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)

We have raised monoclonal antibodies against human milk fat globule membrane antigens and previously shown that one of them, called III D 5, recognises a glycoprotein associated with estrogen receptor activity of breast cancer. In immunoblotting it was shown that the molecule in human milk exclusively stained with III D 5 also binds peanut agglutinin (PNA) and Ricinus communis. In this study we correlate the staining of III D 5 and binding of lectins to tissue sections fixed in formalin and embedded in paraffin. Similar reactions were seen only with III D 5 and PNA. Our results suggest that III D 5 and PNA detect overlapping antigenic epitopes in mammary carcinoma. This is in keeping with previous results that PNA or III D 5 reactivity is correlated with estrogen receptor status of breast cancer.
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PMID:Reactivity of a monoclonal antibody recognizing an estrogen receptor regulated glycoprotein in relation to lectin histochemistry in breast cancer. 309 49

In estrogen-receptor-positive human breast cancer cell lines (MCF7, ZR75-1), estrogens specifically increase the secretion into the culture medium of a 52,000 Da (52K) glycoprotein and stimulate cell proliferation. The 52K protein has been purified to homogeneity using monoclonal antibodies and identified as the secreted precursor of a cathepsin D bearing mannose-6-phosphate signals. The secreted precursor 52K protein is mitogenic in vitro in estrogen-deprived MCF7 cells, can be taken up by these cells via mannose-6-phosphate receptors, and can degrade extracellular matrix and proteoglycans following its auto-activation. The protease is also produced constitutively by ER-negative cell lines, and is inducible by tamoxifen in some antiestrogen-resistant variants. The corresponding cDNA has been cloned using N-terminal sequencing of the protein and monoclonal antibodies. Its complete sequencing indicates a strong homology with pro-cathepsin D of normal tissues. Using a cDNA probe, the regulation of 52K cathepsin D mRNA by estrogens and antiestrogens has been studied and chromosome localization determined by in situ hybridization. Clinical studies using both immunohistochemistry and immunoenzymatic assay of breast cancer cytosol have shown that the concentration of total cellular cathepsin D (52K + 48K + 34K) is related to the proliferation of mammary ducts and to the prognosis of breast cancer. Its cytosolic concentration in primary tumors of postmenopausal patients is correlated slightly with lymph node invasion and significantly with shorter disease-free intervals in a 6-year retrospective study with the Danish Breast Cancer Groups and Finsen Institute (S. Thorpe et al.).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Structure, function, regulation and clinical significance of the 52K pro-cathepsin D secreted by breast cancer cells. 314 27

HMFG antigen is a tumour associated glycoprotein that has been immunohistochemically shown to be expressed by malignant cells in breast and ovarian and to a lesser degree in gastro-intestinal carcinomas. We have developed a non-isotopic sandwich ELISA for secretory HMFG antigen utilizing a polyclonal catcher and a tracer monoclonal antibody (MAb). 52/52 of healthy medical students (controls) had a serum value under 400 U/ml whereas 15/30 patients (50%) with evident ovarian cancer and 13/37 (35%) with advanced breast cancer had a value exceeding 400 U/ml. From other patients with malignant tumours 2/14 (14%) with endometrial carcinoma, 0/5 with cervical carcinoma, 0/5 with vulvar carcinoma, 1/33 with gastro-intestinal carcinoma, 0/4 with oesophageal carcinoma and 2/45 of patients with leukemia or lymphoma had an elevated serum HMFG value. Four cases of Crohn disease, 3 cases of ulcerative colitis and 2 cases of pelvic inflammatory disease all showed a serum value below 400 U/ml. Progression of ovarian cancer was accompanied by increasing serum HMFG antigen levels. The antigen detected by our assay is different from CA 125 but may be related with the tumour associated antigen CA 15-3.
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PMID:Elevated serum HMFG antigen levels in breast and ovarian cancer patients measured with a sandwich ELISA. 316 44

CA72-4 is a novel quantitative immunoradiometric assay system utilizing two monoclonal antibodies CC-49 and B72.3, which recognize a tumor-associated glycoprotein (TAG-72). We have utilized the CA72-4 RIA kit to measure serum levels of TAG-72 in 205 patients with carcinoma and 192 patients without carcinoma. The cut-off value (4.0 U/ml) was obtained according to the levels and the distribution of CA72-4 in 468 healthy individuals. The positive rates in 82 patients with gastric cancer, 55 with colorectal cancer, 24 with pancreatico-choledochal cancer, 36 with breast cancer, and 3 with ovarian cancer were 52%, 55%, 46%, 39%, and 67%, respectively. Fifty percent of the sera from 205 patients with carcinoma demonstrated increased levels of CA72-4, whereas only 10% of the sera from 192 patients without evidence of malignancy showed levels more than 4.0 U/ml. The average level of serum CA72-4 in the patients with carcinoma was 38.6 U/ml, much higher than that (2.7 U/ml) in patients without malignancy. The patients with gastrointestinal cancer at advanced stages or at recurrence showed higher levels of serum CA72-4 than the patients with cancer at early stages. These results thus indicate that CA72-4 is clinically useful as a novel tumor marker, especially for monitoring serum levels of TAG-72 in patients with gastrointestinal cancer, breast cancer, ovarian cancer and other epithelial malignancies.
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PMID:[Levels of circulating tumor-associated glycoprotein (TAG-72) in patients with carcinoma using a novel tumor marker, CA 72-4]. 316 66

