Catabolism of neurotensin by neural (neuroblastoma clone N1E115) and extraneural (HT29) cell lines
Journal Article
·
· Peptides (Fayetteville, N.Y.); (United States)
The mechanisms by which neurotensin (NT) was inactivated by differentiated neuroblastoma and HT29 cells were characterized. In both cell lines, the sites of primary cleavages of NT were Pro7-Arg8, Arg8-Arg9 and Pro10-Tyr11 bonds. The cleavage at the Pro7-Arg8 bond was totally inhibited by N-benzyloxycarbonyl-Prolyl-Prolinal and therefore resulted from the action of proline endopeptidase. This peptidase also contributed in a major way to the cleavage at the Pro10-Tyr11 bond. However the latter breakdown was partly due to an NT-degrading neutral metallopeptidase. Finally, we demonstrated the involvement of a recently purified rat brain soluble metalloendopeptidase at the Arg8-Arg9 site by the use of its specific inhibitor N-(1(R,S)-carboxy-2-Phenylethyl)-alanylalanylphenylalanine-p-amino benzoate. The secondary processing of NT degradation products revealed differences between HT29 and N1E115 cells. Angiotensin converting enzyme was shown to degrade NT1-10 and NT1-7 in N1E115 cells but was not detected in HT29 cells. A post-proline dipeptidyl aminopeptidase activity converted NT9-13 into NT11-13 in HT29 cells but not in N1E115 cells. Finally, bestatin-sensitive aminopeptidases rapidly broke down NT11-13 to Tyr in both cell lines. Models for the inactivation of NT in HT29 and N1E115 cells are proposed and compared to that previously described for purified rat brain synaptic membranes.
- Research Organization:
- Universite de Nice, France
- OSTI ID:
- 6525797
- Journal Information:
- Peptides (Fayetteville, N.Y.); (United States), Journal Name: Peptides (Fayetteville, N.Y.); (United States) Vol. 6; ISSN PPTDD
- Country of Publication:
- United States
- Language:
- English
Similar Records
Neurotensin analogs (D-TYR11) and (D-PHE11)neurotensin resist degradation by brain peptidases in vitro and in vivo
Neurotensin-induced Erk1/2 phosphorylation and growth of human colonic cancer cells are independent from growth factors receptors activation
High affinity binding of (/sup 3/H)neurotensin of rat uterus
Journal Article
·
Wed Nov 30 23:00:00 EST 1983
· J. Pharmacol. Exp. Ther.; (United States)
·
OSTI ID:6541708
Neurotensin-induced Erk1/2 phosphorylation and growth of human colonic cancer cells are independent from growth factors receptors activation
Journal Article
·
Fri Oct 14 00:00:00 EDT 2011
· Biochemical and Biophysical Research Communications
·
OSTI ID:22207520
High affinity binding of (/sup 3/H)neurotensin of rat uterus
Journal Article
·
Sat Oct 31 23:00:00 EST 1987
· Peptides (Fayetteville, N.Y.); (United States)
·
OSTI ID:5209876
Related Subjects
550501* -- Metabolism-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ANIMAL CELLS
ANIMALS
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL MODELS
CATABOLISM
CELL CULTURES
CLEAVAGE
CLONE CELLS
CRYSTAL STRUCTURE
ENZYME ACTIVITY
ENZYME INHIBITORS
ENZYMES
HYDROLASES
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
MAMMALS
METABOLISM
MICE
MICROSTRUCTURE
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PEPTIDES
PROTEINS
REACTION KINETICS
RODENTS
TRACER TECHNIQUES
TRITIUM COMPOUNDS
TUMOR CELLS
VERTEBRATES
59 BASIC BIOLOGICAL SCIENCES
ANIMAL CELLS
ANIMALS
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL MODELS
CATABOLISM
CELL CULTURES
CLEAVAGE
CLONE CELLS
CRYSTAL STRUCTURE
ENZYME ACTIVITY
ENZYME INHIBITORS
ENZYMES
HYDROLASES
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
MAMMALS
METABOLISM
MICE
MICROSTRUCTURE
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PEPTIDES
PROTEINS
REACTION KINETICS
RODENTS
TRACER TECHNIQUES
TRITIUM COMPOUNDS
TUMOR CELLS
VERTEBRATES