Effect of Low-Intensity (3.75-25 J/cm2) Near-Infrared (810 nm) Laser Radiation on Red Blood Cell ATPase Activities and Membrane Structure

2004 ◽  
Vol 22 (2) ◽  
pp. 111-117 ◽  
Author(s):  
Jolanta Kujawa ◽  
Leu Zavodnik ◽  
Ilya Zavodnik ◽  
Vyacheslav Buko ◽  
Alena Lapshyna ◽  
...  
Keyword(s):  
Laser Radiation ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Membrane Structure ◽  
Near Infrared ◽  
Low Intensity

Facile phase transfer of hydrophobic Fe3O4@Cu2−xS nanoparticles by red blood cell membrane for MRI and phototherapy in the second near-infrared window

2020 ◽  
Vol 8 (6) ◽  
pp. 1202-1211 ◽  
Author(s):  
Kecan Lin ◽  
Yanbing Cao ◽  
Dongye Zheng ◽  
Qin Li ◽  
Hui Liu ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Near Infrared ◽  
Phase Transfer ◽  
Red Blood Cell Membrane ◽  
Theranostic Agents ◽  
Infrared Window

Theranostic agents for MRI and NIR II phototherapy by using red blood cell membrane for phase transfer of Fe3O4@Cu2−xS nanoparticles.

Fabrication of red blood cell membrane-camouflaged Cu2−xSe nanoparticles for phototherapy in the second near-infrared window

2019 ◽  
Vol 55 (46) ◽  
pp. 6523-6526 ◽  
Author(s):  
Zhou Liu ◽  
Jinquan Wang ◽  
Kangqiang Qiu ◽  
Xinxing Liao ◽  
Thomas W. Rees ◽  
...  
Keyword(s):  
Photodynamic Therapy ◽  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Near Infrared ◽  
Red Blood Cell Membrane ◽  
Photodynamic Therapy Of Cancer ◽  
Se Nanoparticles ◽  
Infrared Window

Cu2−xSe nanoparticles (Cu2−xSeNPs) were camouflaged with a red blood cell membrane (RBC) for synergistic photothermal and photodynamic therapy of cancer in the second near-infrared (NIR II) window.

scholarly journals A Markedly Disrupted Skeletal Network With Abnormally Distributed Intramembrane Particles in Complete Protein 4.1-Deficient Red Blood Cells (Allele 4.1 Madrid): Implications Regarding a Critical Role of Protein 4.1 in Maintenance of the Integrity of the Red Blood Cell Membrane

Blood ◽  
1997 ◽  
Vol 90 (6) ◽  
pp. 2471-2481 ◽  
Author(s):  
Ayumi Yawata ◽  
Akio Kanzaki ◽  
Florinda Gilsanz ◽  
Jean Delaunay ◽  
Yoshihito Yawata
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Red Blood Cell ◽  
Membrane Structure ◽  
Critical Role ◽  
Electron Microscopic ◽  
Intramembrane Particles ◽  
Protein 4.1 ◽  
Red Blood Cell Membrane

Abstract Electron microscopic (EM) studies were performed to clarify the interactions of membrane proteins in the red blood cell membrane structure in situ of a homozygous patient with total deficiency of protein 4.1 who carried a point mutation of the downstream translation initiation codon (AUG → AGG) of the protein 4.1 gene [the 4.1 (−) Madrid; Dalla Venezia et al, J Clin Invest 90:1713, 1992]. Immunologically, as expected, protein 4.1 was completely missing in the red blood cell membrane structure in situ. A markedly disrupted skeletal network was observed by EM using the quick-freeze deep-etching method and the surface replica method, although the number of spectrin molecules was only minimally reduced (395 ± 63/μm2; normal, 504 ± 36/μm2). The number of basic units in the skeletal network was strikingly reduced (131 ± 21/μm2; normal, 548 ± 39/μm2), with decreased small-sized units (17 ± 4/μm2; normal, 384 ± 52/μm2) and increased large-sized units (64% ± 14%; normal, 5% ± 1%). Concomitantly, immuno-EM disclosed striking clustering of spectrin molecules with aggregated ankyrin molecules in the red blood cell membrane structure in situ. Although no quantitative abnormalities in the number and size distribution of the intramembrane particles were observed, there was a disappearance of regular distribution, with many clusters of various sizes, probably reflecting the distorted skeletal network. Therefore, protein 4.1 suggests by EM to play a crucial role in maintenance of the normal integrity of the membrane structure in situ not only of the skeletal network but also of the integral proteins.

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