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Tracheal and Bronchial Developmental Abnormalities, and Inflammatory Diseases including Bronchiectasis, Cystic Fibrosis and Bronchiolitis.
Published in Fred W Wright, Radiology of the Chest and Related Conditions, 2022
This condition also predisposes to chronic chest infections and bronchiectasis. Afzelius (1976) and Afzelius and Mossberg (1980) found that in men with immotile sperms, the cilia in the respiratory tract and elsewhere showed a similar defect. It may be the cause of some cases of chronic bronchitis (Trapnell, 1982). The abnormality is found in about half of the patients with Kartagener's syndrome (situs inversus, chronic sinusitis and bronchiectasis). This usually presents in childhood with a history of excessive nasal discharge, infections and the finding of nasal polyps. Nadel et al. (1985) studied its radiological appearances and found them to be non-specific; early changes including bronchial wall thickening, with or without hyperinflation. They illustrated their cases with electron micrographs showing - (i) complete dynein defect, (ii) radial spoke defect, and (iii) microtubular transposition. Greenstone et al. (1988) re-termed it the
Manipulating the Intracellular Trafficking of Nucleic Acids
Published in Kenneth L. Brigham, Gene Therapy for Diseases of the Lung, 2020
Kathleen E. B Meyer, Lisa S. Uyechi, Francis C. Szoka
Kinesin and cytoplasmic dynein are the principal ATPase microtubule-based motors involved in organelle transport (65-68). Each type of motor associates with membranous organelles and directs movement along the length of the microtubule. Dynein drives movement toward the minus end of the microtubule, yielding a net inward flow, whereas kinesin drives movement towards the plus end, generating movement toward the cell periphery (69). Dynein is responsible for movement of endosomal and lysosomal vesicles toward the cell nucleus, while kinesin has been implicated in maintaining the extended distribution of the endoplasmic reticulum, the shape of the Golgi complex, the extension of lysosomes, and trafficking of proteins from Golgi to endoplasmic reticulum (70-72).
Structural and Biochemical Studies of the Dynein ATPase
Published in Claude Gagnon, Controls of Sperm Motility, 2020
Silvio P. Marchese-Ragona, Kenneth A. Johnson
Dynein is a multisubunit ATPase complex which is responsible for eukaryotic ciliary and flagellar beating as well as some forms of microtubule-based cytoplasmic transport. In cilia and flagella, the formation and propagation of waves are produced by the relative sliding of adjacent microtubules which, in turn, are driven by an ATP-dependent cycle of detachment and reattachment of the dynein arms. To allow a detailed structural and functional study of the dynein ATPase, it has been necessary to isolate the dynein from the axoneme. In this chapter, we describe the structural and functional properties of dyneins purified from the cilia of Tetrahymena.
Flavanol-rich lychee fruit extract substantially reduces progressive cognitive and molecular deficits in a triple-transgenic animal model of Alzheimer disease
Published in Nutritional Neuroscience, 2021
Xiao Chen, Benhong Xu, Luling Nie, Kaiwu He, Li Zhou, Xinfeng Huang, Peter Spencer, Xifei Yang, Jianjun Liu
The ER protein category included 78 kDa glucose-regulated protein (GRP 78), an ER chaperone of the HSP70 family. GRP 78 was increased in 3×Tg-AD mice and decreased in Oligonol-treated animals. Pyruvate kinase muscle (KPYM), pyruvate dehydrogenase-related (ODPA), and NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (NDUS1) were found in the mitochondrial protein group. NDUS1, a component of mitochondrial Complex I, showed reduced expression in 3×Tg-AD mice and increased expression in Oligonol-treated animal groups. Both KPYM and OPDA participate in pyruvate metabolism. In the third category, Oligonol treatment counteracted the reduction of NDUS1 in the 3×Tg-AD group. The fourth category contained cytoplasmic dynein 1 intermediate chain 1 (DC1I1), dynamin 1, synapsin II and vimentin. Mean vimentin expression was increased in 3×Tg-AD mice and reduced in the Oligonol-treated 3×Tg-AD group. Administration of Oligonol also reduced the level of DC1I1. The synapsin II level was decreased in the 3×Tg-AD group and increased with Oligonol treatment. In summary, whereas the expression of selected proteins associated with the ER, mitochondria, proteasome, and synapse was perturbed in 3×Tg-AD mice, the perturbations were effectively reversed in animals treated with Oligonol.
Molecular mechanisms governing axonal transport: a C. elegans perspective
Published in Journal of Neurogenetics, 2020
Amruta Vasudevan, Sandhya P. Koushika
Retrograde transport of neuronal cargo in axons is mediated largely by cytoplasmic Dynein (Gennerich & Vale, 2009). The Dynein motor complex comprises the heavy chain, light chain, light intermediate and intermediate chain subunits (Roberts, Kon, Knight, Sutoh, & Burgess, 2013). Following the discovery of the retrograde transport complex consisting of Dynein and its various accessory subunits, several C. elegans studies have helped uncover molecular mechanisms of regulation of retrograde transport in vivo. Characterization of C. elegans mutants isolated from a forward genetic screen for misaccumulation of Synaptobrevin (SNB-1) at the distal tip of C. elegans neurons, helped identify subunits of the neuronal Dynein complex and demonstrated that Dynein’s recruitment to synaptic vesicles in vivo is only partially dependent on vesicular spectrin (Koushika et al., 2004), an adaptor for Dynein (Muresan et al., 2001). SNB-1 containing vesicles, returning to the cell body from the synapse in C. elegans touch receptor neurons, have been shown to lack RAB-3 but contain SNT-1 (Synaptotagmin) (Murthy et al., 2011). Consistent with this observation, Dynein complex mutants show neuronal tip accumulation of SNB-1 and SNT-1 but not RAB-3 and SNG-1 (Synaptogyrin), additionally suggesting cargo specificity (Koushika et al., 2004). Thus, retrograde transport in neurons is likely regulated by cargo-specific adaptors. A list of important factors regulating retrograde axonal transport can be found in Table 2.
Genetic aspects of idiopathic asthenozoospermia as a cause of male infertility
Published in Human Fertility, 2020
Zohreh Heidary, Kioomars Saliminejad, Majid Zaki-Dizaji, Hamid Reza Khorram Khorshid
DNAI1 (dynein axonemal intermediate chain 1), DNAH5 (dynein axonemal heavy chain 5) and DNAH11 (dynein axonemal heavy chain 11) genes encode three proteins belonging to the axonemal dynein cluster, particularly expressed in testis and trachea (Zuccarello, Ferlin, Cazzadore, et al., 2008). Dynein is a family of cytoskeletal motor proteins that move along microtubules in cells. There are two kinds of dynein: (i) cytoplasmic and (ii) axonemal. They convert the chemical energy stored in ATP to mechanical work (Roberts, Kon, Knight, Sutoh, & Burgess, 2013). Three missense mutations (R663C in DNAI1, E2666D in DNAH5 and I13040V in DNAH11) have been associated with AZS, with a frequency of 8.0%. These missense mutations cause substitution of amino acids, which are essential for the protein structure. These three proteins in the axonemal dynein cluster permanently attached to the A tubule of each outer microtubule doublet and transiently attached to the B tubule of the adjacent microtubule doublet, to generate a sliding motion (Zuccarello, Ferlin, Cazzadore, et al., 2008).