Academic literature on the topic 'Adsorptive endocytosis'

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Journal articles on the topic "Adsorptive endocytosis"

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Bohn Thomsen, Louiza, Jacek Lichota, Thomas Navndrup Eskehave, et al. "Brain Delivery Systems via Mechanism Independent of Receptor-Mediated Endocytosis and Adsorptive-Mediated Endocytosis." Current Pharmaceutical Biotechnology 13, no. 12 (2012): 2349–54. http://dx.doi.org/10.2174/138920112803341842.

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Banks, W. A., V. Akerstrom, and A. J. Kastin. "Adsorptive endocytosis mediates the passage of HIV-1 across the blood-brain barrier: evidence for a post-internalization coreceptor." Journal of Cell Science 111, no. 4 (1998): 533–40. http://dx.doi.org/10.1242/jcs.111.4.533.

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HIV-1 induces the AIDS dementia complex and infects brain endothelial and glial cells. Because the endothelial cells comprising the blood-brain barrier (BBB) do not possess CD4 receptors or galactosylceramide binding sites, it is unclear how HIV-1 negotiates the BBB. Previous work has suggested that gp120, the glycoprotein viral coat of HIV-1, is capable of inducing adsorptive endocytosis. Glycoprotein lectins like wheatgerm agglutinin induce adsorptive endocytosis and greatly potentiate the uptake by and passage across mouse endothelial cells in vivo and in vitro. We show here that the wheatgerm agglutinin-induced binding of gp120 is dose-dependent and involves components of the cytoskeleton. The uptake is partially dependent on temperature and energy and is modestly enhanced by potassium depletion. Glycosylation of gp120 is critical for its uptake by adsorptive endocytosis since the non-glycosylated form of gp120 is unaffected by wheatgerm agglutinin. Evidence is presented for the existence of a coreceptor sensitive to protamine sulfate that is primarily involved in membrane fusion after 125I-gp120 has bound to the cell membrane and is probably activated after internalization. This coreceptor probably contains a negatively charged heparin sulfate group and could be a member of the chemokine receptor family.
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Raphael, Bernd, and Barbara J. McLaughlin. "Adsorptive and fluid phase endocytosis by cultured rabbit corneal endothelium." Current Eye Research 9, no. 3 (1990): 249–58. http://dx.doi.org/10.3109/02713689009044520.

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Wall, D. A., and T. Maack. "Endocytic uptake, transport, and catabolism of proteins by epithelial cells." American Journal of Physiology-Cell Physiology 248, no. 1 (1985): C12—C20. http://dx.doi.org/10.1152/ajpcell.1985.248.1.c12.

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Adsorptive and/or receptor-mediated endocytosis of proteins is a universal cell property, which is highly expressed in epithelial cells. Some absorbed proteins are transported intact across cells and in this manner subserve specialized functions such as the transference of immunity from mother to child. Mainly, however, absorbed proteins are transported to lysosomes, where they undergo complete hydrolysis to amino acids. This process is essential for the homeostasis of circulating proteins. This brief review considers the intracellular pathways taken by endocytosed proteins and the quantitative aspects and determinants of protein uptake and catabolism by epithelial cells. The topics to be briefly discussed are initial internalization sites, transport organelles (endosomes), and lysosomal and nonlysosomal pathways of transport; intracellular sorting of internalized proteins, membranes, and receptors; kinetics and selectivity of renal cell uptake of low-molecular-weight proteins and proteohormones; receptor-mediated endocytosis of larger proteins (e.g., glycoproteins) by hepatocytes; and lysosomal catabolism of absorbed proteins and its dependence on protein load and endosomal-lysosomal pH and function. The perspectives of the field and some of the outstanding unsolved problems are briefly discussed.
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Raub, T. J., and K. L. Audus. "Adsorptive endocytosis and membrane recycling by cultured primary bovine brain microvessel endothelial cell monolayers." Journal of Cell Science 97, no. 1 (1990): 127–38. http://dx.doi.org/10.1242/jcs.97.1.127.

