Sample Essay on Insulin-Like Growth Factor-Binding Protein

Sample Essay on Insulin-Like Growth Factor-Binding Protein

The role of insulin in regulating metabolism in the body has been subjected to intense studies and research for many years. It dates back as 1869, when Paul Langerhans, a German pathological anatomist recognized the Islet of Langerhans. The many effects of diabetes and the connection between different types of diabetes and insulin have made study in this field valid. Insulin-like growth factors [IGFs] are also significant in the human body as they are the main mediators of the growth hormone [GH]. The IGF family is made up of three peptide hormones or growth factors and they are insulin, IGF-I and IGF-II.

Insulin-like growth factor-binding protein [IGFBP] is imperative when it comes to IGFs. The IGFBP serves as a carrier protein for insulin-like growth factor-I [IGF-1]. This is a group of vertebrate secreted proteins, which bind to IGF-I AND IGF-II with high affinity and moderate the biological activities of the IGFs. Insulin-like growth factor-binding protein [IGFBP] is made up of six unique subgroups IGFBP-I all through to 6 based on the conservation of the gene [intro-exon] organization, structural similarity and binding affinity of IGFs.

Across the six subgroups of IGFBP, IGFBP-5 displays the most sequence conservation while the IGFBP-6 shows the least sequence conservation. Insulin-like growth factor-binding protein contains the inhibitor domain homologues which are related and link well to MEROPS protease inhibitor family 131 [equistatin, clan IX]. All IGFBPs share a common architecture. However, there are certain protein domains that are conserved across vertebrate species and the mid-region is highly adaptable with respect to the protease cleavage sites and phosphorylation and glycosylation sites.

On the N-terminal and the C-terminals regions, the IIGFBPs contain 16-18 conserved cysteines, and they form 8 to 9 disulphide bonds. Insulin-like growth factor-binding proteins are unusually pleiotropic molecules and like any other proteins; they can prolong the half-life of insulin growth factors. This is possible through high affinity binding of the ligands. Besides functioning as carrier proteins, serum IGFBPs also aid modulate the endocrine and paracrine/ autocrine activities of the insulin-like growth building factors.

This is possible because the IGFBPs modulate IGF close by to bind to signaling IGF-I receptors. This is not all; IGFBPs can also work exceptionally well as growth modulators independent of IGFs. For instance, IGFBP-5 stimulates markers of bone formation in osteoblasts lacking functional IGFs. The binding of insulin-like growth factor-binding protein to its putative receptor on the cell membrane may stimulate the signaling pathway independent of an IGF receptor, to easily regulate the effects of IGFBPS in specific target cell types.

The IGFBP-1 place are great role in stimulate cell migration of CHO and human trophoblast cells via an activity mediated by alpha 5 beta 1 integrin. Insulin-like growth factor-binding proteins that are transported into the cell nucleus through a nuclear localization signal may also exert IGF-independent effects by the transcriptional activation of genes. The IGF-binding proteins prolong the half-life of IGFs and make it easy and smooth for them to perform their activities. They have great influence on cell culture and help living organism grow and develop without any complications.

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