scholarly journals Optimization of nano-encapsulation on neonatal porcine islet-like cell clusters using polymersomes

2020 ◽  
Author(s):  
Sang Hoon Lee ◽  
Hyun-Ouk Kim ◽  
Jung-Taek Kang
Keyword(s):  
Extracellular Matrix ◽  
Polyethylene Glycol ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Culture Medium ◽  
Cell Clusters ◽  
Porcine Islet ◽  
Minimal Damage ◽  
Amine Groups

Abstract ObjectiveResearches proving methods for nano encapsulation of neonatal porcine islet-like cell clusters (NPCCs) using polymersomes (PSomes) formed using polymers of polyethylene glycol-block-poly lactide (PEG-b-PLA). Herein, our studies present efficient nano encapsulation procedure with minimal damage and loss of NPCCs. MethodsWe used N-hydroxysuccinimide (NHS) on the N-terminal of PSomes to induce binding of amine groups in the extracellular matrix surrounding NPCCs. F-10 culture medium with bovine serum albumin was used in the nano-encapsulation procedure to minimize damage and loss of NPCCs. Finally, we induced crosslinking between bi-functional PSomes (NHS-/NH2-PSomes). ResultsF-10 culture medium containing 0.25% BSA with pH of 7.3 minimized the damage and loss of NPCCs after nano-encapsulation as compared with using basic HBSS buffer (pH 8.0). Also, we induced the efficiency nano encapsulation through conjugation of PSomes using bi-functional PSomes (NHS-/NH2-PSomes).

scholarly journals Optimization of Nano-encapsulation on Neonatal Porcine Islet-like Cell Clusters Using Polymersomes

2021 ◽  
Vol 16 (1) ◽  
Author(s):  
Sang Hoon Lee ◽  
Hyun-Ouk Kim ◽  
Jung-Taek Kang
Keyword(s):  
Extracellular Matrix ◽  
Polyethylene Glycol ◽  
Bovine Serum Albumin ◽  
Bovine Serum ◽  
Culture Medium ◽  
Cross Linking ◽  
Cell Clusters ◽  
Porcine Islet ◽  
Minimal Damage ◽  
Amine Groups

AbstractResearches proving methods for nano-encapsulation of neonatal porcine islet-like cell clusters (NPCCs) using polymersomes (PSomes) formed using polymers of polyethylene glycol-block-poly lactide. Herein, our studies present efficient nano-encapsulation procedure with minimal damage and loss of NPCCs.We used N-hydroxysuccinimide (NHS) on the N-terminal of PSomes to induce binding of amine groups in the extracellular matrix surrounding NPCCs. F-10 culture medium with bovine serum albumin was used in the nano-encapsulation procedure to minimize damage and loss of NPCCs. Finally, we induced cross-linking between bifunctional PSomes (NHS-/NH2-PSomes). F-10 culture medium containing 0.25% BSA with pH of 7.3 minimized the damage and loss of NPCCs after nano-encapsulation as compared with using basic HBSS buffer (pH 8.0). Also, we induced the efficient nano-encapsulation through conjugation of PSomes using bifunctional PSomes (NHS-/NH2-PSomes).

Bovine serum albumin contained in culture medium used in artificial insemination is an important anaphylaxis risk factor

2008 ◽  
Vol 90 (5) ◽  
pp. 2013.e17-2013.e19 ◽  
Author(s):  
Juan A. Pagán ◽  
Idoia Postigo ◽  
Jorge R. Rodríguez-Pacheco ◽  
Maribel Peña ◽  
Jorge A. Guisantes ◽  
...  
Keyword(s):  
Risk Factor ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Artificial Insemination ◽  
Bovine Serum ◽  
Culture Medium

Albumin reduces basement membrane hydraulic conductance in part due to arginyl side groups

1995 ◽  
Vol 269 (5) ◽  
pp. H1514-H1521 ◽  
Author(s):  
M. A. Katz ◽  
M. L. La Marche
Keyword(s):  
Extracellular Matrix ◽  
Bovine Serum Albumin ◽  
Basement Membrane ◽  
Serum Albumin ◽  
Protective Effect ◽  
Binding Sites ◽  
Bovine Serum ◽  
Hydraulic Conductance ◽  
Experimental Control ◽  
Low Concentrations

