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Differential expression of annexin I in human mammary ductal epithelial cells in normal and benign and malignant breast tissues

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Abstract

Annexins are a family of structurally related, water-soluble proteins that have calcium- and phospholipid-binding domains. Annexin I is thought to be involved in cell proliferation and differentiation and has recently been shown to be expressed on the surfaces of lymphoma cells where it acts as an endothelial cell adhesion molecule. To evaluate the expression of annexin I in relation to human breast cancer development and progression we used breast biopsy tissues. Immunohistochemical analysis of annexin I in paraffin-embedded ductal epithelial cells of various human breast tissues indicated that this annexin was not demonstrable in the ductal luminal cells of normal breast tissues (n = 11) and benign tumors (n = 10) (except for one ductal adenoma) but was generally expressed in various types of breast cancers, including noninvasive ductal carcinoma in situ (DCIS), invasive and metastatic breast tumors (n = 33). The results suggest that annexin I expression might correlate with malignant breast cancer progression but it is most likely involved at an early stage of human breast cancer development.

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References

  1. Crumpton MJ and Dedman JR, 1990, Protein terminology tangle. Nature, 345, 212.

    Google Scholar 

  2. Crompton MR, Moss SE and Crumpton MJ, 1988, Diversity in the lipocortin/calpactin family. Cell, 55, 1–3.

    Google Scholar 

  3. Pepinsky RB, Tizard R, Mattaliano RJ, et al. 1988, Five distinct calcium and phospholipid binding proteins share homology with lipocortin I. J Biol Chem, 263, 10799–811.

    Google Scholar 

  4. Ernst JD, Mall A and Chew G, 1994, Annexins possess functionally distinguishable Ca2+ and phospholipid binding domains. Biochem BiophysRes Commun, 200, 867–76.

    Google Scholar 

  5. Burgoyne RD and Geisow MJ, 1989, The annexin family of calcium-binding proteins. Cell Calcium, 10, 1–10.

    Google Scholar 

  6. Hoekstra D, Buist-Arkema R, Klappe K and Reutelingsperger CP, 1993, Interaction of annexins with membranes: the N-terminus as a governing parameter as revealed with a chimeric annexin. Biochemistry, 32, 14194–202.

    Google Scholar 

  7. Klee CB, 1988, Calcium dependent phospholipid and membrane binding proteins. Biochemistry, 27, 6645–53.

    Google Scholar 

  8. Futter CE, Felder S, Schlessinger J, Ullrich A and Hopkins CR, 1993, Annexin I is phosphorylated in the multivesicular body during the processing of the epidermal growth factor receptor. J Cell Biol, 120, 77–83.

    Google Scholar 

  9. Oudinet JP, Russomarie F, Cavadore JC and Rothhut B, 1993, Protein kinase C-dependent phosphorylation of annexins I and II in mesangeal cells. Biochem J, 292, 63–8.

    Google Scholar 

  10. Michener ML, Dawson WB and Creutz CE, 1986, Phosphorylation of a chromaffin granule-binding protein in stimulated chromaffin cells. J Biol Chem, 261, 6548–55.

    Google Scholar 

  11. Masaki T, Tokuda M, Fujimura T, et al. 1994, Involvement of annexin I and annexin II in hepatocyte proliferation: can annexins I and II be markers for proliferative hepatocytes? Hepatology, 20, 425–35.

    Google Scholar 

  12. Wong WT, Nick HS and Forst SC, 1992, Regulation of annexin I in adipogenesis: cAMP-independent action of methylisobutylxanthine. Am J Physiol, 262, 91–7.

    Google Scholar 

  13. Lozano JJ, Siberstein GB, Hwang SI, Haindl AH and Rocha V, 1989, Developmental regulation of calcium binding proteins (calelectrins and calpactin I) in mammary gland. J Cell Physiol, 138, 503–10.

    Google Scholar 

  14. Horlick KR, Ganjianpour M, Frost SC and Nick HS, 1991, Annexin I regulation in response to suckling and rat mammary cell differentiation. Endocrinology, 128, 1574–9.

