PAA-g-CNT) thin films was compared with that of thin films composed of poly(acrylic acid) (PAA) or PLO. The PAA-g-CNT thin films showed enhanced neuron differentiation while maintaining cell viability, as assessed by measuring the metabolic activity of dehydrogenases. SEM images showed that the differentiated neurons on PAA-g-CNT surfaces have more branches, suggesting that they are more mature. In addition, the CNT-based surface exhibited a higher cell adhesion and protein (laminin) adsorption. Laminin is a glycoprotein found in the extracellular matrix, the sheets of protein that form the substrate of all internal organs (i.e., basement membrane). Laminin has been reported to favour neuronal growth.28 Indeed, laminin is a substrate along which nerve axons can grow both in vivo and in vitro.
Environmental factors contribute to skeletal muscle and spinal cord regeneration
Published in David M. Gardiner, Regenerative Engineering and Developmental Biology, 2017
Ophelia Ehrlich, Yona Goldshmit, Peter Currie
Laminin is the major component of the basement membrane in all tissues (Li et al. 2002). Laminins are cell adhesion molecules and are also implicated in cell signaling pathways (Durbeej 2010). Laminins are heterotrimers, made up of one α, one β, and one γ subunit, forming a cross-like structure (Timpl et al. 1979; Beck et al. 1993). Generally, the α (a), β (b), and γ (c) N-terminals make up a maximum of three short arms. These polypeptides then intertwine to form a coiled-coil domain that forms the long arm, which is followed by a globular structure, named the G domain (Sanes et al. 1990; Tunggal et al. 2000). The G domain is made solely by the α subunit and is critical for laminin–cell interactions (Pegoraro et al. 1998; Tunggal et al. 2000; Allamand and Guicheney 2002). The short arms self-polymerize, forming a laminin network available for other basal lamina components to interact (Colognato et al. 1999; Tunggal et al. 2000).
Extracellular Matrix–Derived Biomaterials: Molecularly Defined Ingredients and Processing Techniques
Published in Gilson Khang, Handbook of Intelligent Scaffolds for Tissue Engineering and Regenerative Medicine, 2017
H.R. Hoogenkamp, L.R.M. Versteegden, T.H. van Kuppevelt, W.F. Daamen
Laminins are considered to be one of the major adhesive glycoproteins and are a main component of the basement membrane. Laminins are large heterotrimeric glycoproteins consisting of α, β, and γ chains. Due to alternative mRNA splicing, different chains can be synthesized respectively. Around 14 chain combinations have been described in vivo and each molecule is named according to their chain composition.91 It is generally believed that the cross-like structure of laminin facilitates both cell adhesion as well as laminin sheet or basement membrane formation. Additionally, laminin has a high affinity for type IV collagen and heparan sulfate (HS), which are also major components of the basement membrane.92 Laminins generally play important roles in cell adhesion, migration, proliferation, neurite outgrowth, and angiogenesis.93 Due to its high affinity for ECM components and cell surface proteins, laminin is widely used in the coating of cell culture surfaces or scaffolds.94
Electrospun natural polymer and its composite nanofibrous scaffolds for nerve tissue engineering
Published in Journal of Biomaterials Science, Polymer Edition, 2020
Fangwen Zha, Wei Chen, Lifeng Zhang, Demei Yu
Laminin is a large cross-shaped glycoprotein and one of the ECM components. Laminin is continuously synthesized after nerve injury and plays a crucial role in cell migration, differentiation and neurite growth [135, 136]. The laminin was immobilized onto poly(L-lactic acid) (PLLA) nanofibers by diamino-poly(ethylene glycol) and heparin, simulating the physical and biochemical properties of native matrix fibrils [133]. The rat dorsal root ganglion (DRG) tissues on this nanofiber scaffold surface had significantly longer neurite length as compared to untreated PLLA fibers. The results showed that laminin treated bioactive nanofiber could deliver and manipulate chemical cues and further promote the nerve growth. Koh et al. utilized various methods to add laminin to PLLA and found the blended electrospinning was a facile and efficient way [134]. The composite nanofibers scaffold supported PC12 cell proliferation and neurite extension. With laminin treated, it can bind soluble cues such as nerve growth factor to the nanofiber scaffolds surface, thus guide cell differentiation and neurite extension.
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.
Proliferation of mouse embryonic stem cells on substrate coated with intact silkworm sericin
Published in The Journal of The Textile Institute, 2022
Chihiro Umehara, Ai Ai Lian, Yuichiro Funahashi, Keiko Takaki, Rina Maruta, Yuto Ohmaru, Yoko Okahisa, Takashi Aoki, Hajime Mori, Eiji Kotani
Laminin is a cell-adhesive, high molecular weight protein, and a truncated region named the E8 fragment can be used as an effective scaffold for the cultivation of human pluripotent stem cells (Miyazaki et al., 2013). In addition, an amino acid sequence, YIGSR, from laminin has been reported to mimic various activities of laminin in various cell lines, including ES cell adhesion, while the addition of the peptide improved the properties of the fabricated hydrogel for ES cell growth (Horák et al., 2011).