Shape-dependent internalization kinetics of nanoparticles by membranes

Soft Matter ◽  
2016 ◽  
Vol 12 (9) ◽  
pp. 2632-2641 ◽  
Author(s):  
Liping Chen ◽  
Shiyan Xiao ◽  
Hong Zhu ◽  
Lei Wang ◽  
Haojun Liang
Keyword(s):  
Internalization Kinetics ◽  
Kinetics Of

scholarly journals Receptor activation and 2 distinct COOH-terminal motifs control G-CSF receptor distribution and internalization kinetics

Blood ◽  
2004 ◽  
Vol 103 (2) ◽  
pp. 571-579 ◽  
Author(s):  
Lambertus H. J. Aarts ◽  
Onno Roovers ◽  
Alister C. Ward ◽  
Ivo P. Touw
Keyword(s):  
Fluorescent Protein ◽  
Surface Expression ◽  
Receptor Activation ◽  
Cell Surface Expression ◽  
Serine Threonine Kinase ◽  
Late Endosomes ◽  
Dileucine Motif ◽  
Internalization Kinetics ◽  
Green Fluorescent ◽  
Kinetics Of

Abstract We have studied the intracellular distribution and internalization kinetics of the granulocyte colony-stimulating factor receptor (G-CSF-R) in living cells using fusion constructs of wild-type or mutant G-CSF-R and enhanced green fluorescent protein (EGFP). Under steady-state conditions the G-CSF-R localized predominantly to the Golgi apparatus, late endosomes, and lysosomes, with only low expression on the plasma membrane, resulting from spontaneous internalization. Internalization of the G-CSF-R was significantly accelerated by addition of G-CSF. This ligand-induced switch from slow to rapid internalization required the presence of G-CSF-R residue Trp650, previously shown to be essential for its signaling ability. Both spontaneous and ligand-induced internalization depended on 2 distinct amino acid stretches in the G-CSF-R COOH-terminus: 749-755, containing a dileucine internalization motif, and 756-769. Mutation of Ser749 at position –4 of the dileucine motif to Ala significantly reduced the rate of ligand-induced internalization. In contrast, mutation of Ser749 did not affect spontaneous G-CSF-R internalization, suggesting the involvement of a serine-threonine kinase specifically in ligand-accelerated internalization of the G-CSF-R. COOH-terminal truncation mutants of G-CSF-R, found in severe congenital neutropenia, lack the internalization motifs and were completely defective in both spontaneous and ligand-induced internalization. As a result, these mutants showed constitutively high cell-surface expression.

Internalization kinetics of the gonadotropin-releasing hormone (GnRH) receptor

2000 ◽  
Vol 439 (7) ◽  
pp. R19-R20
Author(s):  
Milka Vrecl ◽  
Anders Heding ◽  
Aylin Hanyaloglu ◽  
Philip L. Taylor ◽  
Karin A. Eidne
Keyword(s):  
Gnrh Receptor ◽  
Gonadotropin Releasing Hormone ◽  
Releasing Hormone ◽  
Internalization Kinetics ◽  
Kinetics Of

Internalization kinetics of the gonadotropin-releasing hormone (GnRH) receptor

2000 ◽  
Vol 439 (S1) ◽  
pp. r019-r020 ◽  
Author(s):  
Milka Vrecl ◽  
Anders Heding ◽  
Aylin Hanyaloglu ◽  
Philip L. Taylor ◽  
Karin A. Eidne
Keyword(s):  
Gnrh Receptor ◽  
Gonadotropin Releasing Hormone ◽  
Releasing Hormone ◽  
Internalization Kinetics ◽  
Kinetics Of

Cellular Internalization Kinetics of (Luciferin-)Cell-Penetrating Peptide Conjugates

2010 ◽  
Vol 21 (9) ◽  
pp. 1662-1672 ◽  
Author(s):  
Emelía Eiríksdóttir ◽  
Imre Mäger ◽  
Taavi Lehto ◽  
Samir El Andaloussi ◽  
Ülo Langel
Keyword(s):  
Cell Penetrating Peptide ◽  
Cellular Internalization ◽  
Peptide Conjugates ◽  
Cell Penetrating ◽  
Internalization Kinetics ◽  
Kinetics Of

scholarly journals Contrasting internalization kinetics of human and chicken gonadotropin-releasing hormone receptors mediated by C-terminal tail