    Google Scholar 

  15. Creutz CE, Kambouris NG, Snyder SL, et al. 1992, Effects of the expression of mammalian annexins in yeast secretory mutants. J Cell Sci, 103, 1177–92.

    Google Scholar 

  16. Raynal P, Van Bergen en Henegouwen PMP, Hullin F, et al. 1992, Morphological and biochemical evidence for partial nuclear localization of annexin I in endothelial cells. Biochem Biophys Res Commun, 186, 432–9.

    Google Scholar 

  17. Naritoku WY and Taylor CR, 1988, A comparative study of the use of monoclonal antibodies using three different immunohistochemical methods. J Histochem Cytochem, 30, 253–60.

    Google Scholar 

  18. Zokas L and Glenney Jr JR, 1987, The calpactin light chain is tightly linked to the cytoskeleton form of calpactin I; studies using monoclonal antibodies to calpactin subunits. J Cell Biol, 105, 2111–20.

    Google Scholar 

  19. Zokas L, 1988, Antibodies to the N-terminus of calpactin I affect Ca+2 binding and phosphorylation by the epidermal growth factor receptor In vitro. Biochemistry, 27, 2069–76.

    Google Scholar 

  20. Woods GS and Warnke R, 1981, Suppression of endogenous avidin-binding activity in tissues and its relevance to biotin-avidin detection system. J Histochem Cytochem, 29, 1196–204.

    Google Scholar 

  21. Wong WT, Frost SC and Nick HS, 1991, Proteinsynthesis-dependent induction of annexin I by glucocorticoid. Biochem J, 275, 313–9.

    Google Scholar 

  22. Violette SM, King I, Browning JL, Pepinsky RB, Wallner BP and Sartorelli AC, 1990, Role of lipocortin I in the glucocorticoid induction of the terminal differentiation of a human squamous carcinoma. J Cell Physiol, 142, 70–7.

    Google Scholar 

  23. Pencil SD, Toh Y and Nicolson GL, 1993, Candidate metastasis-associated genes of the rat 13762NF mammary adenocarcinoma. Breast Cancer Res Treatm, 25, 165–74.

    Google Scholar 

  24. Toh Y, Pencil SD and Nicolson GL, 1994, A novel candidate metastasis-associated gene mta1differentially expressed in highly metastatic mammary adenocarcinoma cell lines: cDNA cloning, expression and protein analyses. J Biol Chem, 269, 22958–63.

    Google Scholar 

  25. Yeatman TJ, Updyke TV, Kaetzel MA, Dedman JR and Nicolson GL, 1993, Expression of annexins on the surfaces of non-metastatic and metastatic human and rodent tumor cells. Clin Exp Metastasis, 11, 37–44.

    Google Scholar 

  26. Nicolson GL, 1991, Quantitative variations in gene expression: possible role in cellular diversification and tumor progression. J Cell Biochem, 46, 277–83.

    Google Scholar 

  27. Nicolson GL, 1991, Gene expression and tumor progression to the metastatic phenotype. Bioessays, 13, 337–42.

    Google Scholar 

  28. Tressler RJ, Updyke TV, Yeatman TJ and Nicolson GL, 1993, Extracellular annexin II is associated with divalent cation-dependent tumor cell-endothelial cell adhesion of metastatic RAW 117 large-cell lymphoma cells. J Cell Biochem, 53, 265–76.

    Google Scholar 

  29. Tressler RJ, Updyke TV, Yeatman T and Nicolson GL, 1994, Extracellular annexin VI is associated with divalent cation-dependent endothelial cell adhesion of metastatic RAW117 large-cell lymphoma cells. Exp Cell Res, 215, 395–400.

    Google Scholar 

  30. Schwartz-Albiez R, Koretz K, Moller P and Wirl G, 1993, Differential expression of annexins I and II in normal and malignant human mammary epithelial cells. Differentiation, 52, 229–37. 1

    Google Scholar 

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Ahn, SH., Sawada, H., Ro, JY. et al. Differential expression of annexin I in human mammary ductal epithelial cells in normal and benign and malignant breast tissues. Clin Exp Metastasis 15, 151–156 (1997). https://doi.org/10.1023/A:1018452810915

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