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March 17, 2006Journal of Biological ChemistryOpen Access

Mutations changing acidic residues to neutral or polar to basic in the N-domain of IGFBP-5 significantly reduced transactivation activity, with combinatory mutants showing essentially no activity.

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Population

Mouse embryonic skeletal cells and cultured cells

Comparison

Deletion mutants and point mutations of the… vs Wild-type IGFBP-5 and other IGFBPs

Design

Preclinical

Authors

YZYang ZhaoPYPing YinLBLeon A. Bach

Discussion

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Overview

These N-domain residues warrant further study in cardiovascular animal models; leaves open clinical translation to human IGFBP-5 therapies.

Structured PICO

P
Population
Mouse embryonic skeletal cells and cultured cells
I
Intervention
Deletion mutants and point mutations of the N-domain of IGFBP-5 (e.g., E8A, D11S, E12A, E30S/P31A, E43L, E52A, Q56R)
C
Comparator
Wild-type IGFBP-5 and other IGFBPs (IGFBP-1, -2, -3, -4, -6)
O
Outcome
Transactivation activitysurrogate

Several conserved acidic amino acids in the N-terminal region of IGFBP-5 are critical for its transactivation activity.

Cite This Study

Zhao et al. (2006) studied this question.

synapsesocial.com/papers/6a896145a7eee2293bcafb6fhttps://doi.org/10.1074/jbc.m506941200
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