The synthesis of a proteinase inhibitor, alpha-1-antichymotrypsin, by human breast epithelial cells

Z. A. Tokes, Sandra J Gendler, G. B. Dermer

Research output: Chapter in Book/Report/Conference proceedingChapter

20 Citations (Scopus)

Abstract

The synthesis and release of glycoproteins were studied in organ cultures of human breast surgical specimens and in established breast epithelial cell lines, MCF-7 and MDA-MB-231. Biosynthesis was monitored by the incorporation of 14C-glucosamine. Labeled macromolecules in the culture supernatants were analyzed by biochemical and immunological techniques. One to 8% of the labeled glycoproteins from benign breast and infiltrating ductal carcinoma specimens was precipitated by antibodies produced against human serum α-1-antichymotrypsin. Twelve percent of the total glycoproteins from the culture supernatants of the MCF-7 cell line was identified as α-1-antichymotrypsin. Both the normal serum and the human breast epithelia-derived proteinase inhibitor can be resolved into similar subclasses by two-dimensional gel electrophoresis. NDA-MB-231 and MCF-7 cells which were extensively washed with EDTA, serum-free medium, and phosphate-buffered saline retain this proteinase inhibitor on their cell surfaces. Three to 4% of the total cell-surface iodinated components was immunoprecipitated by these specific antibodies. Since α-1-antichymotrypsin is a potent inhibitor of neutral proteinases such as cathepsin G, the demonstration of its synthesis by benign and malignant breast epithelial cells is of considerable interest. This glycoprotein may represent the epithelia's own protective shield of cell surface components and the cell's attempt to moderate the effects of invading leukocytes. In addition, it may play a regulatory role in the maintenance of three-dimensional glandular structures.

Original languageEnglish (US)
Title of host publicationJournal of Supramolecular and Cellular Biochemistry
Pages69-77
Number of pages9
Volume17
Edition1
StatePublished - 1981
Externally publishedYes

Fingerprint

alpha 1-Antichymotrypsin
Glycoproteins
Breast
Peptide Hydrolases
Epithelial Cells
MCF-7 Cells
Epithelium
Cathepsin G
Immunologic Techniques
Carcinoma, Ductal, Breast
Cell Line
Antibodies
Organ Culture Techniques
Glucosamine
Biosynthesis
Serum-Free Culture Media
Electrophoresis, Gel, Two-Dimensional
Cellular Structures
Electrophoresis
Serum

ASJC Scopus subject areas

  • Biochemistry

Cite this

Tokes, Z. A., Gendler, S. J., & Dermer, G. B. (1981). The synthesis of a proteinase inhibitor, alpha-1-antichymotrypsin, by human breast epithelial cells. In Journal of Supramolecular and Cellular Biochemistry (1 ed., Vol. 17, pp. 69-77)

The synthesis of a proteinase inhibitor, alpha-1-antichymotrypsin, by human breast epithelial cells. / Tokes, Z. A.; Gendler, Sandra J; Dermer, G. B.

Journal of Supramolecular and Cellular Biochemistry. Vol. 17 1. ed. 1981. p. 69-77.

Research output: Chapter in Book/Report/Conference proceedingChapter

Tokes, ZA, Gendler, SJ & Dermer, GB 1981, The synthesis of a proteinase inhibitor, alpha-1-antichymotrypsin, by human breast epithelial cells. in Journal of Supramolecular and Cellular Biochemistry. 1 edn, vol. 17, pp. 69-77.
Tokes ZA, Gendler SJ, Dermer GB. The synthesis of a proteinase inhibitor, alpha-1-antichymotrypsin, by human breast epithelial cells. In Journal of Supramolecular and Cellular Biochemistry. 1 ed. Vol. 17. 1981. p. 69-77
Tokes, Z. A. ; Gendler, Sandra J ; Dermer, G. B. / The synthesis of a proteinase inhibitor, alpha-1-antichymotrypsin, by human breast epithelial cells. Journal of Supramolecular and Cellular Biochemistry. Vol. 17 1. ed. 1981. pp. 69-77
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