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Title: | Recombinant C-terminal fragments of the gastrin-releasing peptide precursor are bioactive. | Austin Authors: | Patel, Oneel;Dumesny, Chelsea;Shulkes, Arthur;Baldwin, Graham S | Affiliation: | University of Melbourne, Department of Surgery, Austin Health, Heidelberg, Melbourne, Victoria, Australia | Issue Date: | 29-Mar-2007 | Publication information: | 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. | Gov't Doc #: | 17395367 | URI: | http://ahro.austin.org.au/austinjspui/handle/1/10345 | DOI: | 10.1016/j.canlet.2007.02.014 | Journal: | Cancer letters | URL: | https://pubmed.ncbi.nlm.nih.gov/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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