Recombinant expression of IGF-1 and LR3 IGF-1 fused with xylanase in Pichia pastoris.
The study successfully produced high levels of IGF-1 and LR3 IGF-1 in Pichia pastoris, achieving 0.5 g/L and 1 g/L respectively, but does not provide detailed clinical implications.
Where it sits
this study against the rest of the igf-1 lr3 (long r3 igf-1) corpusSummary and findings
This study reports the recombinant expression of human IGF-1 and its analog Long R3 IGF-1 (LR3 IGF-1) in the Pichia pastoris expression system. The expression levels reached approximately 0.5 g/L for XynCDBFV-IGF-1 and 1 g/L for XynCDBFV-LR3 IGF-1. The purified proteins displayed bioactivity in cell proliferation assays compared to standard IGF-1.
Abstract
Insulin-like growth factor-1 (IGF-1) is a pleiotropic protein hormone and has become an attractive therapeutic target because of its multiple roles in various physiological processes, including growth, development, and metabolism. However, its production is hindered by low heterogenous protein expression levels in various expression systems and hard to meet the needs of clinical and scientific research. Here, we report that human IGF-1 and its analog Long R3 IGF-1 (LR3 IGF-1) are recombinant expressed and produced in the Pichia pastoris (P. pastoris) expression system through being fused with highly expressed xylanase XynCDBFV. Furthermore, purified IGF-1 and LR3 IGF-1 display excellent bioactivity of cell proliferation compared to the standard IGF-1. Moreover, higher heterologous expression levels of the fusion proteins XynCDBFV-IGF-1 and XynCDBFV-LR3 IGF-1 are achieved by fermentation in a 15-L bioreactor, reaching up to about 0.5 g/L XynCDBFV-IGF-1 and 1 g/L XynCDBFV-TEV-LR3 IGF-1. Taken together, high recombinant expression of bioactive IGF-1 and LR3 IGF-1 is acquired with the assistance of xylanase as a fusion partner in P. pastoris, which could be used for both clinical and scientific applications. KEY POINTS: • Human IGF-1 and LR3 IGF-1 are produced in the P. pastoris expression system. • Purified IGF-1 and LR3 IGF-1 show bioactivity comparable to the standard IGF-1. • High heterologous expression of IGF-1 and LR3 IGF-1 is achieved by fermentation in a bioreactor.
Background
The paper addresses the production of IGF-1 and its analog LR3 IGF-1, which are important for various biological functions. Prior knowledge indicates that IGF-1 plays a role in growth and development, but efficient production methods are necessary for research and potential applications. This study is significant as it explores a novel expression system using Pichia pastoris.
Methods
Not reported in abstract.
Results
Not reported in abstract.
Interpretation
Not reported in abstract.
Key findings
- Not reported in abstract.
Limitations
- Not reported in abstract.