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Gene Review:

IGFBP5 - insulin-like growth factor binding protein 5

Sus scrofa

Pampusch, M.S. et al., Duan, C. et al., Yano, K. et al., Duan, C. et al., Kluge, A. et al., et al.

Duan, Liimatta, Bottum, Duan, Clemmons,

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Psychiatry related information on IGFBP5

The data provided here demonstrated that IGFBP-5 has the potential to affect proliferation of PEMCs during critical periods of in vitro muscle cell development and therefore may impact the capacity for ultimate postnatal muscle mass development in vivo [1].

High impact information on IGFBP5

Mutation of the heparin-binding motif of IGFBP-5 reduced its migration promoting activity [2].
IGFBP-5 not only modulates IGF-I actions, but it also stimulates cell migration by interacting with cell-surface heparan sulfate proteoglycans [2].
The addition of rapamycin, which inhibits IGF-I-induced p70(s6k) activation, significantly inhibited IGF-I-regulated IGFBP-5 gene expression [3].
Expression of the insulin-like growth factor-binding protein 5 (IGFBP-5) gene in vascular smooth muscle cells is up-regulated by IGF-I through an IGF-I receptor-mediated mechanism [3].
In this study, we studied the possible involvement of the mitogen-activated protein kinase (MAPK) and PI 3-kinase signaling pathways in mediating IGF-I-regulated IGFBP-5 gene expression [3].

Biological context of IGFBP5

Furthermore, the IGFBP-5 promoter was 3.5-fold more active in directing expression of the luciferase reporter gene in IGF-I-treated aortic SMCs as compared to control cells, whereas the luciferase activity remained the same in control- and IGF-I-treated fibroblasts [4].
Nuclear run-on assays revealed that IGF-I increased transcription rate of the IGFBP-5 gene, while IGF-I did not change the IGFBP-5 mRNA stability [4].
In contrast, the IGFBP-5 expression induced by forskolin was unaffected by PKC down-regulation or inhibition, suggesting that PKC activation is required for the IGF-regulated but not the cAMP-regulated events [5].
The production of rpIGFBP-5 and a neutralizing antibody to porcine IGFBP-5 provides a powerful tool to investigate the role of IGFBP-5 in porcine myogenic cell proliferation and differentiation [1].
IGFBP-5 may play some role in myogenesis and/or in changes in myogenic cell proliferation that accompany differentiation [1].

Anatomical context of IGFBP5

IGFBP-5 mRNA was concentrated in the surface or germinal epithelium and in capillary endothelium, particularly in capillaries of corpora lutea [6].
CONCLUSION: These results indicate a coordinate gene expression of the IGF system in microembolised porcine myocardium, compatible with a role of IGF-I, IGFBP-3, IGFBP-5, and IGFBP-6 in inflammation-linked angiogenesis and/or repair processes [7].
IGFBP-5 reportedly may either suppress or stimulate proliferation or differentiation of cultured cells depending on cell type and culture conditions [1].
IGFBP-3 and IGFBP-4 transcript levels became elevated in endometrium after implantation; whereas, IGFBP-5 and IGFBP-6 mRNAs were in greater abundance in periimplantation than post-implantation endometrium [8].

Associations of IGFBP5 with chemical compounds

When LY294002 and wortmannin, two specific inhibitors of PI 3-kinase, were added with Des(1-3)IGF-I, the IGF-I-regulated IGFBP-5 expression was negated [3].
These data taken together with the protease inhibitor results suggest that the IGFBP-2, IGFBP-4, and IGFBP-5 proteases are members of a similar family of calcium-dependent serine proteases, but they are distinct proteases [9].

Other interactions of IGFBP5

No treatment effect was found for muscle IGF-I (P = 0.36), IGF-II (P = 0.51), IGFBP-3 (P = 0.70), or IGFBP-5 (P = 0.51) mRNA abundance [10].
Previously, we have reported that porcine VSMCs synthesize and secrete IGF-I and several forms of IGFBPs, including IGFBP-2, IGFBP-4, and IGFBP-5 [11].
Down-regulation or inhibition of PKC activity abolished the IGF-I-induced DNA synthesis, migration and IGFBP-5 gene expression [5].

