Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/10345
Title: Recombinant C-terminal fragments of the gastrin-releasing peptide precursor are bioactive.
Authors: Patel, Oneel;Dumesny, Chelsea;Shulkes, Arthur;Baldwin, Graham S
Affiliation: University of Melbourne, Department of Surgery, Austin Health, Heidelberg, Melbourne, VIC, Australia
Issue Date: 29-Mar-2007
Citation: Cancer Letters 2007; 254(1): 87-93
Abstract: C-terminal fragments from the precursor for gastrin-releasing peptide (GRP) have been detected in several human tumour types. We have previously demonstrated that recombinant human proGRP42-98 is biologically active. To investigate the regions responsible, proGRP42-98 was cleaved with thrombin, and the fragments purified by HPLC. Both proGRP42-79 and proGRP80-98 stimulated proliferation of the human colorectal carcinoma cell line DLD-1, but neither peptide bound to the GRP receptor or bombesin receptor subtype 3. We conclude that two distinct regions of the proGRP C-terminus are biologically active, via a receptor distinct from the known GRP receptors. This discovery opens the way for the development of selective antagonists that may offer new therapies for proGRP-producing tumours.
Internal ID Number: 17395367
URI: http://ahro.austin.org.au/austinjspui/handle/1/10345
DOI: 10.1016/j.canlet.2007.02.014
URL: http://www.ncbi.nlm.nih.gov/pubmed/17395367
Type: Journal Article
Subjects: Animals
BALB 3T3 Cells
Cell Line, Tumor
Cell Proliferation.drug effects
Chromatography, High Pressure Liquid
Humans
Mice
Peptide Fragments.genetics.metabolism.pharmacology
Peptides.chemistry.metabolism
Protein Binding
Protein Precursors.chemistry.metabolism
Radioligand Assay
Receptors, Bombesin.genetics.metabolism
Recombinant Proteins.isolation & purification.metabolism.pharmacology
Transfection
Appears in Collections:Journal articles

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