1998 ◽  
Vol 156 (3) ◽  
pp. R9-12 ◽  
Author(s):  
AJ Pawson ◽  
A Katz ◽  
YM Sun ◽  
J Lopes ◽  
N Illing ◽  
...  
Keyword(s):  
Gnrh Agonist ◽  
Hormone Receptors ◽  
Cytoplasmic Tail ◽  
Gonadotropin Releasing Hormone ◽  
Receptor Internalization ◽  
Wild Type ◽  
Releasing Hormone ◽  
In The Wild ◽  
Internalization Kinetics ◽  
Kinetics Of

The chicken gonadotropin-releasing hormone receptor (GnRH-R) is notable for having a cytoplasmic C-terminal tail, which is not present in the mammalian GnRH-Rs. We report here that the cytoplasmic tail mediates rapid agonist-promoted receptor internalization. The chicken GnRH-R mediated internalization of gonadotropin-releasing hormone (GnRH) agonist (125I[His5-D-Tyr6]GnRH) at a rate of 11.3%.min-1, compared with only 0.71 %.min-1 for the human GnRH-R. To determine whether the presence of the cytoplasmic tail was responsible for the more rapid internalization kinetics of the chicken GnRH-R we truncated the tail after the Ile336 residue (S337stop). Receptor-mediated internalization of GnRH agonist by the S337stop-chicken GnRH-R was much slower than in the wild-type chicken receptor, and was similar to the wild-type human GnRH-R (0.55 %.min-1). These data indicate that rapid agonist-promoted internalization of the chicken GnRH-R is mediated through elements in the cytoplasmic C-terminal tail, distal to or including Ser337 and suggests that elimination of the C-terminal tail during evolution of mammalian GnRH-Rs may be related to its effects on internalization.

scholarly journals Quantitative Measurement of the Target-Mediated Internalization Kinetics of Biopharmaceuticals

2014 ◽  
Vol 32 (1) ◽  
pp. 286-299 ◽  
Author(s):  
Inna Vainshtein ◽  
Lorin K. Roskos ◽  
Jackie Cheng ◽  
Matthew A. Sleeman ◽  
Bing Wang ◽  
...  
Keyword(s):  
Quantitative Measurement ◽  
Internalization Kinetics ◽  
Kinetics Of

Direct observations of radiation-enhanced transformations in glass

1983 ◽  
Vol 41 ◽  
pp. 354-355
Author(s):  
J. F. DeNatale ◽  
D. G. Howitt
Keyword(s):  
Glass Matrix ◽  
Diffusion Mechanism ◽  
Bubble Formation ◽  
Silicate Glasses ◽  
Phase Decomposition ◽  
Direct Observations ◽  
Thin Foils ◽  
Oxygen Bubble ◽  
Electron Energy Loss ◽  
Kinetics Of

The electron irradiation of silicate glasses containing metal cations produces various types of phase separation and decomposition which includes oxygen bubble formation at intermediate temperatures figure I. The kinetics of bubble formation are too rapid to be accounted for by oxygen diffusion but the behavior is consistent with a cation diffusion mechanism if the amount of oxygen in the bubble is not significantly different from that in the same volume of silicate glass. The formation of oxygen bubbles is often accompanied by precipitation of crystalline phases and/or amorphous phase decomposition in the regions between the bubbles and the detection of differences in oxygen concentration between the bubble and matrix by electron energy loss spectroscopy cannot be discerned (figure 2) even when the bubble occupies the majority of the foil depth.The oxygen bubbles are stable, even in the thin foils, months after irradiation and if van der Waals behavior of the interior gas is assumed an oxygen pressure of about 4000 atmospheres must be sustained for a 100 bubble if the surface tension with the glass matrix is to balance against it at intermediate temperatures.

Sign in / Sign up

Export Citation Format

Share Document