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Literatura académica sobre el tema "Receptor mediated transcytosis"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 4 de febrero de 2022

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Artículos de revistas sobre el tema "Receptor mediated transcytosis"

Dehouck, Bénédicte, Laurence Fenart, Marie-Pierre Dehouck, Annick Pierce, Gérard Torpier y Roméo Cecchelli. "A New Function for the LDL Receptor: Transcytosis of LDL across the Blood–Brain Barrier". Journal of Cell Biology 138, n.º 4 (25 de agosto de 1997): 877–89. http://dx.doi.org/10.1083/jcb.138.4.877.

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Lipoprotein transport across the blood–brain barrier (BBB) is of critical importance for the delivery of essential lipids to the brain cells. The occurrence of a low density lipoprotein (LDL) receptor on the BBB has recently been demonstrated. To examine further the function of this receptor, we have shown using an in vitro model of the BBB, that in contrast to acetylated LDL, which does not cross the BBB, LDL is specifically transcytosed across the monolayer. The C7 monoclonal antibody, known to interact with the LDL receptor-binding domain, totally blocked the transcytosis of LDL, suggesting that the transcytosis is mediated by the receptor. Furthermore, we have shown that cholesterol-depleted astrocytes upregulate the expression of the LDL receptor at the BBB. Under these conditions, we observed that the LDL transcytosis parallels the increase in the LDL receptor, indicating once more that the LDL is transcytosed by a receptor-mediated mechanism. The nondegradation of the LDL during the transcytosis indicates that the transcytotic pathway in brain capillary endothelial cells is different from the LDL receptor classical pathway. The switch between a recycling receptor to a transcytotic receptor cannot be explained by a modification of the internalization signals of the cytoplasmic domain of the receptor, since we have shown that LDL receptor messengers in growing brain capillary ECs (recycling LDL receptor) or differentiated cells (transcytotic receptor) are 100% identical, but we cannot exclude posttranslational modifications of the cytoplasmic domain, as demonstrated for the polymeric immunoglobulin receptor. Preliminary studies suggest that caveolae are likely to be involved in the potential transport of LDL from the blood to the brain.

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Hansen, S. H. y J. E. Casanova. "Gs alpha stimulates transcytosis and apical secretion in MDCK cells through cAMP and protein kinase A." Journal of Cell Biology 126, n.º 3 (1 de agosto de 1994): 677–87. http://dx.doi.org/10.1083/jcb.126.3.677.

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Recent evidence suggests a role for heterotrimeric G proteins in vesicular transport. Cholera toxin, which activates Gs alpha by ADP-ribosylation, has been reported to stimulate both apical secretion (Pimplikar, S.W., and K. Simons. 1993. Nature (Lond.). 352:456-458) and apically directed transcytosis (Bomsel, M., and K.E. Mostov. 1993. J. Biol. Chem. 268:25824-25835) in MDCK cells, via a cAMP-independent mechanism. Here, we demonstrate that apical secretion and apically directed transcytosis are significantly stimulated by agents that elevate cellular cAMP. Forskolin, which activates adenylyl cyclase directly, and 8BrcAMP augment both transport processes in MDCK cells. The increase is not limited to receptor-mediated transport (polymeric Ig receptor), since transcytosis of ricin, a galactose-binding lectin, is similarly stimulated. The effects of elevated cellular cAMP on apical secretion and transcytosis are apparently mediated via protein kinase A (PKA), as they are inhibited by H-89, a selective PKA inhibitor. Experiments employing a 17 degrees C temperature block indicate that cAMP/PKA acts at a late, possibly rate-limiting stage in the transcytotic pathway, after translocation of internalized markers into the apical cytoplasm. However, no significant stimulus of apical recycling was observed in the presence of FSK, suggesting that cAMP/PKA either affects transcytosis at a level proximal to apical early endosomes and/or specifically increases the efficiency by which transcytosing molecules are delivered to the apical plasma membrane. Finally, we overexpressed wild-type Gs alpha and a mutant, Q227L, which constitutively activates adenylyl cyclase, in MDCK cells. Although Q227L increased transcytosis more than wild-type Gs alpha, neither construct was as effective as FSK in stimulating transcytosis, arguing against a significant role of Gs alpha in transcytosis independent of cAMP and PKA.