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The dynamics of membrane recycling were examined in primary cultures of brain microvessel endothelial cells (BMECs). Because the BMEC surface was dominated by galactosylated glycoconjugates, ricin agglutinin (RCAI) was used as a tracer to follow the endocytosis and recycling of RCAI binding sites. These binding sites accounted for 75% of the iodinatable or most externally disposed plasma membrane proteins. Because greater than 90% of the RCAI that had bound to BMECs was removed by a brief, nontoxic treatment with galactose, the amounts and kinetics for internalization and efflux of [125I]RCAI were measured. Both endocytosis and efflux were energy dependent. By using pseudo-first-order kinetics, the t1/2 values for RCAI binding, internalization and efflux were 5, 18 and 13–14 min, respectively. By comparing efflux with and without galactose present, we found that 60% of the RCAI binding sites that had been internalized were returned to the cell surface and reinternalized. Quantifying the distribution of gold-RCAI following internalization showed kinetics consistent with that obtained using radiolabeled RCAI. Both horseradish peroxidase (HRP) and gold-conjugated RCAI that had bound BMEC at 4 degrees C became localized within more caveolae within 2.5 min of warming to 37 degrees C to permit endocytosis. With time, RCAI appeared within endosomes and tubules and vesicles of which some were located in the trans-Golgi network (TGN). The distribution of HRP-RCAI contrasted with that of free HRP, which was not routed to the TGN. The absence of RCAI conjugates in association with the basolateral membrane domain suggested the presence of functional tight junctions and maintenance of polarity throughout the duration of these experiments. These results showed that membrane recycling was more extensive and much slower than fluid-phase endocytosis in cultured BMECs. Moreover, we found that endocytosis of membrane by BMECs in culture was similar to that reported for brain endothelium in vivo in that a fraction of the cell surface membrane was routed to the TGN.
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Sai, Yoshimichi, Masahiro Kajita, Ikumi Tamai, Jun Wakama, Tateaki Wakamiya, and Akira Tsuji. "Adsorptive-mediated endocytosis of a basic peptide in enterocyte-like Caco-2 cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 275, no. 3 (1998): G514—G520. http://dx.doi.org/10.1152/ajpgi.1998.275.3.g514.

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The internalization of a basic peptide, 001-C8 [H-MeTyr-Arg-MeArg-d-Leu-NH(CH2)8NH2], into enterocyte-like Caco-2 cells was evaluated. Internalization of125I-labeled 001-C8 (125I-001-C8) increased time dependently and reached steady state at 60 min. The steady-state internalization of 125I-001-C8 (7.24 ± 0.41 μl/mg protein) was temperature and concentration dependent and was significantly decreased by dansylcadaverine (500 μM), protamine (1 mM), poly-l-lysine (1 mM), E-2078 (1 mM), and ebiratide (1 mM), whereas poly-l-glutamic acid (1 mM), tyrosine (1 mM), and glycylglycine (25 mM) were not inhibitory. Predigestion of acid mucopolysaccharides by heparinase I, heparitinase, and chondroitinase ABC also decreased the internalization. The maximal internalization, the half-saturation constant, and the nonsaturable internalization of125I-001-C8 were 1.13 ± 0.23 pmol/mg protein, 0.47 ± 0.43 μM, and 3.13 ± 0.19 μl/mg protein, respectively. Confocal microscopy also indicated the internalization of fluorescence-derived 001-C8 [001-C8–4-nitrobenz-2-oxa-1,3-diazole (001-C8-NBD)]. Granular staining seen within the cell, excluding nuclei, indicated the sequestration of 001-C8-NBD within endocytotic vesicles. Dansylcadaverine and protamine strongly decreased the granular distribution of 001-C8-NBD within the cell. These results demonstrate that 001-C8 is taken up by Caco-2 cells via adsorptive-mediated endocytosis.
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Telfer, William H., and Muh-Liang Pan. "Adsorptive endocytosis of vitellogenin, lipophorin, and microvitellogenin during yolk formation inHyalophora." Archives of Insect Biochemistry and Physiology 9, no. 4 (1988): 339–55. http://dx.doi.org/10.1002/arch.940090408.

