Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0006142 (breast cancer)
 160,383 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Serum immunoreactive prolyl hydroxylase protein (S-IRPH), galactosylhydroxylysyl glucosyltransferase activity (S-GGT) and the amino-terminal propeptide of type III procollagen [S-Pro(III)-N-P] were studied in 24 patients with primary hepatocellular carcinoma, 18 with secondary liver neoplasms and 35 with other malignant diseases but no evidence of liver involvement; this latter group included 13 patients with Burkitt's lymphoma, 11 with breast cancer and 11 with other neoplasms. Control values were determined for 60 apparently healthy Nigerians, S-IRPH and S-GGT were above the upper normal limit, defined as the mean + 2 SD of the controls, in all the patients with primary hepatocellular carcinoma and all but one with secondary liver neoplasms, whereas only one S-IRPH value and three S-GGT values exceeded this limit in the patients with other malignant diseases. The mean S-Pro(III)-N-P was even more elevated than S-IRPH and S-GGT in the primary and secondary liver neoplasm cases, but was also elevated in other malignant neoplasms; about one third of the patients with no evidence of liver involvement had a concentration exceeding the upper normal limit. A high correlation was found between the values for the three assays both in primary hepatocellular carcinoma and in the whole series of malignant diseases. The data suggest that primary and secondary malignant neoplasms of the liver have a high rate of collagen synthesis. The three assays may be of some value in the diagnosis of primary hepatocellular carcinoma and secondary liver involvement in other malignant diseases, and in monitoring the treatment provided.
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PMID:Enzymes of collagen synthesis and type III procollagen amino-propeptide in serum from Nigerians with hepato-cellular carcinoma and other malignant diseases. 628 64

Increased synthesis and degradation of extracellular matrix components are associated with breast cancer development. This study evaluated type I and type III procollagen mRNA expression and the corresponding protein synthesis and maturation, as well as the tissue distribution of these collagens, in benign breast lesions, infiltrating ductal carcinomas, and their metastases by in situ hybridization and immunohistochemistry. In the benign lesions, the type I and type III collagen bundles were regularly organized and the expression of the corresponding mRNA was weak, indicating a relatively slow collagen turnover. In the malignant tumours, increased expression of type I and type III procollagen mRNAs was observed in the fibroblastic cells of the stroma; the malignant epithelial cells did not participate. The staining of corresponding newly-synthesized pN-collagens showed aberrant bundles in the invasive front of the malignant tumours. Newly-synthesized type I and type III procollagens were occasionally observed in fibroblastic cells, particularly in grade 2 and grade 3 tumours. Metastases of breast carcinoma resembled poorly differentiated primary tumours with respect to their collagen synthesis and deposition. The increased synthesis of fibrillar type I and type III procollagens may serve as a pathway for tumour invasion. The enhanced synthesis is associated with the formation of aberrant collagen bundles, which may be more readily degradable and may thus facilitate breast tumour invasion.
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PMID:Aberrant type I and type III collagen gene expression in human breast cancer in vivo. 1021 Nov 14