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Nelms, Bradlee, Natasha Furtado Dalomba y Wayne Lencer. "A targeted RNAi screen identifies factors affecting diverse stages of receptor-mediated transcytosis". Journal of Cell Biology 216, n.º 2 (9 de enero de 2017): 511–25. http://dx.doi.org/10.1083/jcb.201609035.

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Endosome transport by transcytosis is the primary mechanism by which proteins and other large cargo traverse epithelial barriers in normal tissue. Transcytosis is also essential for establishing and maintaining membrane polarity in epithelia and other polarized cells. To identify novel components of this pathway, we conducted a high-throughput RNA interference screen for factors necessary for the bidirectional transcytosis of IgG by the Fcγ receptor FcRn. This screen identified 23 genes whose suppression resulted in a reproducible decrease in FcRn-mediated transcytosis. Pulse-chase kinetic transport assays on four of the top-ranking genes (EXOC2, EXOC7, PARD6B, and LEPROT) revealed distinct effects on the apical and basolateral recycling and transcytotic pathways, demonstrating that these pathways are genetically separable. We also found a strong dependence on PARD6B for apical, but not basolateral, recycling, implicating this cell polarity gene in assembly or maintenance of the apical endosomal system. This dataset yields insights into how vesicular transport is adapted to the specialized functions of differentiated cell types and opens new research avenues into epithelial trafficking.

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Apodaca, G., L. A. Katz y K. E. Mostov. "Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes." Journal of Cell Biology 125, n.º 1 (1 de abril de 1994): 67–86. http://dx.doi.org/10.1083/jcb.125.1.67.

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Classically, the polymeric immunoglobulin receptor and its ligand, IgA, are thought to be sorted from basolateral early endosomes into transcytotic vesicles that directly fuse with the apical plasma membrane. In contrast, we have found that in MDCK cells IgA is delivered from basolateral endosomes to apical endosomes and only then to the apical cell surface. When internalized from the basolateral surface of MDCK cells IgA is found to accumulate under the apical plasma membrane in a compartment that is accessible to two apically added membrane markers: anti-secretory component Fab fragments, and avidin internalized from the biotinylated apical pole of the cell. This accumulation occurs in the presence of apical trypsin, which prevents internalization of the ligand from the apical cell surface. Using a modification of the diaminobenzidine density-shift assay, we estimate that approximately 80% of basolaterally internalized IgA resides in the apical endosomal compartment. In addition, approximately 50% of basolaterally internalized transferrin, a basolateral recycling protein, has access to this apical endosomal compartment and is efficiently recycled back to the basolateral surface. Microtubules are required for the organization of the apical endosomal compartment and it is dispersed in nocodazole-treated cells. Moreover, this compartment is largely inaccessible to fluid-phase markers added to either pole of the cell, and therefore seems analogous to the recycling endosome described in nonpolarized cells. We propose a model in which transcytosis is not a specialized pathway that uses unique transcytotic vesicles, but rather combines portions of pathways used by non-transcytosing molecules.

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Nair, Vidhya, Haaris Khan, Ron Mitchell y Michael U. Shiloh. "Role of M Cells in Human Mucosal Immunity to Mycobacterium tuberculosis". Open Forum Infectious Diseases 4, suppl_1 (2017): S48. http://dx.doi.org/10.1093/ofid/ofx162.111.

