Analysis of glycoproteins released from benign and malignant human breast: Changes in size and fucosylation with malignancy

CA15.3, MCA, CAM26, CAM29 Are Members of a Polymorphic Family of Mucin-Like Glycoproteins

“…Aside from the concentration of mucin subsets, the frequency of epitope re petitions may influence the test results. The affinity and access of antibodies to binding sites may be another important factor; aber rant glycosylation of proteins was assumed in breast tumors compared with normal tis sue [13,26]. Our clinical observations on breast cancer patients further supported the theoretical expectations on the variety of mucin tests.…”

CA15.3, MCA, CAM26, CAM29 Are Members of a Polymorphic Family of Mucin-Like Glycoproteins

“…Aside from the concentration of mucin subsets, the frequency of epitope re petitions may influence the test results. The affinity and access of antibodies to binding sites may be another important factor; aber rant glycosylation of proteins was assumed in breast tumors compared with normal tis sue [13,26]. Our clinical observations on breast cancer patients further supported the theoretical expectations on the variety of mucin tests.…”

Immunohistochemical Distribution of a Breast Cancer‐Associated Glycoprotein

“…We have shown in a wide range of tissues the distribution of the high molecular weight glycoprotein (M r 230 OOOkDa), previously identified by us as tumour-associated (Rye and Walker, 1989). Our findings indicate that the expression of this glycoprotein, as detected by the polyclonal antiserum P5252-2, is clearly specific to epithelial cells.…”

“…The antiserum was specific for epithelial cells and showed no reactivity with plasma cells, stromal tissue or other non-epithelial cells. Immunoblotting with P5252-2 identified a broad band of apparent M r 230 OOOkDa on SDS discontinuous polyacrylamide gel electrophoresis (Figure 1), which corresponds to the purified fucosylated N-Iinked glycoprotein used as the immunogen, that has been previously identified (Rye and Walker, 1989).…”

Alterations in the Serum Glycome Due to Metastatic Prostate Cancer

“…The alteration in glycosylation has been previously correlated to tumor progression. [11][12][13]21,36 The differences observed in our work among the high-mannose, complex biantennary, complex triantennary (fucosylated and nonfucosylated), and complex tretraantennary (fucosylated and nonfucosylated) show ANOVA test p-values better than 0.01, indicating there is a less than 1% probability that this difference is due to a chance alone. An increase in the overall fucosylation in the case of the cancer samples, thus, appears statistically significant, as suggested by the ANOVA test p-value of 0.0006.…”

CA15.3, MCA, CAM26, CAM29 Are Members of a Polymorphic Family of Mucin-Like Glycoproteins

“…Aside from the concentration of mucin subsets, the frequency of epitope re petitions may influence the test results. The affinity and access of antibodies to binding sites may be another important factor; aber rant glycosylation of proteins was assumed in breast tumors compared with normal tis sue [13,26]. Our clinical observations on breast cancer patients further supported the theoretical expectations on the variety of mucin tests.…”

Immunohistochemical Distribution of a Breast Cancer‐Associated Glycoprotein

“…We have shown in a wide range of tissues the distribution of the high molecular weight glycoprotein (M r 230 OOOkDa), previously identified by us as tumour-associated (Rye and Walker, 1989). Our findings indicate that the expression of this glycoprotein, as detected by the polyclonal antiserum P5252-2, is clearly specific to epithelial cells.…”

“…The antiserum was specific for epithelial cells and showed no reactivity with plasma cells, stromal tissue or other non-epithelial cells. Immunoblotting with P5252-2 identified a broad band of apparent M r 230 OOOkDa on SDS discontinuous polyacrylamide gel electrophoresis (Figure 1), which corresponds to the purified fucosylated N-Iinked glycoprotein used as the immunogen, that has been previously identified (Rye and Walker, 1989).…”

Alterations in the Serum Glycome Due to Metastatic Prostate Cancer

“…The alteration in glycosylation has been previously correlated to tumor progression. [11][12][13]21,36 The differences observed in our work among the high-mannose, complex biantennary, complex triantennary (fucosylated and nonfucosylated), and complex tretraantennary (fucosylated and nonfucosylated) show ANOVA test p-values better than 0.01, indicating there is a less than 1% probability that this difference is due to a chance alone. An increase in the overall fucosylation in the case of the cancer samples, thus, appears statistically significant, as suggested by the ANOVA test p-value of 0.0006.…”

CA15.3, MCA, CAM26, CAM29 Are Members of a Polymorphic Family of Mucin-Like Glycoproteins

“…Aside from the concentration of mucin subsets, the frequency of epitope re petitions may influence the test results. The affinity and access of antibodies to binding sites may be another important factor; aber rant glycosylation of proteins was assumed in breast tumors compared with normal tis sue [13,26]. Our clinical observations on breast cancer patients further supported the theoretical expectations on the variety of mucin tests.…”

Immunohistochemical Distribution of a Breast Cancer‐Associated Glycoprotein

“…We have shown in a wide range of tissues the distribution of the high molecular weight glycoprotein (M r 230 OOOkDa), previously identified by us as tumour-associated (Rye and Walker, 1989). Our findings indicate that the expression of this glycoprotein, as detected by the polyclonal antiserum P5252-2, is clearly specific to epithelial cells.…”

“…The antiserum was specific for epithelial cells and showed no reactivity with plasma cells, stromal tissue or other non-epithelial cells. Immunoblotting with P5252-2 identified a broad band of apparent M r 230 OOOkDa on SDS discontinuous polyacrylamide gel electrophoresis (Figure 1), which corresponds to the purified fucosylated N-Iinked glycoprotein used as the immunogen, that has been previously identified (Rye and Walker, 1989).…”

Alterations in the Serum Glycome Due to Metastatic Prostate Cancer

“…The alteration in glycosylation has been previously correlated to tumor progression. [11][12][13]21,36 The differences observed in our work among the high-mannose, complex biantennary, complex triantennary (fucosylated and nonfucosylated), and complex tretraantennary (fucosylated and nonfucosylated) show ANOVA test p-values better than 0.01, indicating there is a less than 1% probability that this difference is due to a chance alone. An increase in the overall fucosylation in the case of the cancer samples, thus, appears statistically significant, as suggested by the ANOVA test p-value of 0.0006.…”