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Introduction to Host-Biomaterial Interactions
Published in Nina M. K. Lamba, Kimberly A. Woodhouse, Stuart L. Cooper, Polyurethanes in Biomedical Applications, 2017
Nina M. K. Lamba, Kimberly A. Woodhouse, Stuart L. Cooper
The interactions of cells with surfaces (including biomaterials) and with other cells are mediated by several different families of receptors.63–66 Interest in adhesion receptors and their impact on biomaterial implants is growing in the research community because of the involvement of these receptors in wound healing, inflammation, and thrombogenesis. There are several different families of adhesion receptors. These families include: (1) Integrins which are involved in cell-cell and cell-surface interactions; (2) Members of the immunoglobulin superfamily which are involved in cell adhesion, particularly during wound healing and inflammation; (3) The LEC-cams that mediate white cell/endothelial cell adhesion; and (4) CD44, a leukocyte adhesion molecule responsible for lymphocyte binding to vascular endothelium.
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Published in Splinter Robert, Illustrated Encyclopedia of Applied and Engineering Physics, 2017
[biomedical, chemical] In biology, there is cell-to-cell binding and communication interaction that can be divided into four types of receptors: cadherins, selectins, integrins, and immunoglobulin superfamily. The immunoglobulin superfamily has a molecular structure that is similar to immunoglobulins. Examples of the immunoglobulin superfamily are found in intracellular connective molecular chains and for neural cell molecular binding.
Centralized Endothelial Mechanobiology, Endothelial Dysfunction, and Atherosclerosis
Published in Jiro Nagatomi, Eno Essien Ebong, Mechanobiology Handbook, 2018
Ian Chandler Harding, Eno Essien Ebong
The endothelial glycocalyx layer, also known as the endothelial surface layer, is a cell membrane-attached, hydrated, and porous layer made primarily of proteoglycans, glycoproteins, and associated soluble molecules [116] (Figure 7.3). The glycocalyx encapsulates ECs and is most abundant on the apical cell surface [116]. Taken together, the proteoglycans, glycoproteins, and soluble molecules give the glycocalyx its thickness and a net negative charge. Of these components, proteoglycans are the main constituent and have been strongly implicated in the role of the glycocalyx in mechanobiology. Proteoglycans are transmembrane complexes containing a core protein with an attached glycosaminoglycan (GAG) chain. There are a variety of glycocalyx-associated core proteins, including syndecans, glypicans, perlecans, and versicans; however, the syndecan and glypican families are the dominant forms [117]. Attached to each core protein may be one or more GAGs, linear polysaccharides composed of repeating disaccharide units, which extend into the vessel lumen. Of major interest in endothelial mechanobiology are heparan sulfate, chondroitin sulfate, hyaluronic acid, and sialic acid, with heparan sulfate constituting 50%–90% of total GAGs and attaching mainly to glypican and syndecan core proteins [118]. GAGs can also be further modified through the addition of sugars such as sialic acid, a main contributor to the net negative charge of the glycocalyx [119]. In addition to the proteoglycan component of the glycocalyx, the glycocalyx also contains glycoproteins such as integrins, selectins, and members of the immunoglobulin superfamily. Common immunoglobulin superfamily members include the intercellular adhesion molecule (ICAM), vascular cell adhesion molecule (VCAM), and platelet-EC adhesion molecule (PECAM). These glycoproteins not only contribute to the structure of the glycocalyx, but also more importantly regulate the level of interactions between ECs and cells and molecules in the circulating blood, a vital process relevant to vascular health regulation. Finally, soluble molecule components are embedded within the proteoglycans and glycoproteins of the glycocalyx. Important soluble molecules include albumin and sphingosine 1 phosphate, which assist in enlargement and stabilization of the glycocalyx [120].
