lactoferrin and Breast-Diseases

Breast amyloidosis is a rare condition which is mostly associated with hematological disorders or hereditary genetic disorders. Imaging findings of breast amyloidosis can mimic malignancy, which often leads to biopsy or excision of the lesion. Here, we presented a case of localized lactotransferrin-related breast amyloidosis in an elderly female patient. Histologic examination revealed extensive involvement of breast lobules by amorphous amyloid materials, with attenuation of lobular structures and prominent calcifications. Positive immunostains for myoepithelial cells helped to exclude the possibility of invasive carcinoma. The patient had no hematologic malignancy besides immunoglobulin G lambda monoclonal gammopathy of undetermined significance. Mass spectrometry of the breast amyloid identified lactotransferrin and no immunoglobulin or its light chain. On follow-up, the patient showed no recurrence of the breast lesion after local excision nor showed other systematic comorbidities, indicating the benign nature of the lesion. This first report of lactotransferrin-related amyloidosis may represent a special type of localized breast amyloidosis that has no correlation with systematic disorders.

Topics: Amyloidosis; Biomarkers; Breast Diseases; Diagnosis, Differential; Female; Humans; Lactoferrin; Middle Aged

Topics: Adult; Body Mass Index; Breast Diseases; Breast Feeding; Calcium; Candidiasis; Female; Humans; Infant; Infant, Newborn; Lactoferrin; Male; Mastitis; Milk, Human; Mothers; Neuropeptides; Plasma; Postpartum Period; Prospective Studies; Surveys and Questionnaires; Sweden; Young Adult

Breast duct epithelium produces, secretes, and metabolises several biologically important compounds, which are found in breast secretions obtained in physiologic and pathologic conditions (milk and nipple aspirate fluids, respectively). In order to preliminarily evaluate the ultrastructural morphology of the cells found in Type II nipple aspirate fluids (NAF) and correlate it with the biochemical profile of the extracellular fluid present in these breast secretions and in human milk, we analyzed 72 NAFs from nonlactating premenopausal women affected by various breast diseases and 10 normal milk samples. Although several constitutive proteins were detected in all samples examined, the preliminary biochemical analyses and electrophoretic profiles revealed characteristic behaviours for several biologic constituents, suggesting a possible basic mechanism of production by breast epithelial cells during both physiologic and pathologic conditions. The ultrastructural analysis of milk cellular components give preliminary evidence of the apocrine secretion mechanism peculiar of breast gland, whereas Type II NAF cells appeared as biosynthetically active cells, showing a possible modified secretion mechanism. Our multidisciplinary approach seems to support the hypothesis that cellular and biochemical behaviour of Type II NAF may be an useful tool to identify aberrated breast epithelial cells in nonlactating women that might be prone to premalignant transformation.

Topics: Body Fluids; Breast; Breast Diseases; Cytoplasm; Cytoplasmic Granules; Electrophoresis, Polyacrylamide Gel; Endoplasmic Reticulum, Rough; Endoplasmic Reticulum, Smooth; Epithelial Cells; Female; Humans; Lactoferrin; Microscopy, Electron; Milk, Human; Molecular Weight; Suction

The protein composition of breast secretions from 99 premenopausal women with benign or malignant breast diseases and from 70 control women without breast pathologies has been studied by using polyacrylamide gel electrophoresis. These fluids have been classified into two types according to their major polypeptide components. Type I fluids are defined by three major distinctive bands at Mr 44,000, 24,000, and 17,000, while those designated Type II present distinctive bands at Mr 80,000, 15,000, and 14,000. Amino acid sequencing and immunoblotting analysis demonstrated that proteins in Type I secretions correspond to Zn-alpha 2-glycoprotein, apolipoprotein D, and gross cystic disease fluid protein-15, while those from Type II fluids have been identified as lactoferrin, lysozyme, and alpha-lactalbumin. Most women (93%) without breast pathology and most patients (88%) with benign diseases had secretions with a Type I polypeptide pattern. By contrast, a large percentage (57%) of secretions from women with breast carcinoma presented a Type II protein pattern. Further studies with a large number of women will be useful for corroborating the potential clinical interest of breast fluid protein analysis.

