A monoclonal antibody against acetylcholinesterase inhibits the formation of amyloid fibrils induced by the enzyme

Ariel E. Reyes, Daniel R. Perez, Alejandra Alvarez, Jorge Garrido, Mary K. Gentry, Bhupendra P. Doctor, Nibaldo C. Inestrosa

Resultado de la investigación: Article

85 Citas (Scopus)

Resumen

A monoclonal antibody (mAb) 25B1 directed against fetal bovine serum acetylcholinesterase (FBS AChE) was used to examine the ability of the cholinergic enzyme to promote the assembly of amyloid-β peptides (Aβ) into Alzheimers fibrils. This mAb binds to the peripheral anionic site of the enzyme and allosterically inhibits catalytic activity of FBS AChE. Several techniques, including thioflavine-T fluorescence, turbidity, and negative-staining at the electron microscopy level, were used to assess amyloid formation. Inhibition of amyloid formation was dependent on the molar ratio AChE:mAb 25B1, and at least 50% of the inhibition of the AChE promoting effect occurs at a molar ratio similar to that required for inhibition of the esterase activity. Our results suggest that mAb 25B1 inhibits the promotion of the amyloid fibril formation triggered by AChE by affecting the lag period of the Aβ aggregation process.

Idioma originalEnglish
Páginas (desde-hasta)652-655
Número de páginas4
PublicaciónBiochemical and Biophysical Research Communications
Volumen232
N.º3
DOI
EstadoPublished - 27 mar 1997

Huella dactilar

Acetylcholinesterase
Amyloid
Monoclonal Antibodies
Enzymes
Negative Staining
Fetal Movement
Turbidity
Esterases
Serum
Cholinergic Agents
Electron microscopy
Catalyst activity
Electron Microscopy
Agglomeration
Fluorescence

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Citar esto

Reyes, Ariel E. ; Perez, Daniel R. ; Alvarez, Alejandra ; Garrido, Jorge ; Gentry, Mary K. ; Doctor, Bhupendra P. ; Inestrosa, Nibaldo C. / A monoclonal antibody against acetylcholinesterase inhibits the formation of amyloid fibrils induced by the enzyme. En: Biochemical and Biophysical Research Communications. 1997 ; Vol. 232, N.º 3. pp. 652-655.
@article{6edccdf7aed141ff8f7a51e71060fcfb,
title = "A monoclonal antibody against acetylcholinesterase inhibits the formation of amyloid fibrils induced by the enzyme",
abstract = "A monoclonal antibody (mAb) 25B1 directed against fetal bovine serum acetylcholinesterase (FBS AChE) was used to examine the ability of the cholinergic enzyme to promote the assembly of amyloid-β peptides (Aβ) into Alzheimers fibrils. This mAb binds to the peripheral anionic site of the enzyme and allosterically inhibits catalytic activity of FBS AChE. Several techniques, including thioflavine-T fluorescence, turbidity, and negative-staining at the electron microscopy level, were used to assess amyloid formation. Inhibition of amyloid formation was dependent on the molar ratio AChE:mAb 25B1, and at least 50{\%} of the inhibition of the AChE promoting effect occurs at a molar ratio similar to that required for inhibition of the esterase activity. Our results suggest that mAb 25B1 inhibits the promotion of the amyloid fibril formation triggered by AChE by affecting the lag period of the Aβ aggregation process.",
author = "Reyes, {Ariel E.} and Perez, {Daniel R.} and Alejandra Alvarez and Jorge Garrido and Gentry, {Mary K.} and Doctor, {Bhupendra P.} and Inestrosa, {Nibaldo C.}",
year = "1997",
month = "3",
day = "27",
doi = "10.1006/bbrc.1997.6357",
language = "English",
volume = "232",
pages = "652--655",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

A monoclonal antibody against acetylcholinesterase inhibits the formation of amyloid fibrils induced by the enzyme. / Reyes, Ariel E.; Perez, Daniel R.; Alvarez, Alejandra; Garrido, Jorge; Gentry, Mary K.; Doctor, Bhupendra P.; Inestrosa, Nibaldo C.

En: Biochemical and Biophysical Research Communications, Vol. 232, N.º 3, 27.03.1997, p. 652-655.

Resultado de la investigación: Article

TY - JOUR

T1 - A monoclonal antibody against acetylcholinesterase inhibits the formation of amyloid fibrils induced by the enzyme

AU - Reyes, Ariel E.

AU - Perez, Daniel R.

AU - Alvarez, Alejandra

AU - Garrido, Jorge

AU - Gentry, Mary K.

AU - Doctor, Bhupendra P.

AU - Inestrosa, Nibaldo C.

PY - 1997/3/27

Y1 - 1997/3/27

N2 - A monoclonal antibody (mAb) 25B1 directed against fetal bovine serum acetylcholinesterase (FBS AChE) was used to examine the ability of the cholinergic enzyme to promote the assembly of amyloid-β peptides (Aβ) into Alzheimers fibrils. This mAb binds to the peripheral anionic site of the enzyme and allosterically inhibits catalytic activity of FBS AChE. Several techniques, including thioflavine-T fluorescence, turbidity, and negative-staining at the electron microscopy level, were used to assess amyloid formation. Inhibition of amyloid formation was dependent on the molar ratio AChE:mAb 25B1, and at least 50% of the inhibition of the AChE promoting effect occurs at a molar ratio similar to that required for inhibition of the esterase activity. Our results suggest that mAb 25B1 inhibits the promotion of the amyloid fibril formation triggered by AChE by affecting the lag period of the Aβ aggregation process.

AB - A monoclonal antibody (mAb) 25B1 directed against fetal bovine serum acetylcholinesterase (FBS AChE) was used to examine the ability of the cholinergic enzyme to promote the assembly of amyloid-β peptides (Aβ) into Alzheimers fibrils. This mAb binds to the peripheral anionic site of the enzyme and allosterically inhibits catalytic activity of FBS AChE. Several techniques, including thioflavine-T fluorescence, turbidity, and negative-staining at the electron microscopy level, were used to assess amyloid formation. Inhibition of amyloid formation was dependent on the molar ratio AChE:mAb 25B1, and at least 50% of the inhibition of the AChE promoting effect occurs at a molar ratio similar to that required for inhibition of the esterase activity. Our results suggest that mAb 25B1 inhibits the promotion of the amyloid fibril formation triggered by AChE by affecting the lag period of the Aβ aggregation process.

UR - http://www.scopus.com/inward/record.url?scp=0031587755&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1997.6357

DO - 10.1006/bbrc.1997.6357

M3 - Article

C2 - 9126330

AN - SCOPUS:0031587755

VL - 232

SP - 652

EP - 655

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -