About: Downregulation of Signaling-active IGF-1 by Dipeptidyl Peptidase IV (DPP-IV)

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About: Downregulation of Signaling-active IGF-1 by Dipeptidyl Peptidase IV (DPP-IV) Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Downregulation of Signaling-active IGF-1 by Dipeptidyl Peptidase IV (DPP-IV)
Creator	Chen, Xin Chien, Chia-Hui Han, Yu-San Chiu, Jeng-Jian Huang, Shiu-Feng Lin, Ching-Ting Liu, Hui-Ping Shyy, John Tang, Hsiang-Yun
source	PMC
abstract	Functioning as an extracellular protease, dipeptidyl peptidase IV (DPP-IV) preferentially cleaves the peptide bond after the penultimate proline residue. We report here that DPP-IV cleaves the first two amino acids from insulin-like growth factor 1 (IGF-1), revealed by mass spectrometry. The kinetic parameters of the proteolytic cleavage indicate that this reaction is physiologically relevant. Interestingly, truncated IGF-1 is less potent than the full-length protein in activating the IGF-1R, but binds more readily to IGF-binding protein 3 (IGFBP3). Quantitative RT–PCR showed that the level of DPP-IV mRNA is dramatically lower in lung squamous cell carcinoma tissues than in adjacent nonneoplastic lung tissues. However, this reduction was not observed in lung adenocarcinoma tissues. Our study suggests a possible link between IGF-1 and DPP-IV in cancer development in a specific tumor niche. A DPP-IV-related pathway may be important in mitigating IGF-1 signaling. Consequently, a robust IGF signaling pathway may accelerate early carcinogenesis in environments lacking DPP-IV.
has issue date	2010-12-01(xsd:dateTime)
bibo:pmid	23675206
has license	cc-by
sha1sum (hex)	15640dc97f36ae7b410f731003235ee8a3cae495
resource representing a document's title	Downregulation of Signaling-active IGF-1 by Dipeptidyl Peptidase IV (DPP-IV)
has PubMed Central identifier	PMC3615292
has PubMed identifier	23675206
schema:publication	Int J Biomed Sci
resource representing a document's body	covid:15640dc97f36ae7b410f731003235ee8a3cae495#body_text
is schema:about of	named entity 'cleaves' named entity 'binds' named entity 'tumor' named entity 'DOWNREGULATION' named entity 'INSULIN-LIKE GROWTH FACTOR 1' named entity 'MASS SPECTROMETRY' named entity 'NICHE' named entity 'PROTEIN ' named entity 'FUNCTIONING' named entity 'TUMOR' named entity 'NOT OBSERVED' named entity 'PROLINE RESIDUE' named entity 'DIPEPTIDYL PEPTIDASE IV' named entity 'REVEALED' named entity 'PENULTIMATE' named entity 'DPP' named entity 'LUNG ADENOCARCINOMA' named entity 'DEVELOPMENT' named entity 'CANCER' named entity 'POSSIBLE' named entity 'SIGNALING' named entity 'PROTEOLYTIC' named entity 'REPORT' named entity 'IGF-1' named entity 'ADJACENT' named entity 'RELEVANT' named entity 'TISSUES' named entity 'RELATED' named entity 'ACTIVATING' named entity 'PARAMETERS' named entity 'HERE' named entity 'REDUCTION' named entity 'LINK' named entity 'DIPEPTIDYL PEPTIDASE IV' named entity 'IGF-1' named entity 'IGF SIGNALING PATHWAY' named entity 'REACTION' named entity 'STUDY' named entity 'PROTEASE' named entity 'CLEAVAGE' named entity 'ROBUST' named entity 'ACCELERATE' named entity 'LUNG SQUAMOUS CELL CARCINOMA' named entity 'SCI' named entity 'SIGNALING' named entity 'ACTIVE' named entity 'ENVIRONMENTS' named entity 'BUT' named entity 'PATHWAY' named entity 'LEVEL' named entity 'TRUNCATED' named entity 'MRNA' named entity 'LENGTH' named entity 'LUNG TISSUES' named entity 'LOWER' named entity 'QUANTITATIVE RT-PCR' named entity 'EXTRACELLULAR' named entity 'OUR' named entity 'BIOMED' named entity 'LACKING' named entity 'IGF-1R' named entity 'BINDS' named entity 'IMPORTANT' named entity 'SPECIFIC' named entity 'AMINO ACIDS' named entity 'KINETIC' named entity 'CARCINOGENESIS' named entity 'IGF-BINDING PROTEIN 3' named entity 'EARLY' named entity 'PEPTIDE BOND' named entity 'CLEAVES' covid:arg/15640dc97f36ae7b410f731003235ee8a3cae495 named entity 'protein' named entity 'signaling' named entity 'physiologically'

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