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The Type II Pneumocyte
Published in Jacques R. Bourbon, Pulmonary Surfactant: Biochemical, Functional, Regulatory, and Clinical Concepts, 2019
In all species described so far, while type I cells are characterized by a smooth surface, the apex of type II cells bears numerous short microvilli (0.27 μm ± 0.01 in the fetal cultured rat lung) (Figure 2). A core of actin-like filaments that are in continuity with the dense network lying near the cell surface has been demonstrated in these microvilli.40 Type II cell apical membrane also differs from that of type I cells at the molecular level. Indeed, the use of various exogenous agglutinins, from vegetal or animal origin, showed that the two alveolar cell types exhibit different lectin-binding patterns,41–44 as summarized in Table 1. In addition to providing accurate markers for type II cell tracing in the course of fetal lung development, alveolar epithelium repair, or in culture conditions, this specificity demonstrates the presence of different mucopolysaccharide species at their surface. Such lectin-binding glycoproteins — more specifically, proteins binding to Maclura pomifera agglutinin (MPA) — have recently been isolated and characterized in the rat45 and rabbit.46 These molecules, with a molecular mass of about 200 kDa, are integral membrane glycoproteins. Their function is presently unknown; one possibility is that they might act as ion channels.46
Phytoextracts and Their Derivatives Affecting Neurotransmission Relevant to Alzheimer’s Disease
Published in Akula Ramakrishna, Victoria V. Roshchina, Neurotransmitters in Plants, 2018
Maclura pomifera (Family: Moraceae) contains two major isoflavonoids osajin and pomiferin [Figure 21.3 (xxxvii and xxxviii)], which showed AChE inhibition at IC50 value of 58.02 and 52.87 μM, respectively (Jung and Park, 2007).
Purification and Primary Culture of Type II Pneumocytes and Their Application in the Study of Pulmonary Metabolism
Published in Joan Gil, Models of Lung Disease, 2020
While cells cultured on a matrix generally retained phenotypic characteristics of type II cells better than those on the plastic dishes, the phospholipid composition of the two conditions was similar. Table 2 shows the percentage change in phosphatidyl choline and phosphatidyl glycerol composition in type II cells under various culture conditions. Despite the fact that the morphological features of type II cells are better maintained on a matrix, the content of phosphatidyl choline and phosphatidyl glycerol with time in culture does not differ from cells cultured on plastic (Dobbs et al., 1985; Table 2). Table 2 illustrates that the percentage of phosphatidyl choline does not change markedly with time in culture but that of phosphatidyl glycerol decreases markedly by 48 hr. Since phosphatidyl glycerol is more specific for surfactant lipid than all classes of phosphatidyl choline, these studies suggest that there may be a significant decline of “surfactant lipids” in type II cells by 48 hr. Very few studies have partitioned phosphatidyl choline into disaturated species, which is more specific for “surfactant lipid” than all classes of phosphatidyl choline. Smith et al., (1980) have shown that the content of DSPC in phosphatidyl choline is decreased from 50% to 25% by 24 hr. These data on both DSPC and PG seem to indicate that surfactant lipid synthesis rapidly decreases even if the morphology of type II cells may resemble in vivo type II cells. While type II cells in culture may be merely dedifferentiating, the possibility also exists that type II cells in culture behave similarly to type II cells in vivo by transforming into type I cells (Evans et al., 1973), as suggested at the time of initial successful primary culture of type II cells (Diglio and Kikkawa, 1977). Brandt (1982) reported that the alveolar surface of type I and type II cells have different lectinbinding properties. Maclura pomifera, a lectin binding to alpha-galactose residues, binds to the apical surfaces of type II but not type I cells, while Ricinus communis I, a lectin specific for beta—galactose residues, binds to the surface of type I but not type II cells in. Utilizing these lectins, Dobbs et al., (1985) found evidence that type II cells culture acquire characteristics of type I pneumocytes. The ultimate fate, dedifferentiation to type I cells, cannot be avoided, short of transformation of type II cells, for example, with SV40 virus. The fetal pretype II cells can be cultured and maintained as type II cells for some period of time (Scott et al., 1983). These cells appear to retain a reasonably high proportion of disaturated phosphatidyl choline and phosphatidyl glycerol (38% DSPC, 5,2% PG) after 2 weeks in culture. Since there are no differences in the surfactant machinery in adult and newborn lungs, this cell culture system appears to be the most promising model for study at present.
