The chick embryo appears as a natural model for research in beta-amyloid precursor protein processing

J. A. Carrodeguas; A. Rodolosse; M. V. Garza; A. Sanz-Clemente; R. Pérez-Pé; A. M. Lacosta; L. Domínguez; I. Monleón; R. Sánchez-Díaz; V. Sorribas; M. Sarasa

doi:10.1016/j.neuroscience.2005.05.020

The chick embryo appears as a natural model for research in beta-amyloid precursor protein processing

J. A. Carrodeguas, A. Rodolosse, M. V. Garza, A. Sanz-Clemente, R. Pérez-Pé, A. M. Lacosta, L. Domínguez, I. Monleón, R. Sánchez-Díaz, V. Sorribas, M. Sarasa^*

^*Corresponding author for this work

Pharmacology

Research output: Contribution to journal › Article › peer-review

35 Scopus citations

Abstract

This study reveals that the chick embryo has active the machinery for the production and degradation of the amyloid beta peptide characteristic of Alzheimer's disease. We cloned the principal beta-amyloid precursor protein isoforms in the chick embryo and observed that they are highly homologous to the human sequences and identical at the C-terminal sequence, including the amyloid beta domain. Mammals such as rat or mouse, more commonly used as animal models of human diseases, have a distinct amyloid beta sequence. The distribution of beta-amyloid precursor protein isoforms in the chick embryo revealed that, as in humans, their expression is ubiquitous and the prototype beta-amyloid precursor protein-695 predominated in the nervous system. We also found that the chick embryo expresses the genes for the main proteolytic proteases implicated in the production of amyloid beta, including BACE-1, BACE-2, presenilin-1, presenilin-2 and nicastrin, as well as the amyloid beta-degrading enzyme neprilysin, or ADAM-17, a protease implicated in the non-amyloidogenic processing of beta-amyloid precursor protein. We have also found that between amyloid beta40 and amyloid beta42, this latter seems to be the major amyloid beta peptide produced during chick embryogenesis. The chick embryo appears as a suitable natural model to study cell biology and developmental function of beta-amyloid precursor protein and a potential assay system for drugs that regulate beta-amyloid precursor protein processing.

Original language	English (US)
Pages (from-to)	1285-1300
Number of pages	16
Journal	Neuroscience
Volume	134
Issue number	4
DOIs	https://doi.org/10.1016/j.neuroscience.2005.05.020
State	Published - 2005

Funding

We thank Dr. M. Villarroel-Robinson for reviewing, Dr. I. Ferrer and Dr. J. Esquerda for reading and comments, Dr. A. Alagón for helpful suggestions, Dr. M. A. Ros for the Sonic hedgehog probe, and Dr. V. García-Martínez for the Paraxis probe. J.A.C is a Programa Ramón y Cajal Research Fellow from the Spanish Ministry of Science and Technology (MCYT). M.V.G., A.S.C., and A.M.L. were supported by grants from the government of Mexico (Programa PROMEP), the Spanish Ministry of Education and the government of Aragon, respectively. This work was supported by grant PO68/2000 (M.S.) from the government of Aragon and in part by PM99-0086 (M.S.) from the MCYT and UZ2002-BIO-01 (J.A.C.) from the University of Zaragoza. Parts of this work were presented in abstract form at the III Forum of European Neuroscience Societies (Paris, July 2002) and the X Congreso de la Sociedad Española de Neurociencia (Lérida, Spain, September 2003). The nucleotide sequences of the cDNAs for the proteins presented in the present work were submitted to GenBank and given accession numbers AF289218 (APP-695), AF289219 (APP-751), AY371190 (nicastrin), AY371191 (neprilysin), AY486554 (presenilin-2), AY486555 (BACE-1), AY486556 (BACE-2) and AY486557 (ADAM-17).

