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PubMed2001

Cationic ferritin changes outflow facility in human eyes whereas anionic ferritin does not.

PURPOSE: To determine the effect of charged moieties within the outflow pathway on aqueous outflow facility in human eyes. METHODS: After baseline facility measurement in human eye bank eyes (n = 10 pairs), one eye of each pair received anterior chamber exchange and continued perfusion with medium containing 10 mg/ml cationic ferritin. Contralateral eyes were treated in a similar manner with anionic ferritin (10.0 or 102 mg/ml). Eyes were fixed by anterior chamber exchange and perfusion with universal fixative at 8 mm Hg (corresponding to a physiologic pressure of 15 mm Hg in vivo) and examined by transmission electron microscopy. In a second series of human eyes (n = 8 pairs), facility was measured before and after anterior chamber exchange, with a solution containing 0.1 U/ml neuraminidase. RESULTS: Perfusion of eyes with anionic ferritin at either 10.0 or 102 mg/ml caused a negligible 2% increase in facility, whereas cationic ferritin perfusion reduced facility by 66% (P < 0.00001). Perfusion with fixative reduced facility by approximately 60% in both cationic and anionic ferritin-perfused eyes, relative to facilities after perfusion with ferritin. Transmission electron microscopy showed that the distribution of ferritin was segmentally variable. Cationic ferritin consistently labeled the luminal surface of the inner wall of Schlemm's canal, and variably labeled the juxtacanalicular connective tissue (JCT) and trabecular beam surfaces. Anionic ferritin was more prominent in the JCT and intertrabecular spaces and less so on the luminal surface of Schlemm's canal. By scanning electron microscopy, cationic ferritin was seen to accumulate at intercellular margins of the inner wall. Neuraminidase perfusion had no significant effect on outflow facility. CONCLUSIONS: Cationic ferritin reduces outflow facility, presumably by binding to negatively charged sites in the outflow pathway. A possible mechanism is partial or complete blockage of intercellular clefts in the inner wall of Schlemm's canal by the ferritin that accumulates on the luminal surface of the inner wall. Although they are possible targets for ferritin binding, sialyl residues themselves seem to have little direct effect on outflow facility. Our data indicate that positively charged molecules, especially if they can interact with inner wall pores, have the potential to markedly alter outflow facility.

Adult↗
PubMed1990

Examination of serum ferritin and erythrocyte ferritin--its role in the blood transfusion service.

Blood donors were examined for serum ferritin values and concentration of ferritin in the erythrocytes. The group of male and female donors without previous donations showed average values of 102.27 ng and 51.75 ng of ferritin per one ml of serum, respectively. Males with over 20 donations had 68.04 ng ferritin per one ml, females 37.14 ng of ferritin per one ml. The reduced serum ferritin values in multiple male and female donors is statistically significant. Serum ferritin values in women of the two groups are lower than those of males, the difference also being statistically significant. In male and female blood donors, irrespective of the number of donations, average values of 13.74 ag and 12.07 ag of ferritin per erythrocyte, respectively, were established. The difference in ferritin concentration in the erythrocytes between males and females is statistically insignificant. The correlation coefficient failed to demonstrate any dependence between erythrocyte ferritin concentration and concentration of ferritin in the serum. The object of serum ferritin determination in blood donors is to detect the earliest stage of storage iron deficiency in the organism. For the latter purpose, the determination of erythrocyte ferritin is ineffective.

Blood Donors↗
PubMed1978

An enzyme-linked immunoassay for ferritin in human serum and rat plasma and the influence of the iron in serum ferritin on serum iron measurement, during acute hepatitis.

To measure human serum ferritin and rat plasma ferritin a non-competitive enzyme-linked immunoassay has been developed using horseradish peroxidase as the enzyme. In this assay it proved necessary to use heated rat plasma to obtain reproducible ferritin values. The heating procedure caused a loss of 38% of the plasma ferritin. Rat plasma ferritin values have been corrected for this loss. The standard deviation, from duplicate normal human and rat samples is 10 ng ferritin/ml serum and 69 ng/ml plasma, respectively. (The mean ferritin concentrations are: in human sera, 82 ng/ml and in rat plasma 762 ng/ml.) Mean recovery of added liver ferritin in the human serum is 104% +/- 4% (+/-S.E.M') and in the rat plasma 101% +/- 3% (+/- S.E.M.). Normal ferritin concentrations varied in the human material between 30 ng/ml and 300 ng/ml serum, and in the rat plasma between 500 ng/ml and 1300 ng/ml. During increased body iron and acute hepatitis the ferritin concentrations, in patients as well as in rats, exceeded the upper limit of the normal values in most cases. During human hepatitis high serum ferritin levels combined with high serum iron levels were measured. The high serum iron concentrations could not be explained by the high serum ferritin concentrations, even if the iron content of the ferritin is supposed to be high.

