scholarly journals Time Machine: Can a Dye from 1928 be Re-Purposed for Modern, Fluorescence-Based Detection of Amyloid-Like Fibrils?

2019 ◽  
Author(s):  
O. I. Antimonova ◽  
N. A. Grudinina ◽  
V. V. Egorov ◽  
V. V. Ilyin ◽  
Y. A. Zabrodskaya ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Congo Red ◽  
Spectral Properties ◽  
Time Machine ◽  
Spectral Changes ◽  
Fluorescent Spectrum ◽  
Beta 2 ◽  
Beta 2 Microglobulin

AbstractThis manuscript describes the chemical synthesis of a compound similar to fluorene and Congo red, including characterization of its spectral properties. It was shown that the dye, during interaction with amyloid-like fibrils of several proteins (lysozyme, insulin, and beta-2-microglobulin), has the ability to change fluorescent spectrum. In contrast, monomeric forms of these proteins did not induce significant spectral changes.

Characterization of the beta 2-microglobulin endocytic pathway in rat proximal tubule cells

1994 ◽  
Vol 267 (3) ◽  
pp. F380-F389 ◽  
Author(s):  
D. P. Sundin ◽  
M. Cohen ◽  
R. Dahl ◽  
S. Falk ◽  
B. A. Molitoris
Keyword(s):  
Proximal Tubule ◽  
Endocytic Pathway ◽  
Apical Surface ◽  
Uptake Mechanism ◽  
Proximal Tubule Cells ◽  
Tubule Cells ◽  
Beta 2 ◽  
Beta 2 Microglobulin ◽  
Rat Proximal Tubule

The uptake mechanism(s) of low-molecular-weight proteins by proximal tubule cells remains incompletely characterized. We utilized a biochemical and semiquantitative morphological approach to better characterize the endocytic pathway of an anionic protein, beta 2-microglobulin (beta 2M), in the rat proximal tubule. Indirect immunogold techniques revealed beta 2M was taken up via a classic receptor-mediated endocytic pathway. In vitro biochemical and morphological characterization of iodinated beta 2M and gold-conjugated beta 2M (gold-beta 2M) binding to isolated brush-border membrane vesicles (BBMV) documented specific and quantitatively similar binding interactions of the modified beta 2M with BBMV. Kinetic characterization of the in vivo endocytic pathway of gold-beta 2M was undertaken using microinfusion of individual tubules. beta 2M initially bound at the apical surface, was internalized into subapical coated vesicles and delivered to endosomal-like structures within 5 min, and, finally, was concentrated in lysosomal-like structures within 15 min. This uptake was inhibited by excess unconjugated beta 2M. In addition, we directly showed that uptake did not occur across the basolateral surface. Finally, by passing solubilized BBMV over beta 2M affinity columns we were able to isolate binding activity.

Cloning and characterization of a cDNA encoding walleye (Sander vitreum) beta-2 microglobulin

2007 ◽  
Vol 22 (6) ◽  
pp. 727-733 ◽  
Author(s):  
Darah Christie ◽  
Guang Wei ◽  
Kazuhiro Fujiki ◽  
Brian Dixon
Keyword(s):  
Beta 2 ◽  
Beta 2 Microglobulin

Characterization of arrangement and expression of the beta-2 microglobulin locus in the sandbar and nurse shark

2010 ◽  
Vol 34 (2) ◽  
pp. 189-195 ◽  
Author(s):  
Hao Chen ◽  
Sarika Kshirsagar ◽  
Ingvill Jensen ◽  
Kevin Lau ◽  
Caitlin Simonson ◽  
...  
Keyword(s):  
Nurse Shark ◽  
Beta 2 ◽  
Beta 2 Microglobulin

scholarly journals Identification and Molecular Characterization of Z/ZE Lineage MHC Class I Heavy Chain Homologue and ^|^beta;2-microglobulin from Rock Bream Oplegnathus fasciatus

2014 ◽  
Vol 49 (3) ◽  
pp. 93-112 ◽  
Author(s):  
Chamilani Nikapitiya ◽  
Sung-Ju Jung ◽  
Myung-Hwa Jung ◽  
Jun-Young Song ◽  
Jehee Lee ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Mhc Class I ◽  
Heavy Chain ◽  
Class I ◽  
Oplegnathus Fasciatus ◽  
Rock Bream ◽  
Beta 2 ◽  
Beta 2 Microglobulin

Purification and characterization of mouse beta-2 microglobulin: Allelic variants from two different strains

1982 ◽  
Vol 19 (3) ◽  
pp. 435-446 ◽  
Author(s):  
Lata Ramanathan ◽  
Garrett C. Dubois ◽  
Elizabeth A. Robinson ◽  
Ettore Appella
Keyword(s):  
Purification And Characterization ◽  
Allelic Variants ◽  
Beta 2 ◽  
Different Strains ◽  
Beta 2 Microglobulin

scholarly journals Activated human T lymphocytes express MHC class I heavy chains not associated with beta 2-microglobulin.

1990 ◽  
Vol 171 (5) ◽  
pp. 1431-1442 ◽  
Author(s):  
E Schnabl ◽  
H Stockinger ◽  
O Majdic ◽  
H Gaugitsch ◽  
I J Lindley ◽  
...  
Keyword(s):  
T Lymphocytes ◽  
Mhc Class I ◽  
Hla Class I ◽  
Class I ◽  
Heavy Chains ◽  
Human T Lymphocytes ◽  
Beta 2 ◽  
Beta 2 Microglobulin ◽  
Mhc Class I Molecules

We present here the molecular characterization of a new activation-induced surface structure on human T lymphocytes, termed LA45, with high homology (93% at protein level) to MHC class I molecules. Antigen modulation and sequential immunoprecipitation experiments revealed that LA45 and HLA class I proteins do not crossreact with the corresponding antibodies. Furthermore, LA45 is not associated with beta 2-m. On the other hand, we could show that the separation of HLA-A,B,C and beta 2m molecules, induced by SDS-denaturation, leads to a conformational change in the heavy chain in such a way that it becomes reactive with LA45. The 90/45 kD LA45 proteins thus appear to be non-beta 2m-associated MHC class I alpha chains that are selectively expressed by activated but not by resting human T lymphocytes.

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