Hirose H, Ozsvath K J, Xia S, Gaetz H P, Tilson M D
Columbia University and the Department of Surgery, St. Luke's/Roosevelt Hospital Center, New York, NY 10019, USA.
Pathobiology. 1998;66(1):1-4. doi: 10.1159/000027988.
We have reported that immunoglobulin G (IgG) harvested from specimens of aneurysmal abdominal aorta (AAA) is immunoreactive with a fibrillar component of the matrix of the aortic adventitia. In further studies we have reported the partial amino acid sequence of a 40-kDa protein, purified from the adventitia of the human aorta, which we have called aortic aneurysm antigenic protein-40 kDa (AAAP-40). AAAP-40 has homologies with bovine microfibril-associated glycoprotein-36 kDa (MAGP-36). Both AAAP-40 and MAGP-36 have homologies to fibrinogen beta (FB-b) and vitronectin (VN). The purposes of the present experiments were (1) to determine whether antibodies against VN and fibrinogen are immunoreactive with elements of the normal and/or aneurysmal aortic wall, and (2) to determine whether these antibodies are immunoreactive with soluble extracts of aortic proteins.
Paraffin-embedded tissue sections of normal and aneurysmal aorta were probed with polyclonal rabbit antihuman VN and antihuman FB-b antibodies. Immunoblots of soluble aortic proteins were evaluated with the same antibodies. Histochemical preparations with Gomori's aldehyde fuchsin and elastin-von-Gieson solutions were also performed.
Anti-VN and FB-b antibodies reacted with matrix fibrils in the aortic adventitia in both normal and aneurysmal specimens, with a distribution that resembles the appearance of fibrils that are stained by Gomori's reaction. By comparison to normal adventitial fibrils, fibrils in the specimens from AAA appeared fragmented, coiled, and frayed. Antibodies against VN and FB-b were immunoreactive in immunoblots with a soluble aortic protein of molecular weight approximately 40 kDa, consistent with the migration of AAAP-40.
There appear to be immunodeterminants in AAAP-40 that are recognized by polyclonal antibodies against VN and FB-b.
我们曾报道，从腹主动脉瘤（AAA）标本中收获的免疫球蛋白G（IgG）与主动脉外膜基质的纤维成分具有免疫反应性。在进一步研究中，我们报道了从人主动脉外膜纯化的一种40 kDa蛋白的部分氨基酸序列，我们将其称为主动脉瘤抗原蛋白-40 kDa（AAAP-40）。AAAP-40与牛微原纤维相关糖蛋白-36 kDa（MAGP-36）具有同源性。AAAP-40和MAGP-36均与纤维蛋白原β（FB-b）和玻连蛋白（VN）具有同源性。本实验的目的是：（1）确定抗VN和纤维蛋白原的抗体是否与正常和/或动脉瘤性主动脉壁成分具有免疫反应性；（2）确定这些抗体是否与主动脉蛋白的可溶性提取物具有免疫反应性。
用兔抗人VN和抗人FB-b多克隆抗体检测正常和动脉瘤性主动脉的石蜡包埋组织切片。用相同抗体评估主动脉可溶性蛋白的免疫印迹。还进行了Gomori醛复红和弹性蛋白-冯吉森溶液的组织化学制备。
抗VN和FB-b抗体在正常和动脉瘤标本的主动脉外膜中均与基质纤维发生反应，其分布类似于经Gomori反应染色的纤维外观。与正常外膜纤维相比，AAA标本中的纤维显得破碎、盘绕和磨损。抗VN和FB-b抗体在免疫印迹中与分子量约为40 kDa的主动脉可溶性蛋白具有免疫反应性，这与AAAP-40的迁移情况一致。
AAAP-40中似乎存在被抗VN和FB-b多克隆抗体识别的免疫决定簇。
