Abstract
We have evaluated the radioimmunoassay for type I procollagen carboxy terminal peptide (type I C-peptide), which is liberated from type I procollagen during its conversion to collagen, in the serodiagnosis of scirrhous carcinoma of the stomach. The mean (SD) serum concentration of type I C-peptide in 39 normal subjects was 41.7 (19.7) ng/ml. The mean serum values and the positive ratio of type I C-peptide in 11 patients with stages II and III scirrhous carcinoma of the stomach were 91.2 (41.9) ng/ml and 54.5%, respectively. In 10 patients with other types of gastric carcinoma, the mean type I C-peptide values were not significantly different from the normal value. Serum type I C-peptide values reflected the clinical course of scirrhous gastric carcinoma in five patients who underwent either operation or chemotherapy. The measurement of serum type I C-peptide concentrations could provide a useful way of diagnosing and monitoring scirrhous carcinoma of the stomach.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Al-Adnani M. S., Kirrane J. A., McGee J. O. Inappropriate production of collagen and prolyl hydroxylase by human breast cancer cells in vivo. Br J Cancer. 1975 Jun;31(6):653–660. doi: 10.1038/bjc.1975.112. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bolarin D. M., Savolainen E. R., Kivirikko K. I. Enzymes of collagen synthesis and type III procollagen amino-propeptide in serum from Nigerians with hepato-cellular carcinoma and other malignant diseases. Int J Cancer. 1982 Apr 15;29(4):401–405. doi: 10.1002/ijc.2910290407. [DOI] [PubMed] [Google Scholar]
- Dehm P., Olsen B. R., Prockop D. J. Antibodies to chick-tendon procollagen. Affinity purification with the isolated disulfide-linded NH2-terminal extensions and reactivity with a component in embryonic serum. Eur J Biochem. 1974 Jul 1;46(1):107–116. doi: 10.1111/j.1432-1033.1974.tb03602.x. [DOI] [PubMed] [Google Scholar]
- Iozzo R. V. Proteoglycans and the intercellular tumor matrix. Curr Top Pathol. 1987;77:207–221. doi: 10.1007/978-3-642-71356-9_9. [DOI] [PubMed] [Google Scholar]
- Labat-Robert J., Robert L. Aging of the extracellular matrix and its pathology. Exp Gerontol. 1988;23(1):5–18. doi: 10.1016/0531-5565(88)90015-0. [DOI] [PubMed] [Google Scholar]
- Murphy W. H., von der Mark K., McEneany L. S., Bornstein P. Characterization of procollagen-derived peptides unique to the precursor molecule. Biochemistry. 1975 Jul 15;14(14):3243–3250. doi: 10.1021/bi00685a034. [DOI] [PubMed] [Google Scholar]
- Niitsu Y., Ito N., Kohda K., Owada M., Morita K., Sato S., Watanabe N., Kohgo Y., Urushizaki I. Immunohistochemical identification of type I procollagen in tumour cells of scirrhous adenocarcinoma of the stomach. Br J Cancer. 1988 Jan;57(1):79–82. doi: 10.1038/bjc.1988.13. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rohde H., Vargas L., Hahn E., Kalbfleisch H., Bruguera M., Timpl R. Radioimmunoassay for type III procollagen peptide and its application to human liver disease. Eur J Clin Invest. 1979 Dec;9(6):451–459. doi: 10.1111/j.1365-2362.1979.tb00912.x. [DOI] [PubMed] [Google Scholar]
- Sakakibara K., Suzuki T., Motoyama T., Watanabe H., Nagai Y. Biosynthesis of an interstitial type of collagen by cloned human gastric carcinoma cells. Cancer Res. 1982 May;42(5):2019–2027. [PubMed] [Google Scholar]
- Taubman M. B., Goldberg B., Sherr C. Radioimmunoassay for human procollagen. Science. 1974 Dec 20;186(4169):1115–1117. doi: 10.1126/science.186.4169.1115. [DOI] [PubMed] [Google Scholar]
- Uitto J., Lichtenstein J. R., Bauer E. A. Characterization of procollagen synthesized by matrix-free cells isolated from chick embryo tendons. Biochemistry. 1976 Nov 2;15(22):4935–4942. doi: 10.1021/bi00667a029. [DOI] [PubMed] [Google Scholar]