Alpha-Hemoglobin-Stabilizing Protein: An Erythroid Molecular Chaperone

Fávero, Maria Emília; Costa, Fernando Ferreira

doi:10.1155/2011/373859

Cited by 25 publications

(22 citation statements)

References 47 publications

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“…Prior studies indicate two potential functions for AHSP during normal and pathologic erythropoiesis (8,26,63). First, AHSP acts as a molecular chaperone to bind and stabilize nascent ␣-globin folding intermediates prior to reaction with ␤-globin and assembly into HbA (Fig.…”

Section: Discussionmentioning

confidence: 99%

Insights into Hemoglobin Assembly through in Vivo Mutagenesis of α-Hemoglobin Stabilizing Protein

Khandros

Mollan

et al. 2012

Journal of Biological Chemistry

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Background:The ␣-hemoglobin-stabilizing protein (AHSP) facilitates hemoglobin assembly. Results: AHSP mutations that enhance binding affinity for ␣-globin or slow its rate of autooxidation in vitro do not affect normal or stressed erythropoiesis in mice. Conclusion: AHSP exhibits robust molecular chaperone activity in vivo even when its biochemical interactions with reduced ␣-globin are perturbed. Significance: Our findings support new models for AHSP activities in vivo.

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Section: Discussionmentioning

confidence: 99%

Insights into Hemoglobin Assembly through in Vivo Mutagenesis of α-Hemoglobin Stabilizing Protein

Khandros

Mollan

et al. 2012

Journal of Biological Chemistry

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“…Previous studies have reported that loss of AHSP expression results in globin precipitation in murine model and caused ineffective erythropoiesis, and more exacerbates ß-thalassemia [31, 32] and AHSP - knockdown cells demonstrated an increased reactive oxygen species (ROS) production and increased rate of apoptosis [33]. Moreover, AHSP gene expression is controlled by some regulatory elements, such as GATA binding protein 1 (GATA-1) [30], Organic cation transporter 1 (Oct-1) [34] and Erythroid Kruppel-like factor (EKLF) [35-37].…”

Section: Discussionmentioning

confidence: 99%

High Expression of AHSP, EPB42, GYPC and HEMGN Predicts Favorable Prognosis in FLT3-ITD-Negative Acute Myeloid Leukemia

Zhu¹,

Yi²,

Zhang³

et al. 2017

Cell Physiol Biochem

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Background/Aims: Acute myeloid leukemia (AML) is a heterogeneous clonal disease and patients with AML who harbor an FMS-like tyrosine kinase 3 (FLT3) mutation present several dilemmas for the clinician. This study aims to identify novel targets for explaining the dilemmas. Methods: We analyzed four microarray gene expression profiles to investigate changes in whole genome expression associated with FLT3-ITD mutation. Results: We identified 22 differentially expressed genes which are commonly expressed among all four profiles. Kaplan-Meier analysis of the dataset GSE12417 revealed that low expression of AHSP, EPB42, GYPC and HEMGN predicted poor prognosis (AHSP: P=0.0317, HR=1.894; EPB42: P=0.0382, HR=1.859; GYPC: P=0.0015, HR=2.051; HEMGN: P=0.0418, HR=1.838 in GSE12417 test cohort; AHSP: P=0.0279, HR=1.548; EPB42: P=0.0398, HR=1.505; GYPC: P=0.0408, HR=1.501; HEMGN: P=0.0143, HR=1.630 in GSE12417 validation cohort). When patients were FLT3-ITD positive, the expression of FLT3 was significantly increased (all P<0.05 in four profiles), and correleation analysis of four profiles revealed that the expression of the four candidate genes negatively correlated with FLT3 expression. Conclusions: Our findings suggest that AHSP, EPB42, GYPC and HEMGN may be suitable biomarkers for diagnostic or therapeutic strategies for FLT3-ITD-positive AML patients.

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“…2D, blue spheres) (reviewed in Weiss et al 2005;Favero and Costa 2011). These a-globin variants include Hbs Prato (a1 or a2 31 [B12] Arg .…”

Section: Selected Variants That Illustrate Important Aspects Of Hemogmentioning

confidence: 99%

Hemoglobin Variants: Biochemical Properties and Clinical Correlates

Thom

Dickson

Gell

et al. 2013

Cold Spring Harbor Perspectives in Medicine

225

182

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Diseases affecting hemoglobin synthesis and function are extremely common worldwide. More than 1000 naturally occurring human hemoglobin variants with single amino acid substitutions throughout the molecule have been discovered, mainly through their clinical and/or laboratory manifestations. These variants alter hemoglobin structure and biochemical properties with physiological effects ranging from insignificant to severe. Studies of these mutations in patients and in the laboratory have produced a wealth of information on hemoglobin biochemistry and biology with significant implications for hematology practice. More generally, landmark studies of hemoglobin performed over the past 60 years have established important paradigms for the disciplines of structural biology, genetics, biochemistry, and medicine. Here we review the major classes of hemoglobin variants, emphasizing general concepts and illustrative examples.

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Alpha-Hemoglobin-Stabilizing Protein: An Erythroid Molecular Chaperone

Cited by 25 publications

References 47 publications

Insights into Hemoglobin Assembly through in Vivo Mutagenesis of α-Hemoglobin Stabilizing Protein

Insights into Hemoglobin Assembly through in Vivo Mutagenesis of α-Hemoglobin Stabilizing Protein

High Expression of AHSP, EPB42, GYPC and HEMGN Predicts Favorable Prognosis in FLT3-ITD-Negative Acute Myeloid Leukemia

Hemoglobin Variants: Biochemical Properties and Clinical Correlates

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