Chemotactic properties, cellular binding and uptake of peptides and peptide derivatives: studies with Tetrahymena thermophila

1992 ◽  
Vol 103 (2) ◽  
pp. 565-570
Author(s):  
V. Leick
Keyword(s):  
Bovine Serum Albumin ◽  
Cell Surface ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Tetrahymena Thermophila ◽  
Chemotactic Peptide ◽  
Dansyl Group ◽  
Peptide Derivatives

Receptor-mediated binding of leukocyte chemotactic peptide, N-formylMet-Leu-Phe (fMLP), occurs in the ciliated protozoon Tetrahymena thermophila. In vivo labelling of the cells with N-formylMet-Leu-[3H]Phe ([3H]fMLP) shows that the cells bind the ligand with high affinity (KD = 4 × 10(−9) M to 1 × 10(−8) M). Moreover, Scatchard transformations of the binding data show that there are about 5 × 10(5) binding sites per cell on the cell surface. Two fluorescent derivatives of leukocyte chemotactic peptide, N-dansylMet-Leu-Phe (dansMLP) and N-formylMet-Leu-Phe-(N-dansyl-)Lys (fMLPdanLys) compete for the N-formylMet-Leu-Phe (fMLP) binding sites on the cell surface. Moreover, both derivatives have retained significant chemoattracting potentials. Fluorescence from dansMLP, but not from fMLPdansLys and dansyl-beta-endorphin, is internalized preferentially into small vesicles. The differences may, however, reflect that the fluorescence from the dansyl group is strongly quenched by a hydrophilic microenvironment when using the two latter peptide derivatives. In contrast, the dansyl group from dansMLP must be assumed to be embedded in a hydrophobic microenvironment in the vesicular membrane or membrane protein. Rhodamine-labelled bovine serum albumin, egg albumin and cytochrome c as well as dansylated bovine serum albumin, which are poor chemoattractants, are preferentially seen to be internalized into large vesicles (food vacuoles).

UCNP@BSA@Ru nanoparticles with tumor-specific and NIR-triggered efficient PACT activity in vivo

2021 ◽  
Author(s):  
Chao Zhang ◽  
Xusheng Guo ◽  
Xuwen Da ◽  
Yishan Yao ◽  
Haihua Xiao ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Short Wavelength ◽  
Ru Nanoparticles ◽  
Wavelength Absorption ◽  
Tumor Accumulation ◽  
Accumulation Ability

Ru(II)-based photoactivated chemotherapy (PACT) agents are promising, however, the short wavelength absorption (generally < 550 nm) and poor tumor accumulation ability limit their in vivo applications. Herein bovine serum albumin...

BSA directed-synthesis of biocompatible Fe3O4 nanoparticles for dual-modal T1 and T2 MR imaging in vivo

2017 ◽  
Vol 9 (21) ◽  
pp. 3099-3104 ◽  
Author(s):  
Dong Li ◽  
Minghui Hua ◽  
Kun Fang ◽  
Rong Liang
Keyword(s):  
Bovine Serum Albumin ◽  
Mr Imaging ◽  
Serum Albumin ◽  
Fe3o4 Nanoparticles ◽  
Bovine Serum ◽  
Mild Conditions ◽  
Directed Synthesis ◽  
T1 And T2

Bovine serum albumin-Fe3O4 nanoparticles with undoubted biosafety and robust dual-modal T1 and T2 MR imaging ability were fabricated using a biomineralization approach in a facile way under mild conditions for in vivo MR imaging.

scholarly journals Clearance and binding of native and defucosylated lactoferrin

1983 ◽  
Vol 212 (2) ◽  
pp. 249-257 ◽  
Author(s):  
M J Imber ◽  
S V Pizzo
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Binding ◽  
Gel Filtration ◽  
Peritoneal Macrophages ◽  
Mononuclear Phagocyte ◽  
Stable Complex

These studies explore the role of carbohydrate recognition systems and the direct involvement of terminal alpha 1-3-linked fucose in the clearance of lactoferrin from the murine circulation and in the specific binding of lactoferrin to receptors on murine peritoneal macrophages. As previously reported, radiolabelled lactoferrin cleared very rapidly (t1/2 less than 1 min) after intravenous injection into mice. However, competing levels of ligands specific for the hepatic galactose receptor (asialo-orosomucoid), the hepatic fucose receptor (fucosyl-bovine serum albumin), and the mononuclear-phagocyte system pathway recognizing mannose, N-acetylglucosamine and fucose (mannosyl-, N-acetylglucosaminyl- and fucosyl-bovine serum albumin) did not block radiolabelled lactoferrin clearance in vivo or binding to mouse peritoneal macrophage monolayers in vitro. Almond emulsin alpha 1-3-fucosidase was used to prepare defucosylated lactoferrin in which 88% of the alpha 1-3-linked fucose was hydrolysed. No difference in clearance or receptor binding was observed between radiolabelled native and defucosylated lactoferrin. Fucoidin, a fucose-rich algal polysaccharide, completely inhibits the clearance in vivo and macrophage binding in vitro of lactoferrin. This effect, however, is probably not the result of competition for binding to the fucose receptor, since gel-filtration studies demonstrated formation of a stable complex between lactoferrin and fucoidin. The present results indicate that the lactoferrin-clearance pathway is distinct from several pathways mediating glycoprotein clearance through recognition of terminal galactose, fucose, N-acetylglucosamine or mannose. Furthermore, alpha 1-3-linked fucose on lactoferrin is not essential for lactoferrin clearance in vivo or specific binding to macrophage receptors in vitro.

Corona protein impacts on alternating current biosusceptometry signal and circulation times of differently coated MnFe2O4 nanoparticles

Nanomedicine ◽  
2021 ◽  
Author(s):  
Andre Gonçalves Prospero ◽  
Lais Pereira Buranello ◽  
Carlos AH Fernandes ◽  
Lucilene Delazari dos Santos ◽  
Guilherme Soares ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Signal Intensity ◽  
Alternating Current ◽  
Circulation Time ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

Background: We evaluated the impacts of corona protein (CP) formation on the alternating current biosusceptometry (ACB) signal intensity and in vivo circulation times of three differently coated magnetic nanoparticles (MNP): bare, citrate-coated and bovine serum albumin-coated MNPs. Methods: We employed the ACB system, gel electrophoresis and mass spectrometry analysis. Results: Higher CP formation led to a greater reduction in the in vitro ACB signal intensity and circulation time. We found fewer proteins forming the CP for the bovine serum albumin-coated MNPs, which presented the highest circulation time in vivo among the MNPs studied. Conclusion: These data showed better biocompatibility, stability and magnetic signal uniformity in biological media for bovine serum albumin-coated MNPs than for citrate-coated MNPs and bare MNPs.

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.

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