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

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.

[1]  H. Nick,et al.  Protein-synthesis-dependent induction of annexin I by glucocorticoid. , 1991, The Biochemical journal.

[2]  C. Reutelingsperger,et al.  Interaction of annexins with membranes: the N-terminus as a governing parameter as revealed with a chimeric annexin. , 1993, Biochemistry.

[3]  G. Nicolson,et al.  Candidate metastasis-associated genes of the rat 13762NF mammary adenocarcinoma , 2004, Breast Cancer Research and Treatment.

[4]  G. Nicolson,et al.  A novel candidate metastasis-associated gene, mta1, differentially expressed in highly metastatic mammary adenocarcinoma cell lines. cDNA cloning, expression, and protein analyses. , 1994, The Journal of biological chemistry.

[5]  J. Glenney,et al.  Antibodies to the N-terminus of calpactin II (p35) affect Ca2+ binding and phosphorylation by the epidermal growth factor receptor in vitro. , 1988, Biochemistry.

[6]  K. Koretz,et al.  Differential expression of annexins I and II in normal and malignant human mammary epithelial cells. , 1993, Differentiation; research in biological diversity.

[7]  H. Nick,et al.  Regulation of annexin I in adipogenesis: cAMP-independent action of methylisobutylxanthine. , 1992, The American journal of physiology.

[8]  S. Violette,et al.  Role of lipocortin I in the glucocorticoid induction of the terminal differentiation of a human squamous carcinoma , 1990, Journal of cellular physiology.

[9]  J. Cavadore,et al.  Protein kinase C-dependent phosphorylation of annexins I and II in mesangial cells. , 1993, Biochemical Journal.

[10]  L. Wachter,et al.  Five distinct calcium and phospholipid binding proteins share homology with lipocortin I. , 1988, The Journal of biological chemistry.

[11]  A. Ullrich,et al.  Annexin I is phosphorylated in the multivesicular body during the processing of the epidermal growth factor receptor , 1993, The Journal of cell biology.

[12]  M. R. Nelson,et al.  Effects of the expression of mammalian annexins in yeast secretory mutants. , 1992, Journal of cell science.

[13]  R. Donato,et al.  Two novel brain proteins, CaBP33 and CaBP37, are calcium‐dependent phospholipid‐ and membrane‐binding proteins , 1990, FEBS letters.

[14]  A. Verkleij,et al.  Morphological and biochemical evidence for partial nuclear localization of annexin 1 in endothelial cells. , 1992, Biochemical and biophysical research communications.

[15]  H. Nick,et al.  Annexin-I regulation in response to suckling and rat mammary cell differentiation. , 1991, Endocrinology.

[16]  M. Geisow,et al.  The annexin family of calcium-binding proteins. Review article. , 1989, Cell calcium.

[17]  J. Ernst,et al.  Annexins possess functionally distinguishable Ca2+ and phospholipid binding domains. , 1994, Biochemical and biophysical research communications.

[18]  M. Crumpton,et al.  Diversity in the lipocortin/calpactin family , 1988, Cell.

[19]  C. Taylor,et al.  A comparative study of the use of monoclonal antibodies using three different immunohistochemical methods: an evaluation of monoclonal and polyclonal antibodies against human prostatic acid phosphatase. , 1982, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[20]  G. Nicolson.  Quantitative variations in gene expression: Possible role in cellular diversification and tumor progression , 1991, Journal of cellular biochemistry.

[21]  C. Creutz,et al.  Phosphorylation of a chromaffin granule-binding protein in stimulated chromaffin cells. , 1986, The Journal of biological chemistry.

[22]  S. Hwang,et al.  Developmental regulation of calcium‐binding proteins (calelectrins and calpactin I) in mammary glands , 1989, Journal of cellular physiology.

[23]  T. Yeatman,et al.  Extracellular annexin VI expression is associated with divalent cation-dependent endothelial cell adhesion of metastatic RAW117 large-cell lymphoma cells. , 1994, Experimental cell research.

[24]  C. Klee,et al.  Ca2+-dependent phospholipid- (and membrane-) binding proteins. , 1988, Biochemistry.

[25]  R. Warnke,et al.  Suppression of endogenous avidin-binding activity in tissues and its relevance to biotin-avidin detection systems. , 1981, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[26]  M. Crumpton,et al.  Protein terminology tangle , 1990, Nature.

[27]  M. Ohnishi,et al.  Involvement of annexin I and annexin II in hepatocyte proliferation: Can annexins I and II be markers for proliferative hepatocytes? , 1994, Hepatology.

[28]  G. Nicolson.  Gene expression, cellular diversification and tumor progression to the metastatic phenotype , 1991, BioEssays : news and reviews in molecular, cellular and developmental biology.

[29]  J. Glenney,et al.  The calpactin light chain is tightly linked to the cytoskeletal form of calpactin I: studies using monoclonal antibodies to calpactin subunits , 1987, The Journal of cell biology.

[30]  T. Yeatman,et al.  Expression of annexins on the surfaces of non-metastatic and metastatic human and rodent tumor cells , 2004, Clinical & Experimental Metastasis.

[31]  T. Yeatman,et al.  Extracellular annexin II is associated with divalent cation‐dependent tumor cell–endothelial cell adhesion of metastatic RAW117 large‐cell lymphoma cells , 1993, Journal of cellular biochemistry.