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Neonatal diseases II
Published in Hung N. Winn, Frank A. Chervenak, Roberto Romero, Clinical Maternal-Fetal Medicine Online, 2021
Brian P. Hackett, Jeffrey Dawson, Akshaya Vachharajani, Barbara Warner, F. Sessions Cole
The identification of genetic mutations that result in lethal respiratory failure in newborn infants has led to the discovery of genetic polymorphisms associated with an increased risk of respiratory distress in the premature newborn (32). Polymorphisms associated with an increased risk of RDS in preterm infants have been identified in the surfactant protein-A, surfactant protein-B, surfactant protein-C, and the ATP-binding cassette transporter A3 (ABCA3) genes (33–35). Additionally, polymorphisms associated with preterm RDS have also been identified in genes not directly related to surfactant synthesis and secretion including mannose-binding lectin, interleukin-10, and the G protein–coupled receptor for asthma susceptibility (36–38). Elucidating the interactions between and among genetic variants, environment, and developmental factors may lead to novel management strategies in preterm infants with RDS.
Medicines in neonates
Published in Evelyne Jacqz-Aigrain, Imti Choonara, Paediatric Clinical Pharmacology, 2021
Evelyne Jacqz-Aigrain, Imti Choonara
Pulmonary surfactant is a complex mixture of phospholipids, neutral lipids and specific proteins. It lowers surface tension at the air-liquid interface of the lung to prevent alveolar collapse at end-expiration [1]. The major cause of neonatal respiratory distress syndrome (RDS) is a primary deficiency of surfactant [2], and surfactant replacement therapy has had a major impact in improving the outcome of this disorder in preterm infants [3]. Surfactants were the first drugs designed primarily for use in the newborn, and those licensed for treatment or prevention of RDS fall into 2 broad categories: synthetic and natural. Synthetic surfactants are composed mainly of phospholipids (usually dipalmitoylphosphatidylcholine, DPPC, also known as colfosceril palmitate) but do not contain surfactant proteins. Natural surfactants are derived from animal lungs, and they contain both phospholipids and surfactant proteins B and C [4].
Respiratory Medicine
Published in Stephan Strobel, Lewis Spitz, Stephen D. Marks, Great Ormond Street Handbook of Paediatrics, 2019
Colin Wallis, Helen Spencer, Sam Sonnappa
Lung transplantation: for some lethal disorders, such as surfactant protein B deficiency and alveolar capillary dysplasia, lung transplantation is the only choice of treatment. This is currently only available in a few centres internationally and the long term outcomes of infant lung transplant is unknown.
New perpective for an old problem: extracellular vesicle based management of respiratory distress syndrome
Published in Drug Delivery, 2021
Another therapeutic strategy may be to equip exosomes with surfactant-associated proteins (SFTPs). Commercial surfactants contain hydrophobic surfactant proteins B and C, that essential in the formation, secretion and in the alveolar surfactant dynamics. But, hydrophilic surfactant proteins A and D are deficient in the exogenous products that are currently in clinical use (Engür & Kumral, 2012; Salgado et al., 2014). These proteins also have essential role in alveolar surfactant dynamics, besides their roles as components of the innate immune defence.
Alveolar epithelial cell growth hormone releasing hormone receptor in alveolar epithelial inflammation
Published in Experimental Lung Research, 2023
Tengjiao Cui, Medhi Wangpaichitr, Andrew V. Schally, Anthony J. Griswold, Irving Vidaurre, Wei Sha, Robert M. Jackson
We used human alveolar type 2 epithelial cells derived from induced pluripotent stem cells (iAT2 cells). We extensively phenotyped the iAT2 cells to confirm their identity and function. Cells were cultured on Matrigel, where they formed small monolayers or spheroidal groups. On immunofluorescent staining, the cells expressed surfactant protein C and surfactant protein B.
Bioinspired polymer nanoparticles omit biophysical interactions with natural lung surfactant
Published in Nanotoxicology, 2019
Moritz Beck-Broichsitter, Adam Bohr
The exact mechanisms leading to lung surfactant conversion are mostly undetermined. Surface area cycling and the presence of a serine-active carboxylesterase (also called “convertase”) were described as responsible variables for the transformation of LSA to SSA (Ruppert et al. 2003a, 2003b; Gross and Schultz 1992; Krishnasamy et al. 1997). Accordingly, a low surface tension (i.e. a highly compressed lung surfactant film with a multilayered surfactant “reservoir” underneath) is required for the “convertase” to approach its substrate (i.e. surfactant protein B, which is linked to the lung surfactant “machinery”). A less dense organization at the air/liquid interface, as occurring when adding “classical” inhibitors of lung surfactant function (e.g. plasma proteins or oleic acid), retarded the conversion rate of LSA to SSA. Particularly in the case of in vitro cycling experiments, adsorption of the hydrophobic surfactant proteins to the surface of the cycling tubes also needs to be considered. However, a previous report recovered less than 1% of the initially provided surfactant protein B content from the cycling tubes upon extraction with organic solvents (Günther et al. 1999a). Although plain colloidal drug delivery vehicles were identified as inhibitors of lung surfactant function (Beck-Broichsitter et al. 2014a, 2014b), no such decrease, but an elevation of the lung surfactant subtype conversion rate was observed. This must be due to their unique inhibition mechanism, namely the remarkable adsorption capacity for surfactant protein B during the surface area cycling procedure (Figure 1) (Beck-Broichsitter et al. 2014b; Raesch et al. 2015; Kumar et al. 2016; Whitwell et al. 2016). The remaining “free” surfactant protein B found in close proximity to the interfacial lung surfactant film could then be degraded by the “convertase” and/or adsorb to the surface of the cycling tubes. Polymer nanoparticles featured with a protein-repellent coating layer composed of PMPC did not interfere with the lung surfactant machinery (i.e. no relevant adsorption of surfactant protein B) and, thus, the conversion rate of LSA to SSA remained unaffected.