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Abstract Background Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB), is a bacterial pathogen that infects roughly one-third of the worldÕs population and causes 1–2 million deaths per year. The current paradigm is that phagocytosis of Mtb by patrolling alveolar macrophages initiates Mtb infection. While this model can account for pulmonary TB, it does not adequately explain the occurrence of extrapulmonary forms of TB that manifest in the absence of obvious lung involvement, such as tuberculous cervical lymphadenitis, also known as scrofula. We hypothesized that specialized epithelial cells called microfold cells (M cells) may be an alternate portal of entry for Mtb. Previously we demonstrated that Mtb is able to transcytose across an epithelial barrier in an M cell dependent manner and that M cell mediated transcytosis is vital for Mtb pathogenesis in a mouse model of tuberculosis. Methods We used an in vitro M-cell mediated translocation assay and a Mtb mutant lacking a key virulence factor, ESAT6. We used biochemistry and genetics to identify a novel receptor for ESAT6. We also developed a novel explanted human adenoid Mtb infection model to study mucosal immunity. Results We now demonstrate that the Mtb virulence factor ESAT6 is necessary and sufficient to mediate binding and transcytosis by M cells in vitro and in vivo, and that uptake of Mtb by M cells requires a unique cell surface ESAT6 receptor. We developed a novel explanted human adenoid model of M cell biology and demonstrate rapid Mtb transcytosis by primary human tissue within 60–120 minutes. Using flow cytometry we find that Mtb is first ingested by M cells and then after transcytosis, by tissue resident antigen-presenting cells. Explanted adenoids from 10 independent donors display a wide range of Mtb uptake. Conclusion We conclude that Mtb ESAT6 is necessary for Mtb uptake by M-cells and that binding and transcytosis require a host receptor. Because explanted adenoids display a wide range of Mtb uptake, M cell mediated transcytosis may confer differential susceptibility to scrofula and disseminated disease. These findings are significant as M cells could potentially serve as the basis for novel therapeutic targets against primary Mtb infection. Disclosures All authors: No reported disclosures.

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Perez Bay, Andres E., Ryan Schreiner, Ignacio Benedicto y Enrique J. Rodriguez-Boulan. "Galectin-4-mediated transcytosis of transferrin receptor". Journal of Cell Science 127, n.º 20 (1 de septiembre de 2014): 4457–69. http://dx.doi.org/10.1242/jcs.153437.

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Marinò, Michele, Luca Chiovato, Nicholas Mitsiades, Francesco Latrofa, David Andrews, Sophia Tseleni-Balafouta, A. Bernard Collins, Aldo Pinchera y Robert T. McCluskey. "Circulating Thyroglobulin Transcytosed by Thyroid Cells Is Complexed with Secretory Components of Its Endocytic Receptor Megalin*". Journal of Clinical Endocrinology & Metabolism 85, n.º 9 (1 de septiembre de 2000): 3458–67. http://dx.doi.org/10.1210/jcem.85.9.6804.

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Abstract After its endocytosis from the colloid, some thyroglobulin (Tg) is transcytosed intact across thyrocytes, accounting in part for its presence in the circulation. We previously showed that megalin (gp330), an endocytic Tg receptor, mediates apical to basolateral Tg transcytosis. Here we investigated whether a portion of megalin remains combined with Tg after its transcytosis, using studies with cultured thyroid cells and in vivo observations. FRTL-5 cells, a rat thyroid cell line, cultured on filters in dual chambers form tight junctions and exhibit features of polarity, with expression of megalin exclusively on the upper (apical) surface. After the addition of unlabeled Tg to the upper chamber and incubation at 37 C, some Tg was transcytosed intact across FRTL-5 cells into the lower chamber. Two antimegalin ectodomain antibodies precipitated transcytosed Tg in fluids collected from the lower chamber. After the addition of Tg to surface-biotinylated FRTL-5 cells, an anti-Tg antibody and the two antimegalin ectodomain antibodies precipitated high molecular mass biotinylated material in fluids collected from the lower chamber, corresponding to much of the megalin ectodomain, as well as smaller amounts of lower molecular mass material. The results indicate that Tg transcytosed across FRTL-5 cells remains complexed with megalin ectodomain components, which we refer to as megalin secretory components. In aminotriazole-treated rats, which develop increased megalin-mediated Tg transcytosis, antimegalin antibodies precipitated some of the Tg in the serum. Tg was also precipitated by antimegalin antibodies in sera from patients with Graves’ disease, in which we found increased megalin expression on the apical surface of thyrocytes. In contrast, in thyroidectomized patients with metastatic papillary thyroid carcinoma, in whom Tg is directly secreted by neoplastic thyroid cells into the circulation rather than transcytosed, serum Tg was not precipitated by antimegalin antibodies. The detection of Tg-megalin complexes may help identify the source of serum Tg in patients with thyroid diseases.

