PMID- 1707628
OWN - NLM
STAT- MEDLINE
DCOM- 19910523
LR  - 20191021
IS  - 0952-5041 (Print)
IS  - 0952-5041 (Linking)
VI  - 6
IP  - 1
DP  - 1991 Feb
TI  - Modulation of inositol lipid hydrolysis in human breast cancer cells by two 
      classes of bombesin antagonist.
PG  - 71-8
AB  - Inositol lipid hydrolysis was monitored in the human breast cancer cell line 
      MCF-7 in response to various bombesin (BN) and substance P (SP) analogues. Both 
      members of the BN family of peptides, i.e. BN and gastrin-releasing peptide 
      (GRP), stimulated a dose-related increase in total inositol phosphate production, 
      with a similar half-maximal effective dose (ED50) around 1 nM. The BN receptor 
      antagonist [Leu13-psi-CH2NH-Leu14]-BN (LLBN) at 1 microM was devoid of agonist 
      activity and displaced the BN dose-response to the right, resulting in a tenfold 
      increase in the ED50 for BN. BN also stimulated a dose-related increase in 45Ca2+ 
      efflux which was also inhibited by LLBN. Two SP analogues 
      [DArg1,D-Pro2,D-Trp7,9,Leu11]-SP and [D-Arg1,D-Phe5,D-Trp7,9,Leu11]-SP 
      ([APheTL]-SP), both antagonized BN-stimulated inositol lipid hydrolysis. 
      [APheTL]-SP (60 and 80 microM) alone also exhibited considerable agonist activity 
      which was not antagonized by LLBN. Indeed, a sub-threshold dose of [APheTL]-SP 
      (40 microM) in the presence of LLBN (10 microM) potentiated the inositol lipid 
      hydrolysis response. BN, GRP, LLBN and [APheTL]-SP all inhibited binding of 
      125I-labelled GRP to MCF-7 cells, to 50% of that occurring in the absence of the 
      peptides, at concentrations of 150 pM, 150 pM, 150 nM and 600 nM respectively. 
      These data are consistent with the presence of separate but interacting receptors 
      or binding sites for BN and SP analogues, which are coupled to a common signal 
      transduction pathway in human breast cancer cells.
FAU - Patel, K V
AU  - Patel KV
AD  - Department of Chemical Pathology, St Mary's Hospital Medical School, Imperial 
      College of Science, Technology and Medicine, London.
FAU - Schrey, M P
AU  - Schrey MP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Mol Endocrinol
JT  - Journal of molecular endocrinology
JID - 8902617
RN  - 0 (Inositol Phosphates)
RN  - 0 (Peptides)
RN  - 0 (Receptors, Bombesin)
RN  - 0 (Receptors, Neurotransmitter)
RN  - 33507-63-0 (Substance P)
RN  - 80043-53-4 (Gastrin-Releasing Peptide)
RN  - PX9AZU7QPK (Bombesin)
SB  - IM
MH  - Binding Sites
MH  - Bombesin/*antagonists & inhibitors/metabolism/pharmacology
MH  - Breast Neoplasms/metabolism
MH  - Female
MH  - Gastrin-Releasing Peptide
MH  - Humans
MH  - Hydrolysis
MH  - Inositol Phosphates/*metabolism
MH  - Peptides/metabolism
MH  - Receptors, Bombesin
MH  - Receptors, Neurotransmitter/drug effects/metabolism
MH  - Signal Transduction/drug effects
MH  - Substance P/analogs & derivatives/metabolism/pharmacology
MH  - Tumor Cells, Cultured/drug effects/*metabolism
EDAT- 1991/02/01 00:00
MHDA- 1991/02/01 00:01
CRDT- 1991/02/01 00:00
PHST- 1991/02/01 00:00 [pubmed]
PHST- 1991/02/01 00:01 [medline]
PHST- 1991/02/01 00:00 [entrez]
AID - 10.1677/jme.0.0060071 [doi]
PST - ppublish
SO  - J Mol Endocrinol. 1991 Feb;6(1):71-8. doi: 10.1677/jme.0.0060071.