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IGFBP-5Insulin-like Growth Factor Binding Protein-5
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References in periodicals archive ?
Importantly, the PAPPA2 p.A1033V mutant was unable to cleave IGFBP-3 and IGFBP-5 confirming the loss-of-function effect of this mutation.
Duan, "IGFBP-5 regulates muscle cell differentiation by binding to IGF-II and switching on the IGF-II auto-regulation loop," The Journal of Cell Biology, vol.
Li et al., "IGF-I increases IGFBP-5 and collagen [alpha]1(I) mRNAs by the MAPK pathway in rat intestinal smooth muscle cells," American Journal of Physiology, vol.
Igfbp-5 was most frequently predicted by Opn; Lox was best predicted by lymphocyte antigen 6 complex, locus H; and Opn was most often predicted by brain-derived neurotrophic factor, interleukin 6, and proliferin.
The target genes chosen for study included Ahr, cytochrome P450 1B1 (Cyp1b1), insulin-like growth factor-binding protein-5 (Igfbp-5), lysyl oxidase (Lox), and osteopontin (Opn).
OGX-225 targets both insulin-like growth factor binding protein-5 (IGFBP-5) and insulin-like growth factor binding protein-2 (IGFBP-2), two molecules involved in the development of metastatic disease in hormone-regulated tumors such as prostate and breast cancers.
Recently, PAPP-A has been found to specifically cleave insulin-like growth factor-binding protein-4 (IGFBP-4) in an IGF-dependent manner (4,5) and IGFBP-5 in an IGF-independent manner (6).
IGFBP-5 mRNA is positively correlated with IGF-I in embryonic stage but is negatively correlated after hatching.
Intact insulin-like growth factor binding protein-5 (IGFBP-5) associates with bone matrix and the soluble fragments of IGFBP-5 accumulated in culture medium of neonatal mouse calvariae by parathyroid hormone and prostaglandin E2-treatment.
In this study, we used real-time quantitative PCR to assess IGF-I, IGF-II, IGF-IR, IGFBP-2, IGFBP-5, IGFBP-7, and IGFBP-3 mRNA expression in the breast muscle of slow-growing Langshan (LS) layer and rapidly-growing Arbor Acres (AA) broiler chickens.
Recently, it has been reported that IGFBP-5 can form ternary circulating complexes with ALS and IGF-I (9, 10).
However, the identities of the 31-kDa doublets IGFBPs, which apparently correspond to the 28-kDa doublets found in CCM of porcine embryonic myogenic cells (Pampusch et al., 2005), need to be confirmed, although the latter doublets were identified as IGFBP-5 and a mixture of IGFBPs-4 and -5, respectively, by immunoblotting by Pampusch et al.