Keywords

ADAM
APP
Alzheimer's disease
Chick embryo
Neprilysin
Secretase

ASJC Scopus subject areas

General Neuroscience

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10.1016/j.neuroscience.2005.05.020

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Carrodeguas, J. A., Rodolosse, A., Garza, M. V., Sanz-Clemente, A., Pérez-Pé, R., Lacosta, A. M., Domínguez, L., Monleón, I., Sánchez-Díaz, R., Sorribas, V., & Sarasa, M. (2005). The chick embryo appears as a natural model for research in beta-amyloid precursor protein processing. Neuroscience, 134(4), 1285-1300. https://doi.org/10.1016/j.neuroscience.2005.05.020

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title = "The chick embryo appears as a natural model for research in beta-amyloid precursor protein processing",

abstract = "This study reveals that the chick embryo has active the machinery for the production and degradation of the amyloid beta peptide characteristic of Alzheimer's disease. We cloned the principal beta-amyloid precursor protein isoforms in the chick embryo and observed that they are highly homologous to the human sequences and identical at the C-terminal sequence, including the amyloid beta domain. Mammals such as rat or mouse, more commonly used as animal models of human diseases, have a distinct amyloid beta sequence. The distribution of beta-amyloid precursor protein isoforms in the chick embryo revealed that, as in humans, their expression is ubiquitous and the prototype beta-amyloid precursor protein-695 predominated in the nervous system. We also found that the chick embryo expresses the genes for the main proteolytic proteases implicated in the production of amyloid beta, including BACE-1, BACE-2, presenilin-1, presenilin-2 and nicastrin, as well as the amyloid beta-degrading enzyme neprilysin, or ADAM-17, a protease implicated in the non-amyloidogenic processing of beta-amyloid precursor protein. We have also found that between amyloid beta40 and amyloid beta42, this latter seems to be the major amyloid beta peptide produced during chick embryogenesis. The chick embryo appears as a suitable natural model to study cell biology and developmental function of beta-amyloid precursor protein and a potential assay system for drugs that regulate beta-amyloid precursor protein processing.",

keywords = "ADAM, APP, Alzheimer's disease, Chick embryo, Neprilysin, Secretase",

author = "Carrodeguas, {J. A.} and A. Rodolosse and Garza, {M. V.} and A. Sanz-Clemente and R. P{\'e}rez-P{\'e} and Lacosta, {A. M.} and L. Dom{\'i}nguez and I. Monle{\'o}n and R. S{\'a}nchez-D{\'i}az and V. Sorribas and M. Sarasa",

note = "Funding Information: We thank Dr. M. Villarroel-Robinson for reviewing, Dr. I. Ferrer and Dr. J. Esquerda for reading and comments, Dr. A. Alag{\'o}n for helpful suggestions, Dr. M. A. Ros for the Sonic hedgehog probe, and Dr. V. Garc{\'i}a-Mart{\'i}nez for the Paraxis probe. J.A.C is a Programa Ram{\'o}n y Cajal Research Fellow from the Spanish Ministry of Science and Technology (MCYT). M.V.G., A.S.C., and A.M.L. were supported by grants from the government of Mexico (Programa PROMEP), the Spanish Ministry of Education and the government of Aragon, respectively. This work was supported by grant PO68/2000 (M.S.) from the government of Aragon and in part by PM99-0086 (M.S.) from the MCYT and UZ2002-BIO-01 (J.A.C.) from the University of Zaragoza. Parts of this work were presented in abstract form at the III Forum of European Neuroscience Societies (Paris, July 2002) and the X Congreso de la Sociedad Espa{\~n}ola de Neurociencia (L{\'e}rida, Spain, September 2003). The nucleotide sequences of the cDNAs for the proteins presented in the present work were submitted to GenBank and given accession numbers AF289218 (APP-695), AF289219 (APP-751), AY371190 (nicastrin), AY371191 (neprilysin), AY486554 (presenilin-2), AY486555 (BACE-1), AY486556 (BACE-2) and AY486557 (ADAM-17).",

year = "2005",

doi = "10.1016/j.neuroscience.2005.05.020",

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T1 - The chick embryo appears as a natural model for research in beta-amyloid precursor protein processing

AU - Carrodeguas, J. A.

AU - Rodolosse, A.

AU - Garza, M. V.

AU - Sanz-Clemente, A.

AU - Pérez-Pé, R.

AU - Lacosta, A. M.

AU - Domínguez, L.

AU - Monleón, I.

AU - Sánchez-Díaz, R.

AU - Sorribas, V.

AU - Sarasa, M.

