Pula G, Bianchi R, Ceccarelli P, Giambanco I, Donato R
Department of Experimental Medicine and Biochemical Sciences, University of Perugia, Italy.
FEBS Lett. 1990 Dec 17;277(1-2):53-8. doi: 10.1016/0014-5793(90)80808-v.
Porcine heart was observed to express annexins V (CaBP33) and VI in large amounts, and annexins III and IV in much smaller amounts. Annexin V (CaBP33) in porcine heart was examined in detail by immunochemistry. Homogenization and further processing of heart in the presence of EGTA resulted in the recovery of annexin V (CaBP33) in the cytosolic fraction and in an EGTA-resistant, Triton X-100-soluble fraction from cardiac membranes. Including Ca2+ in the homogenization medium resulted in a significant decrease in the annexin V (CaBP33) content of the cytosolic fraction with concomitant increase in the content of this protein in myofibrils, mitochrondria, the sarcoplasmic reticulum and the sarcolemma. The amount of annexin V (CaBP33) in each of these subfractions depended on the free Ca2+ concentration in the homogenizing medium. At the lowest free Ca2+ concentration tested, 0.8 microM, only the sarcolemma appeared to contain bound annexin V (CaBP33). Membrane-bound annexins V (CaBP33) and VI partitioned in two fractions, one EGTA-resistant and Triton X-100-extractable, and one Triton X-100-resistant and EGTA-extractable. Altogether, these data suggest that annexins V and VI are involved in the regulation of membrane-related processes.
观察发现猪心脏大量表达膜联蛋白V（CaBP33）和VI，少量表达膜联蛋白III和IV。通过免疫化学详细检测了猪心脏中的膜联蛋白V（CaBP33）。在存在乙二醇双四乙酸（EGTA）的情况下对心脏进行匀浆和进一步处理，导致膜联蛋白V（CaBP33）在胞质部分以及来自心肌膜的EGTA抗性、 Triton X - 100可溶性部分中回收。在匀浆培养基中加入Ca2 +导致胞质部分的膜联蛋白V（CaBP33）含量显著降低，同时该蛋白在肌原纤维、线粒体、肌浆网和肌膜中的含量增加。这些亚组分中每个组分的膜联蛋白V（CaBP33）量取决于匀浆培养基中的游离Ca2 +浓度。在测试的最低游离Ca2 +浓度0.8 microM时，似乎只有肌膜含有结合的膜联蛋白V（CaBP33）。膜结合的膜联蛋白V（CaBP33）和VI分为两个部分，一个是EGTA抗性且可被Triton X - 100提取的，另一个是Triton X - 100抗性且可被EGTA提取的。总之，这些数据表明膜联蛋白V和VI参与膜相关过程的调节。