Acute Disease↗
PubMed2000

Effect of altered thyroid hormone status on rat brain ferritin H and ferritin L mRNA during postnatal development.

The iron binding protein ferritin is a heterogeneous mix of 24 heavy (H) and light (L) subunits. The H subunit is associated with iron utilization, while the L subunit is responsible for iron storage. Examination of the developmental pattern of mRNA abundance in rat brain revealed that ferritin L mRNA is highest at birth and declines during the first postnatal week. A similar decline was seen in ferritin H mRNA, but was followed by an increase in ferritin H mRNA in the second postnatal week which continued through postnatal day 21. The pattern of H mRNA regulation is similar to that in previous reports of total ferritin protein in the developing rat brain and is consistent with the fact that brain ferritin is predominately ferritin H. The effect of thyroid hormone on the developmental regulation of ferritin mRNAs was examined by the subcutaneous injection of a single dose of exogenous thyroxine (T(4); 2 microg/g) on postnatal day 1. Hypothyroidism was induced in pregnant dams with propylthiouracil (PTU; 0.05% in drinking water) from gestational day 7. Northern analysis from postnatal days 2-21 showed that T(4) increased ferritin H mRNA throughout development, while ferritin L mRNA was decreased compared to age-matched controls. PTU treatment decreased ferritin H and increased L mRNA in the later stages (days 14-21) of development. Given the distinct functions of ferritin H and L this suggests a role for thyroid hormone in the ability of the brain to regulate stored vs. utilizable iron during critical periods of development.

Animals↗
PubMed1990

Ascorbic acid deficiency affects the metabolism of cytosolic ferritin but not lipid-associated ferritin in livers of guinea pigs.

Two physicochemically and metabolically separate pools of ferritin, namely cytosolic ferritin and lipid-associated ferritin, are present in the livers of guinea pigs. In this paper we establish that the iron content of cytosolic ferritin is dependent on and linearly related to ascorbic acid concentration, whereas changes in concentration of this vitamin do not affect the iron content of lipid-associated ferritin. In livers of ascorbic acid-deficient guinea pigs both synthesis and degradation of cytosolic ferritin are diminished equally. Consequently cytosolic ferritin is metabolized more slowly without changes in its pool size. In contrast with cytosolic ferritin, the metabolism of lipid-associated ferritin is unaffected by ascorbic acid deficiency. The differential effects of ascorbic acid deficiency on the physicochemical characteristics as well as on the metabolism of cytosolic ferritin and lipid-associated ferritin suggest that the two forms of ferritin have different functional roles.

Animals↗
PubMed1987

Ferritin: isolation of aluminum-ferritin complex from brain.

Ferritin was isolated from the livers and brains of two groups of rats, one of which was fed aluminum chloride (100 microM) for 1 year in the drinking water. Brain tissue contained about one-third of the amount of ferritin found in the liver. While brain ferritin from normal rats contained 42.1 +/- 14.3 mol of aluminum, that from the aluminum-fed group contained 115.4 +/- 48.3 mol of aluminum per mol of ferritin. Liver ferritin from both groups contained similar amounts of both aluminum and iron, and the amounts were less than that found associated with brain ferritin. Ferritin isolated from the brains of patients who died of Alzheimer disease contained more aluminum and more iron than that from age-matched controls. Human brain ferritin is composed of two types of subunits--about 70% heavy chain (Mr, 22,000) and 30% light chain (Mr, 19,500). The isoelectric focusing pattern of human brain ferritin was considerably different from that of human liver. Only 5 of the 20 brain ferritin bands migrated similarly to the acidic isoferritins from the liver, and the major component of brain ferritin, representing 30% of the total ferritin, had a pI of 8.0.