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Xiao, Guangqing y Liang-Shang Gan. "Receptor-Mediated Endocytosis and Brain Delivery of Therapeutic Biologics". International Journal of Cell Biology 2013 (2013): 1–14. http://dx.doi.org/10.1155/2013/703545.

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Transport of macromolecules across the blood-brain-barrier (BBB) requires both specific and nonspecific interactions between macromolecules and proteins/receptors expressed on the luminal and/or the abluminal surfaces of the brain capillary endothelial cells. Endocytosis and transcytosis play important roles in the distribution of macromolecules. Due to the tight junction of BBB, brain delivery of traditional therapeutic proteins with large molecular weight is generally not possible. There are multiple pathways through which macromolecules can be taken up into cells through both specific and nonspecific interactions with proteins/receptors on the cell surface. This review is focused on the current knowledge of receptor-mediated endocytosis/transcytosis and brain delivery using the Angiopep-2-conjugated system and the molecular Trojan horses. In addition, the role of neonatal Fc receptor (FcRn) in regulating the efflux of Immunoglobulin G (IgG) from brain to blood, and approaches to improve the pharmacokinetics of therapeutic biologics by generating Fc fusion proteins, and increasing the pH dependent binding affinity between Fc and FcRn, are discussed.

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Cammisotto, Philippe G., Moise Bendayan, Alain Sané, Michel Dominguez, Carole Garofalo y Émile Levy. "Receptor-Mediated Transcytosis of Leptin through Human Intestinal Cells In Vitro". International Journal of Cell Biology 2010 (2010): 1–13. http://dx.doi.org/10.1155/2010/928169.

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Gastric Leptin is absorbed by duodenal enterocytes and released on the basolateral side towards the bloodstream. We investigated in vitro some of the mechanisms of this transport. Caco-2/15 cells internalize leptin from the apical medium and release it through transcytosis in the basal medium in a time- temperature-dependent and saturable fashion. Leptin receptors are revealed on the apical brush-border membrane of the Caco-2 cells. RNA-mediated silencing of the receptor led to decreases in the uptake and basolateral release. Leptin in the basal medium was found bound to the soluble form of its receptor. An inhibitor of clathrin-dependent endocytosis (chlorpromazine) decreased leptin uptake. Confocal immunocytochemistry and the use of brefeldin A and okadaic acid revealed the passage of leptin through the Golgi apparatus. We propose that leptin transcytosis by intestinal cells depends on its receptor, on clathrin-coated vesicles and transits through the Golgi apparatus.

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Haqqani, Arsalan S., Christie E. Delaney, Eric Brunette, Ewa Baumann, Graham K. Farrington, William Sisk, John Eldredge, Wen Ding, Tammy-Lynn Tremblay y Danica B. Stanimirovic. "Endosomal trafficking regulates receptor-mediated transcytosis of antibodies across the blood brain barrier". Journal of Cerebral Blood Flow & Metabolism 38, n.º 4 (15 de noviembre de 2017): 727–40. http://dx.doi.org/10.1177/0271678x17740031.