Topics: Adult; Amino Acid Sequence; Apolipoproteins; Apolipoproteins D; Breast; Breast Diseases; Carrier Proteins; Electrophoresis, Polyacrylamide Gel; Female; Glycoproteins; Humans; Lactalbumin; Lactoferrin; Membrane Transport Proteins; Middle Aged; Molecular Sequence Data; Molecular Weight; Muramidase; Seminal Plasma Proteins; Zn-Alpha-2-Glycoprotein

Topics: Antibodies, Monoclonal; Antigens, Neoplasm; Antigens, Tumor-Associated, Carbohydrate; Biomarkers, Tumor; Breast; Breast Diseases; Breast Neoplasms; Cell Transformation, Neoplastic; Epitopes; Female; Humans; Immunoenzyme Techniques; Keratins; Lactoferrin; Membrane Glycoproteins; Mucin-1; Neoplasm Invasiveness; Neoplasm Metastasis; Precancerous Conditions

An immunoperoxidase staining technique was used for detecting three major iron binding proteins (ferritin, transferrin and lactoferrin) in 40 breast carcinoma cases and six benign breast proliferative lesions. Ferritin staining was detected mainly in connectival stroma and in histiocytes surrounding neoplastic cells. Few and faint ferritin positivities were also detected in neoplastic cells of 20 carcinoma cases. Transferrin was found inconsistently in myoepithelial cells surrounding normal ductules, or around neoplastic ducts of ductal in situ carcinoma. In eight carcinoma cases, transferrin staining was also positive in neoplastic cells. Lactoferrin was detected only in normal breast epithelial cells and in benign breast proliferative lesions. These immunohistochemical findings may suggest that raised serum ferritin concentrations in breast carcinoma patients might be attributed to stromal reaction rather than to tumour synthesis. Transferrin staining of neoplastic cells in these carcinoma cases appears to be very intriguing, particularly since transferrin is considered an obligate requirement for growing cells, and transferrin receptors have been demonstrated only in dividing cells. On the basis of the immunohistochemical data, lactoferrin might be used as a pointer to benign lesions.

Topics: Adenocarcinoma, Mucinous; Breast; Breast Diseases; Breast Neoplasms; Carcinoma; Carcinoma in Situ; Carcinoma, Intraductal, Noninfiltrating; Female; Ferritins; Humans; Immunoenzyme Techniques; Lactoferrin; Lactoglobulins; Transferrin

Milk protein concentrations were determined either by double antibody radioimmunoassay (IgA and IgG) or single radial immunodiffusion (lactoferrin) in the mammary secretions of seven healthy non-lactating subjects and eight patients with breast disease. IgA and IgG were detected in all samples of breast secretion (whether from normal or diseased breasts) and the concentrations observed were very similar to those in post-partum colostrum and milk. However, because the volume of secretion obtained was very small compared with colostrum and milk, total IgA synthesis by the non-lactating breast is very much less than in the lactating breast. The IgA detected in the mammary secretions was demonstrated to be secretory IgA by gel filtration and it is therefore suggested that the secretory immune system is functional in the non-lactating breast.

Topics: Adult; Breast; Breast Diseases; Chromatography, Gel; Female; Humans; Immunoglobulin A; Immunoglobulin G; Lactation; Lactoferrin; Middle Aged; Milk Proteins; Pregnancy; Radioimmunoassay

Topics: Breast Diseases; Breast Neoplasms; Carcinoembryonic Antigen; Cell Differentiation; Female; Humans; Immunoenzyme Techniques; Lactoferrin; Lactoglobulins; Phyllodes Tumor

The synthesis of several proteins in human mammary carcinomas and in dysplastic breast tissues was studied by tissue culture and by immunofluorescence. The synthesis of immunoglobulins showed marked quantitative and qualitative variations from one specimen to another, and a preferential synthesis of immunoglobulin G and C'3 in the carcinomas with lymphocytic infiltration. Fixation of immunoglobulins G and M on the surface of neoplastic cells was noted in some carcinomas. Secretory component was detectable in some cases by immunofluorescence, but no synthesis could be found in vitro, presumably because of unfavorable culture conditions. The synthesis of lactoferrin, casein, and some serum alpha- and beta-globulins was significantly greater in noncancerous tissues than in carcinomas. Synthesis of lactoferrin was also more frequent in the well differentiated carcinomas than in the poorly differentiated carcinomas. The tissue culture technique used in this study, although in need of better adaptation to the requirements in vitro of human mammary tissues, proved to be a useful tool for investigating the synthesis of several protein components by the epithelial cells of cancerous and dysplastic tissues of the human breast. Whether a preferential synthesis of 1 class of immunoglobulins or of other proteins might influence the evolution of a mammary lesion could not be determined in this material but it should be studied further.

Topics: Alpha-Globulins; Amino Acids; Beta-Globulins; Breast Diseases; Breast Neoplasms; Caseins; Culture Techniques; Female; Humans; Immunoglobulin A; Immunoglobulin D; Immunoglobulin G; Immunoglobulin M; Immunoglobulins; Lactoferrin; Milk Proteins; Neoplasm Proteins; Receptors, Antigen, B-Cell