Overview of Morin and Its Complementary Role as an Adjuvant for Anticancer Agents
Published in Nutrition and Cancer, 2021
Solaipriya Solairaja, Mohammad Qasim Andrabi, Nageswara Rao Dunna, Sivaramakrishnan Venkatabalasubramanian
The presence of MN in the below-mentioned sources can be classified based on their ubiquitous distribution in the family of Moraceae, Rosaceae, and Fagaceae. MN is a polyphenolic yellow flavonol compound present majorly in the branches of White mulberry (Morus alba L), Osage orange (Maclura pomifera), Apple guava (Psidium guajava) and Old Fustic (Maclura tinctoria) and Strawberry (Fragaria ananassa). MN is also found in seed weeds, almond hull (Prunus dulcis), figs (Chlorophora tinctoria), sweet chestnut (Castanea sativa), onions (Allium cepa), jack fruit (Artocarpus heterophyllus) and red wine (Supplementary Figure 1). Additionally, MN is also an integral component of complementary and alternative medicine (Traditional Chinese Medicine and Indian system of herbal medicine) preparations (18, 23).
Morin supplementation modulates PERK branch of UPR and mitigates 1,2-dimethylhydrazine-induced angiogenesis and oxidative stress in the colon of experimental rats
Published in Toxicology Mechanisms and Methods, 2020
Sharada H. Sharma, Jayasurya Suresh Kumar, Shenbagam Madhavan, Sangeetha Nagarajan
To conclude in brief, the outcome of this study depicts that morin activated the PERK branch of UPR, which in turn phosphorylated and activated eIF2α that exhibited anti-angiogenic effect via CHOP activation on one hand and on the other hand PERK-mediated Nrf2 phosphorylation and its nuclear translocation followed by the induction of various antioxidant and detoxifying genes that culminate in improved carcinogen detoxification and tumor suppression (Figure 7). However, the impact of morin on the other branches of UPR and its effect on colon tumor suppression is yet to be explored. Based on our findings, the human equivalent dose of morin is found to be 8.1 mg/kg b.wt and regular consumption of morin rich natural sources such as Guava (Psidium guajava L.), Old fustic (Chlorophora tinctoria or Maclura tinctoria), Osage orange (Maclura pomifera), Onion peel (Allium cepa), Skin of Apple (Malus pumila), and Fig (Chlorophora tinctoria) might ensure the required morin intake.
Morin inhibits colorectal tumor growth through inhibition of NF-κB signaling pathway
Published in Immunopharmacology and Immunotoxicology, 2019
Flavonoids are a large and important group of natural products that include flavonols, flavones, flavanones and isoflavones [4]. Morin (3, 5, 7, 20, 40-pentahydroxyflavone), a member of flavonols, is a yellowish pigment found in the old fustic (Chlorophora tinctoria) and osage orange (Maclura pomifera) [5]. It has been reported to exert a variety of biological actions. For example, Morin can inhibit the expression of inflammatory factors and inflammation injury [6,7]. Additionally, Morin is shown to be an antioxidant that protects various human cells, such as myocytes, endothelial cells, hepatocytes, and erythrocytes against oxyradicals damage [8]. Numerous studies showed that Morin exhibits antitumor effects against different types of cancer, including leukemia, oral, lung and prostate carcinomas [5,9,10]. Although morin was suggested as the anticancer agent against colorectal cancer in the early years [11], the detailed molecular mechanisms of Morin have not yet been fully elucidated.