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Current methods for examining antibody trafficking are either non-quantitative such as immunocytochemistry or require antibody labeling with tracers. We have developed a multiplexed quantitative method for antibody ‘tracking’ in endosomal compartments of brain endothelial cells. Rat brain endothelial cells were co-incubated with blood-brain barrier (BBB)-crossing FC5, monovalent FC5Fc or bivalent FC5Fc fusion antibodies and control antibodies. Endosomes were separated using sucrose-density gradient ultracentrifugation and analyzed using multiplexed mass spectrometry to simultaneously quantify endosomal markers, receptor-mediated transcytosis (RMT) receptors and the co-incubated antibodies in each fraction. The quantitation showed that markers of early endosomes were enriched in high-density fractions (HDF), whereas markers of late endosomes and lysosomes were enriched in low-density fractions (LDF). RMT receptors, including transferrin receptor, showed a profile similar to that of early endosome markers. The in vitro BBB transcytosis rates of antibodies were directly proportional to their partition into early endosome fractions of brain endothelial cells. Addition of the Fc domain resulted in facilitated antibody ‘redistribution’ from LDF into HDF and additionally into multivesicular bodies (MVB). Sorting of various FC5 antibody formats away from late endosomes and lysosomes and into early endosomes and a subset of MVB results in increased antibody transcytosis at the abluminal side of the BBB.

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Más fuentes

Tesis sobre el tema "Receptor mediated transcytosis"

Malcor, Jean-Daniel. "Conception et synthèse de nouveaux ligands du LDLR comme vecteurs ciblant le système nerveux central". Thesis, Montpellier 2, 2011. http://www.theses.fr/2011MON20140/document.

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La distribution de principes actifs dans le système nerveux central (SNC) est entravée par la présence d'une barrière physiologique, la barrière hémato-encéphalique (BHE). L'endothélium cérébral est pourvu d'un large éventail de systèmes de transport, parmi lesquels la trancytose récepteur-dépendante, qui peut être mise à profit pour vectoriser toute une gamme d'agents thérapeutiques vers le SNC de manière non invasive. Dans le cadre de cette approche, le LDLR (Low Density Lipoprotein Receptor), exprimé à la surface de la BHE, est une cible particulièrement intéressante. L'objectif de ce travail est le développement de nouveaux ligands du LDLR en tant que vecteurs potentiels de la BHE. Le criblage d'une librairie de peptides aléatoires dirigée contre le LDLR a permis l'identification d'un peptide 15-mer cyclique ayant une haute affinité in vitro. Une étude des relations structure/activité a ensuite été menée afin d'améliorer l'affinité pour le LDLR et d'augmenter la stabilité plasmatique de ce peptide. Cette étude a abouti à l'identification d'un nouveau peptide « lead » qui a été conjugué à des molécules actives afin d'évaluer la capacité du peptide à vectoriser un principe actif à travers la BHE après administration in vivo chez la souris
Drug delivery to the central nervous system (CNS) is hindered by the presence of a physiological barrier, the blood-brain barrier (BBB). The brain endothelium is endowed with a series of transport systems, including receptor-mediated transcytosis. This system can also be used to transport therapeutics into the brain as a non-invasive manner. Among receptors expressed on the BBB, the low density lipoprotein receptor (LDLR) is relevant as a drug delivery system. This project is dedicated to the development of new peptide-based ligands of LDLR as potential BBB-vectors. The screening of a random peptide library directed to the LDLR led to the identification of hits such as a cyclic 15-mer peptide with high in vitro affinity. A structure/activity relationship study was then carried out in order to improve its affinity towards the LDLR and to increase its plasmatic stability. This study led to the identification of a new lead peptide which was conjugated to bioactive compounds in order to assess the ability of our peptide to shuttle a drug across the BBB following in vivo administration in mice

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Monhasery, Niloufar Verfasser], Jürgen [Gutachter] Scheller y William F. [Gutachter] [Martin. "Transcytosis of Interleukin (IL-)11 and apical redirection of gp130 is mediated by IL-11 -receptor and Identification of MAD2B as a novel regulatory protein of IL-6 classic signaling / Niloufar Monhasery. Gutachter: Jürgen Scheller ; William Martin". Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2016. http://d-nb.info/1101693894/34.

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Monhasery, Niloufar [Verfasser], Jürgen Gutachter] Scheller y William F. [Gutachter] [Martin. "Transcytosis of Interleukin (IL-)11 and apical redirection of gp130 is mediated by IL-11 -receptor and Identification of MAD2B as a novel regulatory protein of IL-6 classic signaling / Niloufar Monhasery. Gutachter: Jürgen Scheller ; William Martin". Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2016. http://d-nb.info/1101693894/34.

