Zhu G G, Risteli L, Mäkinen M, Risteli J, Kauppila A, Stenbäck F
Department of Obstetrics and Gynecology, University of Oulu, Finland.
Cancer. 1995 Feb 15;75(4):1010-7. doi: 10.1002/1097-0142(19950215)75:4<1010::aid-cncr2820750417>3.0.co;2-o.
Type I collagen is a major constituent of the interstitial connective tissue. Although ovarian carcinoma is known to induce the expression of type I collagen in the peritoneal cavity, the distribution and metabolic activity of this collagen in ovarian tumor tissue are not known.
The distributions and staining intensities of different molecular forms of type I collagen in ovarian neoplasms were studied immunohistochemically with antibodies to the aminoterminal propeptide of type I procollagen (PINP) and the cross-linked carboxyterminal telopeptide of type I collagen (ICTP), reflecting the presence of newly synthesized and old, cross-linked type I collagen, respectively.
A regular pattern of moderately staining, relatively uniform fibers was observed in the stroma of benign serous and mucinous cystadenomas, indicating limited participation in tumor growth. The staining was accentuated subepithelially in borderline epithelial neoplasms and in well differentiated cystadenocarcinomas, suggesting induction of the stromal collagen synthesis by the tumor cells. Fewer degraded collagen fibers were found in moderately differentiated carcinomas, most likely because of enzymatic degradation of the stroma surrounding the neoplasms during tumor spread. Strongly staining, irregular collagen fibers occurred closely around islets of tumor cells in undifferentiated malignant neoplasms and in metastases of ovarian carcinomas; also, intracellular staining was present in part of the malignant cells. In most cases, the staining reactions obtained with the two different antibodies were similar, probably indicating rapid processing of the newly synthesized type I collagen (indicated by PINP) to a maturely cross-linked form (indicated by ICTP).
Synthetic and degradative processes are typical of the collagenous matrix in malignant ovarian tumors. Aberrant expression of type I collagen may occur in anaplastic ovarian carcinomas.
I型胶原蛋白是间质结缔组织的主要成分。虽然已知卵巢癌可诱导腹膜腔中I型胶原蛋白的表达,但该胶原蛋白在卵巢肿瘤组织中的分布和代谢活性尚不清楚。
使用针对I型前胶原氨基末端前肽(PINP)和I型胶原蛋白交联羧基末端端肽(ICTP)的抗体,通过免疫组织化学研究卵巢肿瘤中不同分子形式的I型胶原蛋白的分布和染色强度,分别反映新合成的和陈旧的、交联的I型胶原蛋白的存在情况。
在良性浆液性和黏液性囊腺瘤的间质中观察到适度染色、相对均匀的纤维的规则模式,表明其对肿瘤生长的参与有限。在交界性上皮性肿瘤和高分化囊腺癌中,上皮下染色增强,提示肿瘤细胞诱导间质胶原蛋白合成。在中分化癌中发现较少的降解胶原纤维,最可能的原因是肿瘤扩散过程中肿瘤周围间质的酶促降解。在未分化恶性肿瘤和卵巢癌转移灶中,强染色、不规则的胶原纤维紧密围绕肿瘤细胞岛;此外,部分恶性细胞内也有染色。在大多数情况下,用两种不同抗体获得的染色反应相似,可能表明新合成的I型胶原蛋白(由PINP表示)快速加工成成熟的交联形式(由ICTP表示)。
合成和降解过程是恶性卵巢肿瘤胶原基质的典型特征。I型胶原蛋白的异常表达可能发生在间变性卵巢癌中。