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Hormonal Effects on Fascia in Women
Published in David Lesondak, Angeli Maun Akey, Fascia, Function, and Medical Applications, 2020
Angeli Maun Akey, Kathleen O’Neil-Smith
Fascia, at the microscopic level, has hormonal receptors that can affect the body’s mechanical properties on a macroscopic level.28 In pregnancy and at the end of the follicular phase of the menstrual cycle, the sex steroid hormones progesterone and estrogen induce components of the extracellular matrix (ECM), namely expression of collagen, elastin, and fibrillin 1.29,30 Collagen is responsible for the stiffness of connective tissue while elastin and fibrillin are responsible for its stretchiness.3 Both elastin and fibrillin are elastic fiber components.30 Fibroblasts secrete the glycoprotein fibrillin, which increases fascial elasticity.31 Recall the clinical consequences of tissue collagen weakness as seen in Ehlers-Danlos syndrome, which results from defects in the genetic coding of collagen synthesis,31 and the hypermobility seen in Marfan syndrome, which results from a genetic mutation in the fibrillin-1 gene causing defects in fibrillin-1 synthesis.32
Tissue injury and repair
Published in C. Simon Herrington, Muir's Textbook of Pathology, 2020
Some tissues require elasticity for their function and this is facilitated by another matrix protein, elastin. This forms the core of elastic fibres found in blood vessels, skin, and the lungs. The elastin molecules are surrounded by a microfibrillar network containing the protein fibrillin. Elastic fibres can recoil after transient stretching and this is important in tissues such as large blood vessels and the skin.
Disorders of bone and connective tissue
Published in Angus Clarke, Alex Murray, Julian Sampson, Harper's Practical Genetic Counselling, 2019
Marfan syndrome is an important disorder now known to be due to deficiency of the connective tissue protein fibrillin, determined by a gene on chromosome 15 (FBN1). This disorder tends to be overdiagnosed in tall individuals of slender habitus but with no cardinal signs, especially rapidly growing adolescents. There is rarely doubt, however, when the presence or absence of the various major features is considered as a whole.
Pre-implantation genetic testing for Marfan syndrome using mini-sequencing
Published in Journal of Obstetrics and Gynaecology, 2022
Sirivipa Piyamongkol, Krit Makonkawkeyoon, Vorasuk Shotelersuk, Opas Sreshthaputra, Tawiwan Pantasri, Rekwan Sittiwangkul, Theera Tongsong, Wirawit Piyamongkol
The genetic basis of Marfan syndrome is from various mutations within the fibrillin-1 (FBN-1) gene, with over 400 mutations having been reported. About a quarter of MFS are a result of de novo mutations (Robinson et al. 2002). The FBN-1 gene is 230-kb in size, located on 15q21.1 (Lee et al. 1991). The FBN-1 gene is composed of 65 exons, encoding a 2871 amino acid long profibrillin. Profibrillin is then cleaved into FBN-1 by the furin convertase enzyme. Structural defects in fibrillin protein caused decreased vascular strength (Robinson et al. 2006). Some Marfan patients require emergency surgery for aortic root dissection and many need prophylactic aortic root replacement. Aortic surgery is a major surgical procedure with a high intraoperative and postoperative mortality risk even in experienced centres (Fletcher et al. 2020). Permanent paraplegia is one of the most devastating complications with an incidence of 3–5% in elective cases and 19% in emergency cases (Robinson et al. 2006). In addition, re-operative cardiac surgery is not uncommon in Marfan syndrome patients with aortopathy due to dissection of other parts of the aorta (Fletcher et al. 2020).
One size does not fit all: navigating the multi-dimensional space to optimize T-cell engaging protein therapeutics
Published in mAbs, 2021
Wei Chen, Fan Yang, Carole Wang, Jatin Narula, Edward Pascua, Irene Ni, Sheng Ding, Xiaodi Deng, Matthew Ling-Hon Chu, Amber Pham, Xiaoyue Jiang, Kevin C. Lindquist, Patrick J. Doonan, Tom Van Blarcom, Yik Andy Yeung, Javier Chaparro-Riggers
Epidermal growth factor (EGF)-like domains, originally identified in EGF and characterized by three intradomain disulfide bonds, are protein subunits present in a wide variety of extracellular proteins such as Notch, fibrillin, and various blood factors.21 One of their important functions is to serve as relatively rigid structural spacers,22as observed in crystal structures of tandem EGF-like domains from Notch 1 receptor (PDB ID: 5MWB)23 and Jagged-1 protein (PDB ID: 2VJ2).24 To investigate the effect of antigen epitope location in T-cell redirected lysis in a systematic fashion, we engineered cell lines that express BCMA antigen with different EGF-like domains as tethers to increase the distance to the target cell membrane. Based on the numbers of EGF-like domains used, these cell lines were named T0, T1, T2, …,T7, with T abbreviated from “tether.” Schematic views of these receptors based on structural modeling are shown in Figure 2a. Fluorescence-activated cell sorting (FACS) analysis revealed similar BCMA expression levels (~104 receptors per cell) across all eight cell lines (Supplementary Figure 1), making a direct comparison of these cell lines feasible.
Extracellular Matrix Remodeling During Palate Development
Published in Organogenesis, 2020
Xia Wang, Chunman Li, Zeyao Zhu, Li Yuan, Wood Yee Chan, Ou Sha
Fibrillins are a group of large extracellular glycoproteins including three isoforms, Fibrillin-1, −2, −3.43 They compose the core microfibrils in the ECM of elastic and non-elastic tissues, and interact with integrins directly43 or bind and activate Tgf-β.67Fibrillin-1 mRNA is weakly expressed in the palatal mesenchyme only before palatal shelf elevation (Table 2).6 In contrast, Fibrillin-2 mRNA is enriched in the nasal side of palatal mesenchyme before palatal shelf elevation, then increased and expanded around Tgf-β3+MEE cells and in the oral side of palatal mesenchyme.6 The close relationship of strong Fibrillin-2+mesenchyme cells and Tgf-β3+MEE cells indicates that Fibrillin-2 may be important for Tgf-β mediated palatal fusion. Retinoid acid, an important regulator during embryogenesis, dose-dependently inhibit fibrillin-2 production in human fetal palatal mesenchymal cells in vitro.49