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Molino, Yves. "Mise en place de modèles in vitro de barrière hémato‐encéphalique et étude du transfert transendothélial de vecteurs et conjugués ciblant le récepteur au LDL". Thesis, Aix-Marseille, 2015. http://www.theses.fr/2015AIXM5076/document.

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La barrière hémato-encéphalique (BHE) protège le système nerveux central (SNC) des fluctuations plasmatiques des molécules endogènes, mais aussi exogènes, et notamment des molécules à potentiel thérapeutique. L’imperméabilité de la BHE est compensée par la présence de mécanismes qui assurent le transport transendothélial des nutriments nécessaires au tissu nerveux, parmi lesquels la transcytose relayée par différents récepteurs. Dans le but d’améliorer le transfert d’agents thérapeutiques à travers la BHE, nous développons des « vecteurs » qui se lient à certains de ces récepteurs. Au cours de notre thèse, nous avons développé et optimisé des modèles in vitro de BHE et barrière sang-moelle épinière (BSME) syngéniques de rats et souris, basés sur la co-culture de cellules endothéliales microvasculaires (CEMs) cérébrales (CEMCs) ou spinales (CEMSs) et d'astrocytes. Parmi les récepteurs étudiés, nous montrons que le LDLR est exprimé à la membrane plasmique apicale des CEMCs et qu’il est impliqué dans la transcytose du LDL tout en évitant le compartiment lysosomal, confirmant l’intérêt de son ciblage dans nos approches. Nous montrons que nos vecteurs, conjugués à une molécule organique ou à un cargo protéique, sont endocytés par les CEMCs de façon LDLR-dépendante, évitent le compartiment lysosomal et franchissent la monocouche de CEMCs. Nous avons également mis en place des modèles in vitro de BHE et BSME enflammés, sachant que l’inflammation des CEMs est associée à de nombreuses pathologies du SNC. Ces modèles seront utiles pour évaluer des stratégies de vectorisation ciblant préférentiellement les structures du SNC en situation pathologique
The blood-brain barrier (BBB) protects the central nervous system (CNS) from plasma fluctuations of endogenous, but also exogenous molecules, including therapeutic molecules. The BBB’s restrictive properties are compensated by the presence of different mechanisms that provide transport of nutrients across the BBB, including transcytosis of endogenous ligands mediated by receptors. Our objective is to improve drug delivery across the BBB and we developed “vectors” that target different recpetors. During our thesis we developed and optimized cellular tools and approaches, in particular syngeneic in vitro models of the BBB and blood-spinal cord barrier (BSCB) from both rat and mouse, based on the co-culture of brain (BMECs) or spinal cord (SCMECs) microvascular endothelial cells (MECs) and astrocytes. Among the receptors we studied, we show that the LDL receptor (LDLR) is expressed at the apical plasma membrane of BMECs and confirmed that it is involved in transcytosis of LDL through the vesicular compartment, while avoiding the lysosomal compartment, further establishing its interest as a target receptor. We show that our vectors conjugated to an organic molecule or to a protein cargo are endocytosed by BMECs in a LDLR-dependent manner, avoid the lysosomal compartment and cross the BMEC monolayers. Finally, we developed BBB and BSCB in vitro models in inflammatory conditions, considering that MECs inflammation is associated with many CNS lesions and pathologies. These models will be useful to better understand the inflammatory processes of CNS endothelial cells and to evaluate vectorization strategies preferentially targeting CNS structures in pathological condition

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Wiley, Devin Thomas. "Design of Nanoparticles that Cross the Blood-Brain Barrier by Receptor Mediated Transcytosis". Thesis, 2013. https://thesis.library.caltech.edu/7498/1/Wiley%20PhD%20Thesis.pdf.

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The primary objective of my thesis work is to establish a set of design criteria for nanoparticles whose purpose is to safely and efficiently access the brain after systemic injection. Nanoparticles that can access the brain may be able to deliver therapeutic molecules to the brain that otherwise would be excluded by the blood-brain barrier.