Cytoplasmic and periplasmic expression of recombinant shark VNAR antibody in Escherichia coli
Published in Preparative Biochemistry and Biotechnology, 2019
Herng C. Leow, Katja Fischer, Yee C. Leow, Katleen Braet, Qin Cheng, James McCarthy
In contrast to camelids, immunoglobulin new antigen receptor (IgNAR) is an intra-domain disulfide bond immunoglobulin superfamily protein that provided additional stability without adversely affecting antigen binding efficiency. This protein was naturally discovered from nurse shark (Ginglymostoma cirratum)[5] and wobbegong shark (Orectolobus maculates).[6] Unlike immunoglobulin (Ig) isotypes found in higher mammals, the variable domains of shark IgNAR (VNAR) is an unusual single domain antibody that contains only a single H-chain homodimer and lacks a light chain.[7] According to molecular analysis, the deletion of a large portion of framework region 2-complementarity determining region 2 (FR2-CDR2) has made VNAR the smallest variable domain with a size of ∼12 kDa in the animal kingdom.[7] It may be due to VNARs have evolved from separate lineage from immunoglobulins and thus have never had a CDR2.[8,9]Moreover, VNAR domains possess an extraordinary CDR3 domain which is much longer than that of conventional antibodies. The inter- or intra-loop of CDR3 is typically influenced by the numbers of cysteine residues and the penetration capability into the cleft region of the target antigen.[10,11] Owing to peculiar structure, the excellent solubility and thermostability of these natural single domain fragments may be due to the substitutions of amino acid at heavy and light variable domains (VH-VL) interface, resulting to be more hydrophilicity rather than a hydrophobic interface as exhibited in conventional antibodies.[7,12]
Core genes in lung adenocarcinoma identified by integrated bioinformatic analysis
Published in International Journal of Environmental Health Research, 2023
Liu Yang, Qi Yu, Yonghang Zhu, Manthar Ali Mallah, Wei Wang, Feifei Feng, Qiao Zhang
In addition, our study also found that VWF, PECAM1, TEK, ANGPT1, SCGB1A1, CD36 and SPARCL1 were lower expressed in LUAD and were associated with good overall survival, which need to be further attention. VWF encodes a glycoprotein involved in hemostasis. Once this gene is mutated, it can lead to an inherited bleeding disorder (Favaloro et al. 2018). According to some experimental and clinical studies, immune responses such as chronic inflammation, may influence the development and progression of cancer. VWF is regarded as an anti-tumor factor, which negatively regulates angiogenesis and apoptosis (Franchini et al. 2013). On the contrary, VWF has been reported to promote tumorigenesis of LUAD by modulating inflammatory effects in lung cancer (Liu et al. 2017). As a result, more research on this gene is required. Platelet-endothelial cell adhesion molecule-1 (PECAM1) is a member of the immunoglobulin superfamily located at the endothelial cell–cell junctions (Woodfin et al. 2007). One previous study has revealed that mRNA expression of PECAM1 was significantly higher in clear cell renal cell carcinoma (ccRCC) tissues than that in normal tissues (Yang et al. 2019). PECAM1 was also discovered to be important in ARDS lung repair and regeneration (Villar et al. 2019). The angiogenin receptor TEK is a tyrosine kinase which regulates homeostasis through its own and transphosphoric acid actions, which is regarded as a potential biomarker of ccRCC and lung cancer (Piao et al. 2018; Ha et al. 2019). Additionally, ANGPT1 is one of the key pro-angiogenic factors that enhances endothelial cell migration and capillary-like structure formation, and miRNAs can regulate these genes involved in tumor angiogenesis-dependent growth (Dews et al. 2006; Flores-Perez et al. 2016). Some researchers have the opinion that miRNA can affect many characteristics of breast cancer by targeting key angiogenic gene ANGPT1, which has the reference significance to the LUAD (Flores-Perez et al. 2016). CD36 is a membrane protein receptor located on the cell surface and it belongs to the scavenger receptor B family. By combining with different ligands, it participates in a variety of important physiological and pathological processes. A previous study had reported that changes in CD36 expression are related to NSCLC (Mehan et al. 2012). Thus, CD36 provides new evidence as a therapeutic target for cancer. SPARC-like protein 1 (SPARCL1) is a member of the cysteine-rich acid secreted protein (SPARC) family of cell matrix proteins. Wang et al. found that the expression of SPARCL1 in LUAD was down-regulated, and this gene regulates DNA methylation (Wang et al. 2019). Our study found that SCGB1A1 is related to the prognosis of LUAD patients, but its role in LUAD remains to be explored. Considering these reports and our research, we can conclude that VWF, PECAM1, TEK, ANGPT1, SCGB1A1, CD36 and SPARCL1 play an important prognostic role in LUAD.