N1 - Funding Information: We thank Dr. M. Villarroel-Robinson for reviewing, Dr. I. Ferrer and Dr. J. Esquerda for reading and comments, Dr. A. Alagón for helpful suggestions, Dr. M. A. Ros for the Sonic hedgehog probe, and Dr. V. García-Martínez for the Paraxis probe. J.A.C is a Programa Ramón y Cajal Research Fellow from the Spanish Ministry of Science and Technology (MCYT). M.V.G., A.S.C., and A.M.L. were supported by grants from the government of Mexico (Programa PROMEP), the Spanish Ministry of Education and the government of Aragon, respectively. This work was supported by grant PO68/2000 (M.S.) from the government of Aragon and in part by PM99-0086 (M.S.) from the MCYT and UZ2002-BIO-01 (J.A.C.) from the University of Zaragoza. Parts of this work were presented in abstract form at the III Forum of European Neuroscience Societies (Paris, July 2002) and the X Congreso de la Sociedad Española de Neurociencia (Lérida, Spain, September 2003). The nucleotide sequences of the cDNAs for the proteins presented in the present work were submitted to GenBank and given accession numbers AF289218 (APP-695), AF289219 (APP-751), AY371190 (nicastrin), AY371191 (neprilysin), AY486554 (presenilin-2), AY486555 (BACE-1), AY486556 (BACE-2) and AY486557 (ADAM-17).

PY - 2005

Y1 - 2005

N2 - This study reveals that the chick embryo has active the machinery for the production and degradation of the amyloid beta peptide characteristic of Alzheimer's disease. We cloned the principal beta-amyloid precursor protein isoforms in the chick embryo and observed that they are highly homologous to the human sequences and identical at the C-terminal sequence, including the amyloid beta domain. Mammals such as rat or mouse, more commonly used as animal models of human diseases, have a distinct amyloid beta sequence. The distribution of beta-amyloid precursor protein isoforms in the chick embryo revealed that, as in humans, their expression is ubiquitous and the prototype beta-amyloid precursor protein-695 predominated in the nervous system. We also found that the chick embryo expresses the genes for the main proteolytic proteases implicated in the production of amyloid beta, including BACE-1, BACE-2, presenilin-1, presenilin-2 and nicastrin, as well as the amyloid beta-degrading enzyme neprilysin, or ADAM-17, a protease implicated in the non-amyloidogenic processing of beta-amyloid precursor protein. We have also found that between amyloid beta40 and amyloid beta42, this latter seems to be the major amyloid beta peptide produced during chick embryogenesis. The chick embryo appears as a suitable natural model to study cell biology and developmental function of beta-amyloid precursor protein and a potential assay system for drugs that regulate beta-amyloid precursor protein processing.

AB - This study reveals that the chick embryo has active the machinery for the production and degradation of the amyloid beta peptide characteristic of Alzheimer's disease. We cloned the principal beta-amyloid precursor protein isoforms in the chick embryo and observed that they are highly homologous to the human sequences and identical at the C-terminal sequence, including the amyloid beta domain. Mammals such as rat or mouse, more commonly used as animal models of human diseases, have a distinct amyloid beta sequence. The distribution of beta-amyloid precursor protein isoforms in the chick embryo revealed that, as in humans, their expression is ubiquitous and the prototype beta-amyloid precursor protein-695 predominated in the nervous system. We also found that the chick embryo expresses the genes for the main proteolytic proteases implicated in the production of amyloid beta, including BACE-1, BACE-2, presenilin-1, presenilin-2 and nicastrin, as well as the amyloid beta-degrading enzyme neprilysin, or ADAM-17, a protease implicated in the non-amyloidogenic processing of beta-amyloid precursor protein. We have also found that between amyloid beta40 and amyloid beta42, this latter seems to be the major amyloid beta peptide produced during chick embryogenesis. The chick embryo appears as a suitable natural model to study cell biology and developmental function of beta-amyloid precursor protein and a potential assay system for drugs that regulate beta-amyloid precursor protein processing.

KW - ADAM

KW - APP

KW - Alzheimer's disease

KW - Chick embryo

KW - Neprilysin

KW - Secretase

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The chick embryo appears as a natural model for research in beta-amyloid precursor protein processing

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