Murine monoclonal antibody 3E1.2, made against human breast cancer cells, detects a glycoprotein (Mr greater than 300,000) called mammary serum antigen (MSA) which is elevated in the serum of patients with breast cancer. An enzyme immunoassay was developed to detect MSA in human serum and used to detect MSA in subjects with breast cancer and other diseases. Raised levels of MSA (greater than 300 inhibition units) were found in the serum of 1.9% of 2406 blood donors, in 18% of sera from 40 subjects with benign breast disease, and in 16% of sera from 222 subjects with non-breast cancers. However, in patients with a diagnosis of breast cancer, 76% (84 of 110) of Stage I and II, and 86% (142 of 166) of Stage III and IV had levels of greater than 300 inhibition units. Nineteen % of patients, classified clinically disease free, had raised MSA levels. In 34 of 37 (92%) patients followed over 2 to 11 mo the level of MSA correlated with the clinical course of disease. Changes in MSA levels not only corresponded to changes in the clinical course of disease, but also preceded the clinical detection of progressive disease. Immunoblotting has detected a heterogeneous molecule of Mr greater than 300,000 and been used to confirm the elevation of MSA in breast cancer patients. Determination of MSA level may be useful for the detection of breast cancer and for monitoring progress of disease and response to therapy.
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PMID:Detection of mammary serum antigen in sera from breast cancer patients using monoclonal antibody 3E1.2. 319 82

Gross Cystic Disease Fluid Protein (GCDFP-15) is a 60,000 dalton glycoprotein isolated from human breast cyst fluid, composed of four 15,000 dalton monomers. Carbohydrate analysis indicates that each monomer has a single carbohydrate chain of the complex type. GCDFP-15 intravenously injected into rats showed a rapid circulatory clearance, the rate of clearance being faster in female animals [t1/2 = 12.8 (+/- 2.0) min. females, and 16.7 (+/- 2.6) min. males]. The major organs of clearance were the liver (70%) and kidneys (15%). Immunoperoxidase staining showed localization in Kupffer cells and the proximal convoluted tubules of the kidney. Removal of sialic acid from GCDFP-15 resulted in a more rapid clearance (t1/2 = 2.2 min) by the liver (85%). This clearance was inhibited by coinjection of asialo alpha 1 acid glycoprotein. About 3% of GCDFP-15 was excreted in bile with a transit time through the liver of 38 min. Examination of the uptake of GCDFP-15 by isolated rat Kupffer cells showed that yeast mannan, fucosylated BSA, and carcinoembryonic antigen (CEA) failed to inhibit uptake, though the binding of GCDFP-15 was clearly saturable. This suggests that a novel receptor system on the rat Kupffer cell may be responsible for GCDFP-15 clearance.
Breast Cancer Res Treat 1988 Oct
PMID:Hepatic clearance and metabolism in the rat of a human breast cancer associated glycoprotein (GCDFP-15). 324 52

The murine monoclonal antibody (MAb) DF3 was prepared against a human breast carcinoma. Previous studies have demonstrated that DF3 antigen levels are elevated in plasma of patients with breast cancer. Furthermore, MAb DF3 reacts with circulating glycoproteins of different molecular weights ranging from approximately 300 to 450 kd. The present study demonstrates that plasma DF3 antigen is comprised of at least four moieties with slow (S), intermediate (I), rapid (R) and very rapid (VR) electrophoretic mobilities. The electrophoretic mobility patterns for circulating DF3 antigen differ among individuals. Moreover, DF3 antigen is detectable in urine, and the electrophoretic mobility of the urinary moieties is similar, but not identical, to that in the plasma. Studies in family members suggest that the electrophoretic heterogeneity of plasma DF3 antigen is determined by codominant expression of multiple alleles at a single locus. This locus may code for the core protein of DF3 antigen. These findings thus identify a genetically determined polymorphism of a circulating tumor-associated glycoprotein.
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PMID:Genetically determined polymorphism of the circulating human breast cancer-associated DF3 antigen. 333 5