Albumin reduces capillary hydraulic conductance (Lp) even at low concentrations. To determine if part of this barrier protective effect might be extracellular, we studied the effects of bovine serum albumin (BSA) on Lp of self-assembled basement membrane (Matrigel). Lp with tris(hydroxymethyl)aminomethane (Tris) buffer superfusate was stable at 1.77 +/- 0.22 x 10(-5) (SE) cm.s-1.cmH2O-1 over several hours. At 0.1 g/dl BSA, experimental/control (Tris) Lp fell to 83.1 +/- 6.0% (2P < 0.025), with decreases to 72.4 +/- 3.7% at 1 g/dl (2P < 0.005), 45.3 +/- 5.1% at 2.5 g/dl (2P < 0.001), and 45.0 +/- 4.8% at 4.0 g/dl (2P < 0.001). In separate experiments, BSA arginine groups were neutralized by 1,2-cyclohexanedione (CHD), and experimental/control Lp values were measured. At 2.5 g/dl, CHD-BSA depressed Lp to 54.4 +/- 4.8%, while unmodified BSA reduced Lp to 40.8 +/- 3.5% of Tris control (2P = 0.05). Finally, soluble arginine at three- and sixfold the arginine in BSA was added to BSA superfusate. For threefold, Lp rose to 120 +/- 8% of BSA level and for sixfold to 129 +/- 9% (2P < 0.05). We conclude that some part of the albumin protective effect is very likely due to consequences on extracellular matrix and that at least 18-22% of this effect is related to arginine groups on albumin when computed from Lp, and up to 34% when viscosity is taken into account. Membrane-saturable arginine-binding sites can be unbound with arginine, thus nullifying part of the barrier protective effect of BSA.

Human corticotropin (ACTH) radioimmunoassay with synthetic 1--24 ACTH.

1979 ◽  
Vol 25 (7) ◽  
pp. 1267-1273 ◽  
Author(s):  
P C Kao ◽  
N S Jiang ◽  
P C Carpenter
Keyword(s):  
Polyethylene Glycol ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Confidence Limit ◽  
Normal Subjects ◽  
Cross Reactivity ◽  
Normal Range ◽  
Beta Endorphin

Abstract A corticotropin antiserum was obtained from rabbits immunized with synthetic 1--24 corticotropin conjugated with bovine serum albumin. The antiserum did not cross react with synthetic alpha-melanotropin or with synthetic beta-endorphin and had a cross reactivity of 0.23% with human beta-lipotropin. We developed a radioimmunoassay with the antiserum obtained, in which we used polyethylene glycol in conjunction with a second precipitating antibody for fast (15-min) separation of antibody-bound and free corticotropin. The assay had a sensitivity of 16 ng/L and was validated on patients with various pituitary and adrenal diseases. From 103 normal subjects, the median value for corticotropin in specimens collected during the morning was 34 ng/L of plasma; the upper 95% confidence limit of the normal range was 98 ng/L.

A Method of Obtaining a Suspension of Intact Parenchymal Cells from Adult Rat Liver

1971 ◽  
Vol 8 (1) ◽  
pp. 73-86
Author(s):  
JENNIFER J. GALLAI-HATCHARD ◽  
G. M. GRAY
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Culture Medium ◽  
High Yield ◽  
Alkaline Ph ◽  
High Osmolarity ◽  
Adult Rat ◽  
Parenchymal Cells ◽  
Phosphate Buffered Saline

The perfusion of liver with either citrate or tetraphenyl boron to remove Ca2+ or K+ or with a solution of high osmolarity and alkaline pH yields plenty of cells but they are all damaged. Perfusion of the liver with hyaluronidase and collagenase followed by incubation of liver slices in the same enzyme solution produced a high yield of cells (25%, w/w, of liver) of which only about 1% were undamaged. However, perfusion with 0.3% hyaluronidase, 0.3% collagenase and 0.1% trypsin in phosphate-buffered saline (excluding Mg2+ and Ca2+) followed by incubation at 25 °C of the chopped liver gave a small yield (2-4%, w/w) of undamaged cells which were not permeable to eosin for up to an hour when suspended in culture medium containing 2% bovine serum albumin.

Interaction Mechanism between Bovine Serum Albumin and Polyethylene Glycol Revealed with Elastic Light Scattering Spectroscopy

2013 ◽  
Vol 704 ◽  
pp. 43-50
Author(s):  
Wen Zhi Zhang ◽  
Kuan Zhang ◽  
Jian Long Zheng ◽  
Hong Shu Chen ◽  
Wei Xing Chen ◽  
...  
Keyword(s):  
Polyethylene Glycol ◽  
Light Scattering ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Interaction Mechanism ◽  
Interaction Force ◽  
Elastic Light Scattering ◽  
Apparent Binding Constant ◽  
Light Scattering Spectroscopy

In order to gain deeper insight into the interaction mechanism between bovine serum albumin (BSA) and polyethylene glycol (PEG), the present work applied elastic light scattering (ELS) spectroscopy to investigate the interaction between BSA and PEG, and explore the effects of concentration and molecular weight of PEG on the interaction at physiological pH. The results showed that the interaction force existed between linear PEG and spherical BSA molecules was mainly hydrogen bonding. In addition, the apparent binding constant of system was evaluated by model calculation.

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