China
Africa
Explore chapters and articles related to this topic
Drug Targeting to the Lung: Chemical and Biochemical Considerations
Published in Anthony J. Hickey, Sandro R.P. da Rocha, Pharmaceutical Inhalation Aerosol Technology, 2019
Peter A. Crooks, Narsimha R. Penthala, Abeer M. Al-Ghananeem
Idiopathic pulmonary fibrosis (IPF) is a fatal lung disease with few options for treatment (Kim et al. 2006), since the aetiology of the disease is poorly understood. It has a 5-year survival rate of 30%–50%. Recent studies have shown that accumulation of extracellular matrix plays an important role in IPF, and repeated alveolar injury causes fibroblast activation, proliferation, and differentiation myofibroblasts (Wolters et al. 2014, Blackwell et al. 2014). The myofibroblasts overgrow the alveolar lung tissue, and this results in an irreversible increase in the amounts of extracellular matrix (Parker et al. 2014). Current therapeutic interventions involve targeting matrix and matrix-processing enzymes, and inhibition of the collagen cross-linking enzyme, lysyl oxidase-like 2 is currently being investigated as a treatment option for IPF (Ahluwalia et al. 2014). The FDA approved drugs pirfenidone and nintedanib are also being utilized to treat IPF (King et al. 2014, Richeldi et al. 2014). It is known that a deficiency in the chaperone protein, FK506-binding protein 10 can attenuate collagen secretion and decrease extracellular collagen cross-linking, and this might provide a potentially specific and effective drug for treatment of IPF (Staab-Weijnitz et al. 2015).
Tissue Engineering of Articular Cartilage
Published in Kyriacos A. Athanasiou, Eric M. Darling, Grayson D. DuRaine, Jerry C. Hu, A. Hari Reddi, Articular Cartilage, 2017
Kyriacos A. Athanasiou, Eric M. Darling, Grayson D. DuRaine, Jerry C. Hu, A. Hari Reddi
Another structure-modifying agent is lysyl oxidase, which acts to cross-link collagen (Figure 4.28) (Siegel et al. 1970; Makris et al. 2014b). When cartilage explants were treated with β-aminopropionitrile, an inhibitor of lysyl oxidase, both the amount of new cross-links and tensile integrity decreased (Wong et al. 2002; McGowan and Sah 2005; Asanbaeva et al. 2008a). One of the regulatory pathways for lysyl oxidase is through hypoxia-inducible factor (HIF). Hypoxia culture stabilizes HIF-α, leading to the upregulation of lysyl oxidase, resulting in increased cross-links and tensile properties for a variety of native, musculoskeletal soft tissues, including cartilage, fibrocartilage, and ligament (Makris et al. 2014a,b), and also for engineered articular cartilage. Applying lysyl oxidase is also useful in increasing the strength of the interface between engineered and native articular cartilage, leading to its potential use for implant integration (Athens et al. 2013).
Cu, 29]
Published in Alina Kabata-Pendias, Barbara Szteke, Trace Elements in Abiotic and Biotic Environments, 2015
Alina Kabata-Pendias, Barbara Szteke
In the body, Cu shifts between the Cu+ and Cu2+ forms, though the majority of the body’s Cu is in the Cu2+ form. Ability of Cu to easily accept and donate electrons explains its important role in oxidation–reduction reactions, and in scavenging free radicals. Cytochrome c oxidase plays an essential role in cellular energy, lysyl oxidase, participates in cross-linking of collagen and elastin, which form the connective tissue. The impact of lysyl oxidase helps maintain the integrity and elasticity of connective tissue in heart and blood vessels, but also plays a role in bone formation.
Spectroscopic imaging: Nuclear magnetic resonance and Raman spectrometry for the detection of collagen cross-linking from giant squid mantle, fin, and tentacle tissues
Published in Instrumentation Science & Technology, 2018
Héctor M. Sarabia-Sainz, Wilfrido Torres-Arreola, Josafat Marina Ezquerra-Brauer
Recent years have seen increased interest in identifying and characterizing bioactive proteins derived from marine sources. Among them, squid by-products are valuable underutilized sources of protein, where the predominant protein is collagen. Collagen is a fibrous insoluble protein mostly found in skin, cartilage, and connective tissues, whose primary function is to provide support; this protein maintains the union between cells.[1] Several types of collagen have been identified; the primary characteristics of all types are amino acid arrangements that are rich in proline and glycine. These arrays form three chains that intertwine to create a triple helix, which varies in composition and size.[2] The principal collagen fiber cross-linking mechanism reported is the oxidation of hydroxylysine by lysyl oxidase, which results in pyridinoline.[3] Pyridinoline is an aromatic molecule that can be covalently linked to up to three collagen chains.[4]