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^*

^*Corresponding author for this work

Medicine, Endocrinology Division

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

13 Scopus citations

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.

Original language	English (US)
Pages (from-to)	166-168
Number of pages	3
Journal	Brain research
Volume	600
Issue number	1
DOIs	https://doi.org/10.1016/0006-8993(93)90416-K
State	Published - Jan 8 1993

Keywords

Amyloid β protein
Phosphoinositide hydrolysis
Substance P
UC-11MG astrocytoma cell

ASJC Scopus subject areas

General Neuroscience
Molecular Biology
Clinical Neurology
Developmental Biology

Access to Document

10.1016/0006-8993(93)90416-K

Cite this

@article{963a15a9093a44d2983548fcd149d5d0,

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",

month = jan,

day = "8",

doi = "10.1016/0006-8993(93)90416-K",

language = "English (US)",

volume = "600",

pages = "166--168",

journal = "Brain research",

issn = "0006-8993",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

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 - http://www.scopus.com/inward/record.url?scp=0027472468&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027472468&partnerID=8YFLogxK

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

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

M3 - Article

C2 - 7678535

AN - SCOPUS:0027472468

SN - 0006-8993

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

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this