Background[1-3]
BPGM erythrocyte 2,3-bisphosphoglycerate synthase antibody is a type of polyclonal antibody that can specifically bind to BPGM erythrocyte 2,3-bisphosphoglycerate synthase. It is mainly used for in vitro detection of BPGM erythrocyte 2 in samples. , the content of 3-bisphosphoglycerate synthase.
BPGM erythrocyte 2,3-bisphosphoglycerate synthase is a key enzyme in the process of glucose metabolism, catalyzing the mutual conversion between 3-phosphoglycerate and 2-phosphoglycerate. According to the dependence on the cofactor 2,3-bisphosphoglycerate in the catalytic reaction, it is divided into two types: cofactor-dependent PGM (dPGM) and cofactor-independent PGM (iPGM).
BPGM erythrocyte 2,3-diphosphoglycerate synthase antibody immunohistochemistry
2,3-Bisphosphoglycerate (2,3-BPG,2,3-Bisphosphoglycerate) is an intermediate product of the glycolysis pathway in life, 1,3-bisphosphoglycerate (1,3-BPG,1 , an isomer of 3-Bisphosphoglycerate), catalyzed by the enzyme bisphosphoglycerate mutase (BPGM, Bisphosphoglycerate mutase, formerly known as DPGM, diphosphoglycerate mutase) that only exists in red blood cells and placenta. generate. 2,3-BPG was first discovered in 1925 and its function was not elucidated until the 1960s by Benesch et al.
Because 2,3-BPG is an allosteric modulator of hemoglobin and binds to hemoglobin on an equimolar basis, it is an important factor in regulating the affinity between O2 and hemoglobin. When blood flows through tissues, the presence of high levels of 2,3-BPG can significantly increase the release of O2 and provide silica for tissue needs. Therefore, 2,3-BPG has great application value in preventing and treating altitude sickness and improving athletes’ physical functions.
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For research on the regulatory effect of H2S on blood oxygen saturation and oxygen-carrying capacity of red blood cells and the role of CBS in the placenta in intrauterine growth restriction
H2S from peripheral sources regulates the production of 2,3-BPG in red blood cells and affects the oxygen-carrying capacity of red blood cells. Previous studies have shown that in Cse gene knockout transgenics In mice, 2,3-BPG in red blood cells was significantly increased, and P50 increased. GYY4137 reduced 2,3-BPG and P50 in Cse-/- red blood cells.
At the same time, GYY4137 can also directly regulate 2,3-BPG and P50 in mouse and human erythrocyte bentonite cultured in vitro. Next, in the hypoxic animal model, it was found that: (1) Compared with normoxic mice, GYY4137 can reduce the increase in 2,3-BPG and P50 induced by hypoxia.
(2) In mouse red blood cells cultured in vitro, GYY4137 can reduce the production of 2,3-BPG in red blood cells induced by hypoxia.
H2S from peripheral sources regulates 2,3-BPG in erythrocytes 5. H2S regulates the cytoplasm-to-membrane translocation of BPGM 1. H2S regulates the activity of BPGM (1) Compared with WT mice, Cse- /-The activity of BPGM in the cytoplasm of mouse erythrocytes was significantly increased. GYY4137 treatment reduced the activity of BPGM in the cytoplasm of Cse-/- mice; at the same time, GYY4137 could also reduce the activity of BPGM in WT mice. (2) H2S treatment of in vitro cultured red blood cells can significantly reduce the activity of BPGM in the cytoplasm.
2. H2S inhibits the release of membrane-anchored BPGM into the cytoplasm (1) Western blotting results showed that compared with WT mice, the cytoplasmic distribution of BPGM in the erythrocytes of Cse-/- mice increased, and the cytoplasmic distribution of BPGM was also increased. reduce. GYY4137 treatment reduced the cytoplasmic distribution of BPGM in erythrocytes of Cse-/- mice and increased the membrane localization.
(3) Confocal results show that in WT mouse erythrocytes, BPGM is mainly located in the cell membrane of erythrocytes, while in Cse-/- mouse erythrocytes, most BPGM is located in the cytoplasm, and GYY4137 increases Cell membrane anchoring of BPGM.
(4) Western blotting results showed that GYY4137 increased the cell membrane localization of BPGM in isolated cultured erythrocytes and conversely reduced the cytoplasmic expression.
(5) Confocal results also show that GYY4137 promotes the translocation of BPGM from the cytoplasm to the plasma membrane in isolated cultured erythrocytes.
