Universal metastability of sickle hemoglobin polymerization

2021 ◽  
Author(s):  
Weijun Weng
Keyword(s):  
Sickle Hemoglobin

The orientation of sickle hemoglobin fibers within fascicles

1988 ◽  
Vol 46 ◽  
pp. 400-401
Author(s):  
Christopher A. Miller ◽  
Bridget Carragher ◽  
William A. McDade ◽  
Robert Josephs
Keyword(s):  
Sickle Cell ◽  
Sickle Cell Anemia ◽  
Relative Orientation ◽  
Unit Cell ◽  
Red Cell ◽  
High Ph ◽  
Sickle Hemoglobin ◽  
Polar Crystal ◽  
Helical Configuration

Highly ordered bundles of deoxyhemoglobin S (HbS) fibers, termed fascicles, are intermediates in the high pH crystallization pathway of HbS. These fibers consist of 7 Wishner-Love double strands in a helical configuration. Since each double strand has a polarity, the odd number of double strands in the fiber imparts a net polarity to the structure. HbS crystals have a unit cell containing two double strands, one of each polarity, resulting in a net polarity of zero. Therefore a rearrangement of the double strands must occur to form a non-polar crystal from the polar fibers. To determine the role of fascicles as an intermediate in the crystallization pathway it is important to understand the relative orientation of fibers within fascicles. Furthermore, an understanding of fascicle structure may have implications for the design of potential sickling inhibitors, since it is bundles of fibers which cause the red cell distortion responsible for the vaso-occlusive complications characteristic of sickle cell anemia.

scholarly journals Structural specificities in acylation of hemoglobin and sickle hemoglobin by diaspirins.

1981 ◽  
Vol 256 (13) ◽  
pp. 7046-7052
Author(s):  
L.E. Wood ◽  
D.N. Haney ◽  
J.R. Patel ◽  
S.E. Clare ◽  
G.Y. Shi ◽  
...  
Keyword(s):  
Sickle Hemoglobin

scholarly journals Monomer diffusion into polymer domains in sickle hemoglobin

1990 ◽  
Vol 58 (4) ◽  
pp. 1067-1073 ◽  
Author(s):  
M.R. Cho ◽  
F.A. Ferrone
Keyword(s):  
Sickle Hemoglobin ◽  
Monomer Diffusion

scholarly journals Aggregation of Normal and Sickle Hemoglobin in High Concentration Phosphate Buffer

2004 ◽  
Vol 87 (6) ◽  
pp. 4113-4121 ◽  
Author(s):  
Kejing Chen ◽  
Samir K. Ballas ◽  
Roy R. Hantgan ◽  
Daniel B. Kim-Shapiro
Keyword(s):  
Phosphate Buffer ◽  
High Concentration ◽  
Sickle Hemoglobin

scholarly journals Influence of Haptoglobin Polymorphism on Stroke in Sickle Cell Disease Patients

Genes ◽  
2022 ◽  
Vol 13 (1) ◽  
pp. 144
Author(s):  
Olivia Edwards ◽  
Alicia Burris ◽  
Josh Lua ◽  
Diana J. Wilkie ◽  
Miriam O. Ezenwa ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Sickle Cell Disease ◽  
Sickle Cell ◽  
Blood Cells ◽  
Cell Disease ◽  
Free Hemoglobin ◽  
Cerebral Tissue ◽  
Sickle Hemoglobin ◽  
Haptoglobin Polymorphism

This review outlines the current clinical research investigating how the haptoglobin (Hp) genetic polymorphism and stroke occurrence are implicated in sickle cell disease (SCD) pathophysiology. Hp is a blood serum glycoprotein responsible for binding and removing toxic free hemoglobin from the vasculature. The role of Hp in patients with SCD is critical in combating blood toxicity, inflammation, oxidative stress, and even stroke. Ischemic stroke occurs when a blocked vessel decreases oxygen delivery in the blood to cerebral tissue and is commonly associated with SCD. Due to the malformed red blood cells of sickle hemoglobin S, blockage of blood flow is much more prevalent in patients with SCD. This review is the first to evaluate the role of the Hp polymorphism in the incidence of stroke in patients with SCD. Overall, the data compiled in this review suggest that further studies should be conducted to reveal and evaluate potential clinical advancements for gene therapy and Hp infusions.

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