Ice Recrystallization Inhibition Is Insufficient to Explain Cryopreservation Abilities of Antifreeze Proteins

被引:24
|
作者
Sun, Yuling [1 ,2 ]
Maltseva, Daria [1 ]
Liu, Jie [2 ]
Hooker, Theordore, II [3 ]
Mailaender, Volker [1 ,4 ]
Ramlov, Hans [5 ]
DeVries, Arthur L. [6 ]
Bonn, Mischa [1 ]
Meister, Konrad [1 ,3 ]
机构
[1] Max Planck Inst Polymer Res, D-55128 Mainz, Germany
[2] Chinese Acad Sci, Inst Chem, Beijing 100190, Peoples R China
[3] Univ Alaska Southeast, Juneau, AK 99801 USA
[4] Johannes Gutenberg Univ Mainz, Univ Med Ctr, Dermatol Dept, D-55131 Mainz, Germany
[5] Roskilde Univ, DK-4000 Roskilde, Denmark
[6] Univ Illinois, Urbana, IL 61801 USA
基金
美国国家卫生研究院;
关键词
RED-BLOOD-CELLS; HYDROXYETHYL STARCH; GROWTH; MEMBRANE; SURVIVAL; KERATINOCYTES; TRANSFUSION; MONOLAYERS; MECHANISM; INTEGRITY;
D O I
10.1021/acs.biomac.1c01477
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Antifreeze proteins (AFPs) and glycoproteins (AFGPs) are exemplary at modifying ice crystal growth and at inhibiting ice recrystallization (IRI) in frozen solutions. These properties make them highly attractive for cold storage and cryopreservation applications of biological tissue, food, and other water-based materials. The specific requirements for optimal cryostorage remain unknown, but high IRI activity has been proposed to be crucial. Here, we show that high IRI activity alone is insufficient to explain the beneficial effects of AF(G)Ps on human red blood cell (hRBC) survival. We show that AF(G)Ps with different IRI activities cause similar cell recoveries of hRBCs and that a modified AFGP variant with decreased IRI activity shows increased cell recovery. The AFGP variant was found to have enhanced interactions with a hRBC model membrane, indicating that the capability to stabilize cell membranes is another important factor for increasing the survival of cells after cryostorage. This information should be considered when designing novel synthetic cryoprotectants.
引用
收藏
页码:1214 / 1220
页数:7
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