Nonenzymatic Glycosylation of Erythrocyte Cytoskeletal Proteins in Diabetes Mellitus1

2015 ◽  
pp. 190-193 ◽  
Author(s):  
Anjaneyulu Kowluru ◽  
Renu A. Kowluru ◽  
Mark W. Bitensky
Keyword(s):  
Cytoskeletal Proteins ◽  
Nonenzymatic Glycosylation

Modulated polarization microscopy displays the dynamics of cytoskeletal structures in living, motile cells

1995 ◽  
Vol 53 ◽  
pp. 902-903
Author(s):  
J. R. Kuhn ◽  
M. Poenie
Keyword(s):  
Mitotic Spindle ◽  
Actin Filaments ◽  
Cell Shape ◽  
Dynamic Structure ◽  
Living Cells ◽  
Cytoskeletal Proteins ◽  
Polarization Microscopy ◽  
Video Enhancement ◽  
Ultrastructural Studies ◽  
Motile Cells

Cell shape and movement are controlled by elements of the cytoskeleton including actin filaments an microtubules. Unfortunately, it is difficult to visualize the cytoskeleton in living cells and hence follow it dynamics. Immunofluorescence and ultrastructural studies of fixed cells while providing clear images of the cytoskeleton, give only a static picture of this dynamic structure. Microinjection of fluorescently Is beled cytoskeletal proteins has proved useful as a way to follow some cytoskeletal events, but long terry studies are generally limited by the bleaching of fluorophores and presence of unassembled monomers.Polarization microscopy has the potential for visualizing the cytoskeleton. Although at present, it ha mainly been used for visualizing the mitotic spindle. Polarization microscopy is attractive in that it pro vides a way to selectively image structures such as cytoskeletal filaments that are birefringent. By combing ing standard polarization microscopy with video enhancement techniques it has been possible to image single filaments. In this case, however, filament intensity depends on the orientation of the polarizer and analyzer with respect to the specimen.

Structural and Chemical Studies of Pathological Fibers in Human Neurofibrillary Degeneration

1985 ◽  
Vol 43 ◽  
pp. 726-729
Author(s):  
K.S. Kosik ◽  
L.K. Duffy ◽  
S. Bakalis ◽  
C. Abraham ◽  
D.J. Selkoe
Keyword(s):  
Monoclonal Antibodies ◽  
Alzheimer Disease ◽  
Human Brain ◽  
Neurofibrillary Tangles ◽  
Morphological Analysis ◽  
High Specificity ◽  
Cytoskeletal Proteins ◽  
Neuritic Plaque ◽  
Protein Chemistry ◽  
Chemical Studies

The major structural lesions of the human brain during aging and in Alzheimer disease (AD) are the neurofibrillary tangles (NFT) and the senile (neuritic) plaque. Although these fibrous alterations have been recognized by light microscopists for almost a century, detailed biochemical and morphological analysis of the lesions has been undertaken only recently. Because the intraneuronal deposits in the NFT and the plaque neurites and the extraneuronal amyloid cores of the plaques have a filamentous ultrastructure, the neuronal cytoskeleton has played a prominent role in most pathogenetic hypotheses.The approach of our laboratory toward elucidating the origin of plaques and tangles in AD has been two-fold: the use of analytical protein chemistry to purify and then characterize the pathological fibers comprising the tangles and plaques, and the use of certain monoclonal antibodies to neuronal cytoskeletal proteins that, despite high specificity, cross-react with NFT and thus implicate epitopes of these proteins as constituents of the tangles.

The Effect of Agonists and Antagonists of Platelet Aggregation on von Willebrand Factor-Mediated Platelet Agglutination

1991 ◽  
Vol 65 (05) ◽  
pp. 573-577 ◽  
Author(s):  
Jean McPherson ◽  
Marjorie B Zucker ◽  
Evelyn A Mauss ◽  
Sandra Brownlea
Keyword(s):  
Receptor Antagonist ◽  
Intracellular Calcium ◽  
Calcium Ions ◽  
Inhibitory Action ◽  
Platelet Rich Plasma ◽  
Cytoskeletal Proteins ◽  
A 23187 ◽  
Sulphydryl Groups ◽  
Affinity Receptor ◽  
Adp Receptor