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Lalli, M. F., V. Lacroix, L. Hermo, Y. Clermont, and C. E. Smith. "Localization of various phosphatase activities within the golgi apparatus and lysosomes of rat leydig cells." Proceedings, annual meeting, Electron Microscopy Society of America 44 (August 1986): 294–95. http://dx.doi.org/10.1017/s0424820100143092.

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The testosterone-secreting Leydig cells contain an abundance of smooth endoplasmic reticulum, peroxisomes, mitochondria as well as a large, spheroidal, juxtanuclear Golgi apparatus composed of interconnected stacks of saccules (Figs. 1,2). Each Golgi stack appears to be composed of between 5 to 7 saccules or sacculo-tubular elements (Figs.1,2). These cells also possess pale and dense multivesicular bodies and dense membrane-bound bodies identified assecondary lysosomes, all of which have been shown to be involved in fluid phase and adsorptive endocytosis as well as in receptor mediated endocytosis. The purpose of the present study was to characterize the reactivity of Golgi saccules, multivesicular bodies and lysosomes of Leydig cells for different phosphatases.
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Banks, William A., Abba J. Kastin, and Victoria Akerstrom. "HIV-1 protein gp120 crosses the blood-brain barrier: Role of adsorptive endocytosis." Life Sciences 61, no. 9 (1997): PL119—PL125. http://dx.doi.org/10.1016/s0024-3205(97)00597-3.

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Drin, Guillaume, Christophe Rousselle, Jean-Michel Scherrmann, Anthony R. Rees, and Jamal Temsamani. "Peptide delivery to the brain via adsorptive-mediated endocytosis: Advances with SynB vectors." AAPS PharmSci 4, no. 4 (2002): 61–67. http://dx.doi.org/10.1208/ps040426.

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Dissertations / Theses on the topic "Adsorptive endocytosis"

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Ntwatwa, Ziphozihle. "Formulation and evaluation of the biocompatibility of chitosan-dextran nanoparticles using a blood-brain barrier model." University of the Western Cape, 2018. http://hdl.handle.net/11394/6431.

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Magister Scientiae - MSc (Medical BioSciences)<br>Central nervous system (CNS) infections are a therapeutic challenge. This is partly due to insufficient drug penetration across the blood-brain barrier (BBB). The BBB is a specialized, highly selective, metabolically active physiological barrier that regulates the movement of molecules into-and-out of the brain. As a result, large hydrophilic antibiotics such as colistin poorly penetrate to the CNS. Colistin is an old 'last line of defence'; a gram-negative antibiotic that has seen its clinical re-emergence due to the surge of multidrug resistance (MDR) infections. However, owing to systemic toxicity, increasing the intravenous dosage, in order to obtain higher CNS penetration, is inimical. Chitosan (CS) based nanoparticles (NPs) have been proposed as drug delivery systems across the BBB. CS is a cationic, natural polysaccharide that has the ability to be complexed with multivalent polymers like dextran (DS) thus forming CS-DS NPs. Naturally, CS has remarkable inherent features such as biocompatibility, biodegradability, ability to encapsulate poorly soluble drugs and it is favourable for endothelial cell uptake. However, polymeric NPs (even those derived from natural polysaccharides) have limited use due to toxicity. Considering the vital role of the BBB, toxicity would denote dire effects on CNS functioning. Therefore, treatment of CNS infections fringes on a deeper understanding of the interactions between drug delivery systems and the BBB.
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Wilhelm, Claire. "Développement d'une sonde intracellulaire : l'endosome magnétique." Paris 7, 2002. http://www.theses.fr/2002PA077198.

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Book chapters on the topic "Adsorptive endocytosis"

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Raub, Thomas J., and Carolyn R. Newton. "Membrane Recycling, Adsorptive and Receptor-Mediated Endocytosis by Primary Bovine Cerebral Microvessel Endothelial Cell Monolayers in Vitro." In Pharmaceutical Applications of Cell and Tissue Culture to Drug Transport. Springer New York, 1991. http://dx.doi.org/10.1007/978-1-4757-0286-6_16.

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"Adsorptive Endocytosis." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_324.

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