Amyloid β protein does not interact with tachykinin receptors coupled to inositol phospholipid hydrolysis in human astrocytoma cells

M. Di Stefano; G. Aleppo; G. Casabona; A. A. Genazzani; U. Scapagnini; F. Nicoletti

doi:10.1016/0006-8993(93)90416-K

Amyloid β protein does not interact with tachykinin receptors coupled to inositol phospholipid hydrolysis in human astrocytoma cells

M. Di Stefano, G. Aleppo, G. Casabona, A. A. Genazzani, U. Scapagnini, F. Nicoletti

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

Abstract

We have tested the interaction between amyloid β protein (AβP) and tachykinin receptors in cultured UC-11MG astrocytoma cells, which express high affinity substance P receptors and respond to substance P with an unusually large stimulation of polyphosphoinositide hydrolysis. Both the full-length AβP (AβP_1-40) and the fragment 25-35 (AβP_25-35) did not affect the stimulation of [³H]inositolmonophosphate (InsP) formation by substance P. AβP_25-35 was also inactive when applied to the cultures 18 or 72 h prior to the assay. In addition, AβP_25-35 did not displace specifically bound [³H]SarMet substance P from its recognition sites in intact UC-11MG cells. These results suggest that, at least in this specific cell type, amyloid peptides do not interact with substance P receptors.

Lingua originale	Inglese
pagine (da-a)	166-168
Numero di pagine	3
Rivista	Brain Research
Volume	600
Numero di pubblicazione	1
DOI	https://doi.org/10.1016/0006-8993(93)90416-K
Stato di pubblicazione	Pubblicato - 8 gen 1993
Pubblicato esternamente	Sì

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10.1016/0006-8993(93)90416-K

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title = "Amyloid β protein does not interact with tachykinin receptors coupled to inositol phospholipid hydrolysis in human astrocytoma cells",

abstract = "We have tested the interaction between amyloid β protein (AβP) and tachykinin receptors in cultured UC-11MG astrocytoma cells, which express high affinity substance P receptors and respond to substance P with an unusually large stimulation of polyphosphoinositide hydrolysis. Both the full-length AβP (AβP1-40) and the fragment 25-35 (AβP25-35) did not affect the stimulation of [3H]inositolmonophosphate (InsP) formation by substance P. AβP25-35 was also inactive when applied to the cultures 18 or 72 h prior to the assay. In addition, AβP25-35 did not displace specifically bound [3H]SarMet substance P from its recognition sites in intact UC-11MG cells. These results suggest that, at least in this specific cell type, amyloid peptides do not interact with substance P receptors.",

keywords = "Amyloid β protein, Phosphoinositide hydrolysis, Substance P, UC-11MG astrocytoma cell",

author = "\{Di Stefano\}, M. and G. Aleppo and G. Casabona and Genazzani, \{A. A.\} and U. Scapagnini and F. Nicoletti",

year = "1993",

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T1 - Amyloid β protein does not interact with tachykinin receptors coupled to inositol phospholipid hydrolysis in human astrocytoma cells

AU - Di Stefano, M.

AU - Aleppo, G.

AU - Casabona, G.

AU - Genazzani, A. A.

AU - Scapagnini, U.

AU - Nicoletti, F.

PY - 1993/1/8

Y1 - 1993/1/8

N2 - We have tested the interaction between amyloid β protein (AβP) and tachykinin receptors in cultured UC-11MG astrocytoma cells, which express high affinity substance P receptors and respond to substance P with an unusually large stimulation of polyphosphoinositide hydrolysis. Both the full-length AβP (AβP1-40) and the fragment 25-35 (AβP25-35) did not affect the stimulation of [3H]inositolmonophosphate (InsP) formation by substance P. AβP25-35 was also inactive when applied to the cultures 18 or 72 h prior to the assay. In addition, AβP25-35 did not displace specifically bound [3H]SarMet substance P from its recognition sites in intact UC-11MG cells. These results suggest that, at least in this specific cell type, amyloid peptides do not interact with substance P receptors.

AB - We have tested the interaction between amyloid β protein (AβP) and tachykinin receptors in cultured UC-11MG astrocytoma cells, which express high affinity substance P receptors and respond to substance P with an unusually large stimulation of polyphosphoinositide hydrolysis. Both the full-length AβP (AβP1-40) and the fragment 25-35 (AβP25-35) did not affect the stimulation of [3H]inositolmonophosphate (InsP) formation by substance P. AβP25-35 was also inactive when applied to the cultures 18 or 72 h prior to the assay. In addition, AβP25-35 did not displace specifically bound [3H]SarMet substance P from its recognition sites in intact UC-11MG cells. These results suggest that, at least in this specific cell type, amyloid peptides do not interact with substance P receptors.

KW - Amyloid β protein

KW - Phosphoinositide hydrolysis

KW - Substance P

KW - UC-11MG astrocytoma cell

UR - https://www.scopus.com/pages/publications/0027472468

U2 - 10.1016/0006-8993(93)90416-K

DO - 10.1016/0006-8993(93)90416-K

M3 - Article

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VL - 600

SP - 166

EP - 168

JO - Brain Research

JF - Brain Research

IS - 1

ER -

Amyloid β protein does not interact with tachykinin receptors coupled to inositol phospholipid hydrolysis in human astrocytoma cells

Abstract

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