SummaryRistocetin-induced platelet agglutination (RIPA) in EDTA-treated citrated platelet-rich plasma was reduced to 49 ± 11% by 1.25 ΜM ADP, 41 ± 14% by 1 ΜM A 23187, and 26 ± 7% by 0.1 Μg/ml platelet activating factor (PAF). The effect of 5-110 ΜM epinephrine was not dose-dependent, but varied between donors, with RIPA from 56-100% of the control. The inhibitory effects of these agonists were not altered by prior treatment of platelets with aspirin. Prior addition of 200 ΜM ATP (an ADP receptor antagonist acting at both high and low affinity ADP receptors) prevented the inhibitory action of ADP but not that of A 23187 or PAF, suggesting that the inhibitory actions of the latter are not mediated by released ADP. As 700 ΜM 8-bromoadenosine 5-diphosphate (an ADP receptor antagonist acting mainly at the high affinity receptor) did not prevent ADP-induced inhibition of RIPA, interaction of ADP with the low affinity receptor is presumably responsible for its inhibitory action. As A 23187, but not phorbol myristate acetate (0.1 ΜM) inhibited RIPA, an increase in intracellular calcium ions rather than direct stimulation of protein kinase C appears to mediate agonist-induced inhibition. Cytochalasin B (10.5-21 ΜM), dibucaine (0.5-1 mM), and prostaglandin E1 (25 nM), added before or after the agonist, prevented or reversed ADP-, A23187-, and PAF-induced inhibition of RIPA, suggesting that the state of the platelet cytoskeleton affects inhibition. N-ethylmaleimide (0.25-0.5 mM), an agent that can penetrate cell membranes and block sulphydryl groups, prevented or reversed ADP, A 23187- and PAF-induced inhibition of RIPA, but 0.5 mM dithionitrobisbenzoic acid, a non-penetrating sulphydryl blocker, had no effect. Diamide (0.1-0.5 mM), an agent that can crosslink cytoskeletal proteins by oxidation of sulphydryl groups, reduced RIPA. Thus an increase in intracellular calcium ions with resultant cytoskeletal changes and reorganisation of intracellular sulphydryl groups may mediate the inhibitory action of agonists on RIPA.

Rearrangement of Enterocyte Cytoskeletal Proteins in Coeliac Disease

Endoscopy ◽  
2004 ◽  
Vol 36 (05) ◽  
Author(s):  
S Wilson ◽  
Y Volkov ◽  
C Feighery
Keyword(s):  
Coeliac Disease ◽  
Cytoskeletal Proteins

Nonenzymatic glycosylation of low density lipoproteins in vitro. Effects on cell-interactive properties

Diabetes ◽  
1981 ◽  
Vol 30 (10) ◽  
pp. 875-878 ◽  
Author(s):  
B. Gonen ◽  
J. Baenziger ◽  
G. Schonfeld ◽  
D. Jacobson ◽  
P. Farrar
Keyword(s):  
Low Density Lipoproteins ◽  
Low Density ◽  
Nonenzymatic Glycosylation ◽  
In Vitro Effects

Nonenzymatic glycosylation of laminin and the laminin peptide CIKVAVS inhibits neurite outgrowth

Diabetes ◽  
1993 ◽  
Vol 42 (4) ◽  
pp. 509-513 ◽  
Author(s):  
H. J. Federoff ◽  
D. Lawrence ◽  
M. Brownlee
Keyword(s):  
Neurite Outgrowth ◽  
Nonenzymatic Glycosylation ◽  
Laminin Peptide

Nonenzymatic glycosylation of erythrocytic proteins in normal and diabetic subjects. Enzymes of nucleoside and nucleotide metabolism

Diabetes ◽  
1985 ◽  
Vol 34 (3) ◽  
pp. 251-255 ◽  
Author(s):  
K. C. Agarwal ◽  
R. E. Parks ◽  
J. A. Widness ◽  
R. Schwartz
Keyword(s):  
Nucleotide Metabolism ◽  
Nonenzymatic Glycosylation

The effect of salicylates on nonenzymatic glycosylation and thermal stability of collagen in diabetic rats

Diabetes ◽  
1984 ◽  
Vol 33 (8) ◽  
pp. 745-751 ◽  
Author(s):  
D. K. Yue ◽  
S. McLennan ◽  
D. J. Handelsman ◽  
L. Delbridge ◽  
T. Reeve ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Diabetic Rats ◽  
Nonenzymatic Glycosylation ◽  
Thermal Stability Of

Collagen aging in vitro by nonenzymatic glycosylation and browning

Diabetes ◽  
1984 ◽  
Vol 33 (1) ◽  
pp. 57-59 ◽  
Author(s):  
R. R. Kohn ◽  
A. Cerami ◽  
V. M. Monnier
Keyword(s):  
Nonenzymatic Glycosylation
Sign in / Sign up

Export Citation Format

Share Document