Bode M K, Mosorin M, Satta J, Risteli L, Juvonen T, Risteli J
Department of Clinical Chemistry, FIN-90014, University of Oulu, Finland.
Eur J Vasc Endovasc Surg. 2002 May;23(5):413-20. doi: 10.1053/ejvs.2002.1606.
the extent of the processing of type III procollagen to type III collagen was determined in nine human abdominal aortic aneurysms (AAA), and compared with ten samples of aortoiliac occlusive disease (AOD).
the aminoterminal propeptide (PIIINP) and telopeptide (IIINTP) of type III procollagen and collagen, respectively, were immunologically measured in the soluble and insoluble fractions of the extracellular matrix. The assay for PIIINP in the insoluble matrix was further validated.
the insoluble matrices of AAAs contained at least 12 times more incompletely processed type III pN-collagen than AOD specimens (0.74% and 0.061%, respectively). Also, the soluble extracts of AAAs tended to contain more non-processed type III pN-collagen than free, properly cleaved aminoterminal propeptide.
the larger amount of type III pN-collagen suggests an alteration in the metabolism of type III collagen in AAAs. This may partially explain the decreased tensile strength of the aortic tissue.
测定9例人腹主动脉瘤(AAA)中III型前胶原向III型胶原的加工程度,并与10例主髂动脉闭塞性疾病(AOD)样本进行比较。
分别在细胞外基质的可溶性和不溶性部分对III型前胶原的氨基末端前肽(PIIINP)和III型胶原的端肽(IIINTP)进行免疫测定。对不溶性基质中PIIINP的检测方法进行了进一步验证。
AAA的不溶性基质中未完全加工的III型前胶原(pN-胶原)含量至少比AOD标本高12倍(分别为0.74%和0.061%)。此外,AAA的可溶性提取物中未加工的III型前胶原含量往往比游离的、正确切割的氨基末端前肽更多。
大量的III型前胶原表明AAA中III型胶原的代谢发生了改变。这可能部分解释了主动脉组织抗张强度的降低。