BIOLOGY OF SERUM AMYLOID P-COMPONENT
BIOLOGY OF SERUM AMYLOID P-COMPONENT
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DOI：
10.1111/j.1749-6632.1982.tb22144.x
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发表时间：
1982-01-01
影响因子：
5.2
通讯作者：
FEINSTEIN, A
中科院分区：
文献类型：
--
作者：
PEPYS, MB;BALTZ, ML;FEINSTEIN, A
血清淀粉样蛋白P组分(SAP)是一种正常人血浆糖蛋白，它是通过与抗淀粉样物提取物的抗血清发生交叉反应而发现的。从血清中分离的SAP与从淀粉样物中分离的淀粉样蛋白P组分[AP]之间尚未发现区别。它们在非变性条件下在梯度聚丙烯酰胺凝胶电泳(PAGE)和十二烷基硫酸钠(SDS)-PAGE中有和没有还原(MB Pepys)中运行相同。Rf Dyck，M.Skinner和As Cohen，未出版]。在针对抗AP或抗SAP血清的双重免疫差异分析中，它们给出了完全相同的线，可用的部分氨基酸序列也是相同的。3观察到SAP和AP与未被取代的普通琼脂Se‘，~进行特异的钙依赖性结合，极大地促进了这些蛋白在人和其他动物中的分离，并为其结构和功能鉴定提供了材料。然而，SAP的体内功能仍不清楚。毫无疑问，它与淀粉样变性有密切的联系，但目前还不能确定这是具有致病意义的还是一种附带现象。一些假定SAP的功能，如参与补体激活或参与凝血级联，已经被其他观察到，特别是在正常的TISS~ES中存在免疫交叉反应蛋白，最近，它的选择性结合其他感兴趣的血浆蛋白的能力，似乎可能为其生物学作用提供新的见解。小鼠SAP作为一个主要的急性时相反应‘~’的行为与其他被测试的物种的SAP水平模式是一个有趣的差异，是研究急性时相反应的一个有价值的实验模型。无论从哪一方面得出结论
Serum amyloid P component (SAP) is a normal human plasma glycoprotein which was discovered by its cross-reactivity with antisera raised against extracts of amyloid deposits.'No difference has yet been discovered between SAP isolated from serum and amyloid P component [AP) isolated from amyloid deposits. They run identically in nondenaturing conditions in gradient polyacrylamide gel electrophoresis (PAGE) and in sodium dodecyl sulphate (SDS)-PAGE with and without reduction (MB Pepys. RF Dyck, M. Skinner and AS Cohen, unpublished]. They give lines of complete identity in double immunodiff usion analysis against anti-AP or anti-SAP sera'and the partial amino acid sequences available are also the same. 3The observation that SAP and AP undergo specific calcium-dependent binding to plain unsubstituted agar~ se',~ has greatly facilitated the isolation of these proteins in man and other animals and provided material for their structural and functional characterization. However the in vivo function of SAP remains obscure. It undoubtedly has an intimate association with amyloidosis but it is not yet possible to decide whether this is of pathogenetic significance or is an epiphenomenon. Some functions postulated for SAP, such as participation in complement activation5 or involvement in the coagulation cascade,'have been Other observations, particularly of the presence of an immunologically cross-reactive protein in normal tiss~ es'~~'~ and, most recently, of its capacity for selective binding of other interesting plasma proteins,''seem likely to provide new insights into its biological role. The behavior of mouse SAP as a major acute phase rea~ tant'~ is an intriguing divergence from the pattern of SAP levels in other species tested"-" and is a valuable experimental model for studies of the acute phase response in general. Whatever conclusions may be reached from