Riewald M, Schleef R R
Department of Vascular Biology, Scripps Research Institute, La Jolla, California 92037, USA.
J Biol Chem. 1995 Nov 10;270(45):26754-7. doi: 10.1074/jbc.270.45.26754.
Serine proteinase inhibitors or serpins are a super-family of homologous proteins that are for the most part involved in the regulation of proteolytic processes in a variety of biological systems. Utilizing a polymerase chain reaction-based strategy we have cloned a novel member of the ovalbumin family of serpins from a human bone marrow cDNA library. The new gene encodes a 397-amino acid protein, designated bomapin, with a calculated molecular mass of 45 kDa and 48% amino acid identity with plasminogen activator inhibitor-2, human leukocyte elastase inhibitor, and cytoplasmic antiproteinase. A single 2.3-kilobase bomapin transcript is highly expressed in human bone marrow cells but was undetectable in all other analyzed human tissues. In vitro transcription and translation of the bomapin cDNA revealed the synthesis of an appropriately sized protein that was able to form SDS-stable complexes with thrombin and trypsin. The restricted expression of bomapin to the bone marrow raises the possibility that this serpin may play a role in the regulation of protease activities during hematopoiesis.
丝氨酸蛋白酶抑制剂或丝氨酸蛋白酶抑制因子是一类同源蛋白超家族，在很大程度上参与多种生物系统中蛋白水解过程的调控。利用基于聚合酶链反应的策略，我们从人骨髓cDNA文库中克隆了丝氨酸蛋白酶抑制因子卵清蛋白家族的一个新成员。这个新基因编码一种397个氨基酸的蛋白质，命名为博马平，计算分子量为45 kDa，与纤溶酶原激活物抑制剂-2、人白细胞弹性蛋白酶抑制剂和细胞质抗蛋白酶有48%的氨基酸同一性。一个2.3千碱基的博马平转录本在人骨髓细胞中高度表达，但在所有其他分析的人体组织中均未检测到。博马平cDNA的体外转录和翻译显示合成了一种大小合适的蛋白质，该蛋白质能够与凝血酶和胰蛋白酶形成SDS稳定复合物。博马平在骨髓中的限制性表达增加了这种丝氨酸蛋白酶抑制因子可能在造血过程中调节蛋白酶活性的可能性。
