Surface markers of human gingival fibroblasts in vitro were investigated using monoclonal and helerologous unlisera against a range of cell surface antigens, together with resetting techniques to characterize surface receptors for IgG and C., WI‐38 fibroblasts and human peripheral blood monocytes were used as control cells. Human gingival fibroblasts exhibited complement receptors and (β2‐micro‐globulin, as did W1–3S cells. Ten per cent of the human gingival fibroblasts were positive for HLA‐DR antigens and additionally exhibited a granulocyte antigen not apparent on WI‐3K cells. Monolayers of the gingival fibroblasts were further exposed for short periods to varying concentrations of enzymes (trypsin, collagenase and neuraminidase), bacterial extracts (lipopolysaccharide and lipoteichoic acid) and crude supra‐ and subgingival plaque sonicates. Surface‐marker analysis was then carried out. The most noticeable effects were obtained with Vibrio cholerae neuraminidase which enhanced C3, receptor and surface antigen expression, and supragingival plaque sonicate which depressed the expression of HLA‐DR and granulocytc antigens while not affecting β2microglobulin expression. Trypsin reduced antigen expression to a degree, but its effects were mainly on cell adherence.
Sialyltransferase (CMP-sialic acid:asialofetuin sialyltransferase) and human mammary epithelial antigens (HME-Ags, cell surface antigens specific to human mammary epithelial cells) were determined in plasma of nude mice grafted with breast and non-breast human tumors to assess their possible usefulness as breast cancer markers. The plasma transferase activity was significantly higher (p less than 0.01) in tumor groups relative to the control. However, no significant difference (p less than 0.05) could be found in the transferase level between breast and non-breast tumor groups, showing the enzyme's lack of specificity for breast cancer. Furthermore, the surgical procedure performed on the control normal healthy group (no tumor), resulted in an important increase of the enzyme level, while HME-Ags remained unchanged. HME-Ags were essentially negative in control as well as non-breast tumor groups. After surgical removal of breast tumors, HME-Ags level dropped drastically to the background level (from 122 to less than 30 ng/ml plasma). These data indicate that HME-Ags are more sensitive and specific than sialyltransferase as markers for human breast tumor, and suggest that HME-Ags may be clinically useful in the early detection of breast cancer as well as in the followup of patients with metastatic breast tumor.
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