E. coli glycoprotein 96 (Ecgp96) is explored as a candidate receptor on the blood-brain barrier that could potentially facilitate nanoparticle-receptor mediated transcytosis into the brain. Results from studies utilizing PET/CT, SPECT/CT, MRI, Xenogen fluorescence imaging, and confocal microscopy conclude that Ecgp96 is observed in the blood-brain barrier endothelial cells, but is not accessible from the blood of adult or neonatal mice under normal, non-pathological conditions.

Transferrin receptor is a well-characterized receptor on the blood-brain barrier that is accessible from the blood and known to transcytose transferrin. I focused on this receptor and on synthesizing and characterizing a well-defined set of transferrin containing gold nanoparticles of various sizes and transferrin compositions that would be investigated during in-vivo studies. Nanoparticle sizes were measured by DLS and nanoparticle tracking analysis. Zeta potentials were also measured. Nanoparticle transferrin content was directly measured by labeling transferrin with 64Cu and measuring the nanoparticle associated gamma activity. The nanoparticle binding avidities to mouse transferrin receptors were ranked by a silver enhancement fluorescence-based method using the mouse Neruo2A cell line.

Each nanoparticle formulation was systemically injected into mice, and localization in the mouse brain was observed by silver enhancement light microscopy, and TEM. The quantitation of the gold was determined by ICP-MS. Nanoparticles with large amounts of transferrin remain strongly attached to brain endothelial cells, while nanoparticles with less transferrin are capable of both interacting with transferrin receptor on the luminal side of the blood-brain barrier and detaching from transferrin receptor on the brain side of the blood-brain barrier. These results highlight the fact that the nanoparticle avidity must be tuned to maximize the number of nanoparticles exiting the endothelial cells and entering the brain tissue. Lanthanum nitrate perfusion-fixation studies demonstrate that the nanoparticle formulations investigated do not degrade the blood-brain barrier integrity and enter the brain by transferrin receptor-mediated transcytosis. The results from these studies provide initial design criteria for creating nanoparticle therapeutics for delivery to the brain from systemic administrations.

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Capítulos de libros sobre el tema "Receptor mediated transcytosis"

Simionescu, Maya. "Receptor-Mediated Transcytosis of Plasma Molecules by Vascular Endothelium". En Endothelial Cell Biology in Health and Disease, 69–104. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-0937-6_4.

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Courtoy, Pierre-J., Michèle Leruth-Deridder, Jean-Pierre Vaerman y Pierre Baudhuin. "Analytical Subcellular Fractionation of Receptor-Mediated Transcytosis in Rat Hepatocytes". En Endocytosis, 291–300. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-84295-5_36.

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Descamps, Laurence, Marie-Pierre Dehouck, Gérard Torpier y Roméo Cecchelli. "Receptor-Mediated Transcytosis of Transferrin through Blood-Brain Barrier Endothelial Cells". En Biology and Physiology of the Blood-Brain Barrier, 51–54. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4757-9489-2_10.

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"Receptor-mediated transcytosis of peptides". En Brain Drug Targeting, 82–125. Cambridge University Press, 2001. http://dx.doi.org/10.1017/cbo9780511549571.005.

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Amet, Nurmamet, Xiaoying Chen, Hsin-Fang Lee, Jennica Zaro y Wei-Chiang Shen. "Transferrin Receptor–Mediated Transcytosis in Intestinal Epithelial Cells for Gastrointestinal Absorption of Protein Drugs". En Targeted Delivery of Small and Macromolecular Drugs, 31–52. CRC Press, 2010. http://dx.doi.org/10.1201/9781420087734-c3.

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"Chapter Transferrin Receptor–Mediated Transcytosis in Intestinal Epithelial Cells for Gastrointestinal Absorption of Protein Drugs". En Targeted Delivery of Small and Macromolecular Drugs, 47–68. CRC Press, 2010. http://dx.doi.org/10.1201/9781420087734-7.

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