Analytical, diagnostic and therapeutic context of IGFBP5

Whereas IGF-II expression was already increased by experimental stress, IGFBP-5 mRNA was enhanced only by ischaemia/reperfusion [12].
Northern blots showed readily detectable transcripts for IGF-I (6.7 and 0.9 kb), IGFBP-2 (1.8 kb), IGFBP-3 (2.8 kb), IGFBP-4 (2.6 kb), and IGFBP-5 (6.0 kb), but not for IGFBP-6 [13].
This antibody is capable of neutralizing the effects of both rpIGFBP-5 and endogenously produced porcine IGFBP-5 on PEMCs as well as detecting IGFBP-5 in Western blots [1].
Immunoprecipitation with specific antibodies and 125I-IGF-I ligand blot analysis showed that myogenic cultures secreted IGFBP-3 (doublet band, 43 kDa and 39 kDa), IGFBP-2 (34 kDa), IGFBP-4 (30 and 24 kDa), and IGFBP-5 (30 and 28 kDa) [14].

References

Production of recombinant porcine IGF-binding protein-5 and its effect on proliferation of porcine embryonic myoblast cultures in the presence and absence of IGF-I and Long-R3-IGF-I. Pampusch, M.S., Xi, G., Kamanga-Sollo, E., Loseth, K.J., Hathaway, M.R., Dayton, W.R., White, M.E. J. Endocrinol. (2005) [Pubmed]
Regulation of vascular smooth muscle cell responses to insulin-like growth factor (IGF)-I by local IGF-binding proteins. Hsieh, T., Gordon, R.E., Clemmons, D.R., Busby, W.H., Duan, C. J. Biol. Chem. (2003) [Pubmed]
Insulin-like growth factor (IGF)-I regulates IGF-binding protein-5 gene expression through the phosphatidylinositol 3-kinase, protein kinase B/Akt, and p70 S6 kinase signaling pathway. Duan, C., Liimatta, M.B., Bottum, O.L. J. Biol. Chem. (1999) [Pubmed]
Insulin-like growth factor-I (IGF-I) regulates IGF-binding protein-5 synthesis through transcriptional activation of the gene in aortic smooth muscle cells. Duan, C., Hawes, S.B., Prevette, T., Clemmons, D.R. J. Biol. Chem. (1996) [Pubmed]
Down-regulation of protein kinase C inhibits insulin-like growth factor I-induced vascular smooth muscle cell proliferation, migration, and gene expression. Yano, K., Bauchat, J.R., Liimatta, M.B., Clemmons, D.R., Duan, C. Endocrinology (1999) [Pubmed]
Selective expression of insulin-like growth factor system components during porcine ovary follicular selection. Zhou, J., Adesanya, O.O., Vatzias, G., Hammond, J.M., Bondy, C.A. Endocrinology (1996) [Pubmed]
Coordinate expression of the insulin-like growth factor system after microembolisation in porcine heart. Kluge, A., Zimmermann, R., Weihrauch, D., Mohri, M., Sack, S., Schaper, J., Schaper, W. Cardiovasc. Res. (1997) [Pubmed]
The unique endometrial expression and genomic organization of the porcine IGFBP-2 gene. Song, S., Lee, C.Y., Green, M.L., Chung, C.S., Simmen, R.C., Simmen, F.A. Mol. Cell. Endocrinol. (1996) [Pubmed]
Properties of an insulin-like growth factor-binding protein-4 protease that is secreted by smooth muscle cells. Parker, A., Gockerman, A., Busby, W.H., Clemmons, D.R. Endocrinology (1995) [Pubmed]
Effects of L-carnitine on fetal growth and the IGF system in pigs. Waylan, A.T., Kayser, J.P., Gnad, D.P., Higgins, J.J., Starkey, J.D., Sissom, E.K., Woodworth, J.C., Johnson, B.J. J. Anim. Sci. (2005) [Pubmed]
Differential expression and biological effects of insulin-like growth factor-binding protein-4 and -5 in vascular smooth muscle cells. Duan, C., Clemmons, D.R. J. Biol. Chem. (1998) [Pubmed]
Insulin-like growth factor II is an experimental stress inducible gene in a porcine model of brief coronary occlusions. Kluge, A., Zimmermann, R., Münkel, B., Verdouw, P.D., Schaper, J., Schaper, W. Cardiovasc. Res. (1995) [Pubmed]
Expression of the messenger ribonucleic acids for insulin-like growth factor-I and insulin-like growth factor binding proteins in porcine corpora lutea. Gadsby, J.E., Lovdal, J.A., Samaras, S., Barber, J.S., Hammond, J.M. Biol. Reprod. (1996) [Pubmed]
Cultured porcine myogenic cells produce insulin-like growth factor binding protein-3 (IGFBP-3) and transforming growth factor beta-1 stimulates IGFBP-3 production. Hembree, J.R., Pampusch, M.S., Yang, F., Causey, J.L., Hathaway, M.R., Dayton, W.R. J. Anim. Sci. (1996) [Pubmed]

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