MAM-6 is a major epithelial sialomucin which is abundantly present at the apical surface of ductal and alveolar cells of normal tissues and on many different carcinoma cells. MAM-6, as defined by monoclonal antibodies, consists of one or two sialylated glycoproteins with apparent molecular masses of over 400 kDa under reducing as well as nonreducing conditions. The mobility and number of glycoproteins immunoprecipitated vary depending on the cell line of origin. We have employed immunoprecipitation techniques to study the biosynthesis and glycosylation of this mucin. The biosynthesis of MAM-6 was studied in the ZR-75-1 breast cancer cell line. Two glycoproteins with apparent molecular masses of approximately 450 and 650 kDa, representing the mature form, were immunoprecipitated. By pulse-chase analysis, we show that the biosynthesis of the 450-kDa glycoprotein proceeded through intermediates of 220, 200, and 500 kDa which became perceptible after 1, 4, and 30 min, respectively. The biosynthesis of the 650-kDa glycoprotein followed a similar course through 380, 350, and 700-kDa intermediates. The processing of the 220- and 350-kDa precursors involves a rare proteolytic cleavage step which occurs in the endoplasmic reticulum. The late precursors of 500/700 kDa, observed after 30 min chase, and the mature glycoproteins were generated by extensive O-linked glycosylation. The formation of the 500/700-kDa precursors was not affected by monensin. However, the final step of maturation, sialylation of the 500/700-kDa precursors, could be inhibited by monensin. The extensive O-linked glycosylation causes the apparent high molecular weight as observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Our data on the biosynthesis show that the early MAM-6 precursors contain N-linked glycans, suggesting the presence of N-linked glycans on the mature MAM-6 molecule. Although the copresence of N- and O-linked glycans has been found on many molecules, no N-linked glycans have been reported on mucus glycoproteins previously.
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PMID:Biosynthesis of MAM-6, an epithelial sialomucin. Evidence for involvement of a rare proteolytic cleavage step in the endoplasmic reticulum. 334 46

Laminin P1, a pepsin-resistant fragment of the glycoprotein laminin, was determined in body fluids using a double-antibody radioimmunoassay. The median serum concentrations found were: men 1.32, premenopausal women 1.22, postmenopausal women 1.38 and pregnant women (35th gestational week) 2.18 U/ml. The median concentration in amniotic fluid was 1.90, in urine 0.28 and in follicle cyst fluid 1.74 U/ml. During gestation, rising serum levels of up to 5 U/ml were observed which decreased within a few days after delivery. The cut-off value of laminin P1 for 95% specificity of the normal female control group was found to be 1.8 U/ml. The frequencies of elevated serum concentrations were 11, 18, 23 and 33% in patients with primary malignant lesions of the breast, endometrium, cervix and ovary, respectively, and rose up to 50-51% in patients with recurrent or metastatic gynaecological cancer. Laminin P1 was found in high concentrations in the cytosol fractions of breast cancer biopsies. Long-term sequential determinations of serum levels in 10 individual patients with progressive cancer reflected the course of the disease in 8 cases. Although laminin P1 can be considered as a tumour-associated protein, low sensitivity to primary cancer and insufficient specificity limit its application as a tumour marker and its usefulness in monitoring of patients with gynaecological cancer.
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PMID:Radioimmunoassay of laminin P1 in body fluids of pregnant women, patients with gynaecological cancer and controls. 336 85

Lymphocytes from lymph nodes obtained from breast cancer patients undergoing mastectomy were fused with the 0467.3, UC729HF2, or KR-12 human cell lines, totaling 42 fusions with lymphocytes from 23 patients. A total of 1696 human-human hybridomas were generated, 675 (39.8%) of which produced human IgG and/or IgM. Seventy-three human hybridomas produced antibodies binding to autologous malignant breast tissue and/or MCF-7 cells, as assayed by immunohistology or by cell-binding enzyme-linked immunosorbent assay. Twelve of these hybridomas, all reacting with malignant breast tissue, were subcloned to stabilize the production of human immunoglobulin. The reaction patterns of these 12 human monoclonal antibodies were investigated further by immunohistology on formalin-fixed, paraffin-embedded tissues. The reaction patterns of the various antibodies showed substantial variation and the antibodies reacted with a varying frequency with antigens expressed by different malignant breast tumors. One of these antibodies, MAC 40/43 (IgM), reacted with malignant breast and colon carcinomas and other epithelial derived neoplasms but did not react with normal breast tissue or with other normal and malignant tissues tested, except for a weak reaction with certain normal epithelial tissues. The antigen defined by MAC 40/43 was identified as a Mr approximately equal to 47,000 glycoprotein.
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PMID:Human-human hybridomas and human monoclonal antibodies obtained by fusion of lymph node lymphocytes from breast cancer patients. 336 3


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