Administration, Oral↗
PubMed1985

Use of a monoclonal antibody against human heart ferritin for evaluating acidic ferritin concentration in human serum.

Immunoassays for acidic ferritins rich in H subunits have shown that these isoferritins are predominant in some cells such as monocytes and red blood cells but have provided conflicting results about their presence in human serum. We have used an immunoradiometric assay based on a monoclonal antibody against human heart ferritin (monoclonal 2A4) for evaluating acidic ferritin concentration in human serum. This assay proved to be highly specific for acidic isoferritins having more than 60% H subunits. Heart-type ferritin was detected in only one fifth of normal sera and sera from patients with iron overload; values were very low compared with those for basic ferritin. Acidic ferritin was found in relatively high concentrations in most patients with iron deficiency anaemia. In other disease states characterized by increased serum concentrations of basic ferritin, acidic ferritin was always less than 21% of the total ferritin. Dialysis in low-ionic-strength buffer showed that both normal and pathological sera had binding factors for human heart ferritin. We conclude that: (i) human serum contains low concentrations of acidic isoferritins which, at variance with basic ferritin, do not appear to be directly related to the amount of storage iron; (ii) the findings of the present study reinforce the opinion that basic and acidic ferritins have different functional behaviours.

Anemia, Hypochromic↗
PubMed1999

Reference values for a homogeneous Ferritin assay and traceability to the 3rd International Recombinant Standard for Ferritin (NIBSC code 94/572).

Reference values for two ferritin assays (Tina-quanta Ferritin, Enzymun, both Roche Diagnostics, Mannheim, Germany) were established (136 males and 139 females). To rule out inflammation as well as iron deficiency in the reference population, subjects with the C-reactive protein concentration < 5 mg/l, and zinc protoporphyrin < 40 micromol/mol heme and the soluble transferrin receptor < 3 mg/l were selected. Taking into account latent iron deficiency as well as hereditary hemochromatosis the 5-95 percentile range was as follows: male, 27-365 microg/l; female, 13-148 microg/l for Tina-quanta and 12-151 microg/l for Enzymun. The Tina-quanta Ferritin assay showed a very good correlation (r > or = 0.990) to Enzymun ferritin, Ferritin Abbott (Abbott Diagnostics, Delkenheim, Germany), N Latex Ferritin (Dade Behring, Marburg, Germany) and the Ferritin Chiron (Chiron Diagnostics, Fernwald, Germany). However, the slopes of the standard principal component method analysis were calculated to be between 1.03 (Enzymun) and 1.41 (N Latex Ferritin). For four assays the median recovery of the 3rd International Recombinant Ferritin Standard (NIBSC 94/572) measured by serial dilution was 89-109%. The N Latex Ferritin assay recovered half of the target values. Because of the good correlation with other assays, a matrix effect is likely. The question arises whether the manufacturers' agreement on the recombinant ferritin standard would harmonize ferritin measurement.

Adult↗
PubMed2002

Reference values for a heterogeneous ferritin assay and traceability to the 3rd International Recombinant Standard for Ferritin (NIBSC code 94/572).

Reference values for Ferritin Flex on the Dimension RxL analyzer calibrated against the 3rd International Standard for Ferritin (recombinant) and N-Latex Ferritin on the BNA II nephelometer calibrated against the 2nd International Standard for Ferritin (spleen) both from Dade Behring (Marburg, Germany) were established (77 men and 182 women). Exclusion criteria were iron deficiency or iron deficiency anemia, inflammation, liver disease, malignancy, and other hematological or chronic disorders. The reference values (5.0th-95th percentiles) were as follow: for N-Latex Ferritin - men, 12-399 microg/l; women <50 years, 11-102 microg/l and women > or =50 years, 17-219 microg/l; for Ferritin Flex - men, 14-415 microg/l; women <50 years, 11-111 microg/l and women > or =50 years, 22-224 microg/l. Both assays correlated very closely with each other (r=0.993). The linearity was acceptable down to 2 microg/l for the Ferritin Flex method, but only down to 15 microg/l for the N-Latex Ferritin assay. The mean recovery of the 3rd International Standard by N-Latex Ferritin and Ferritin Flex was comparable (approximately 80%). We conclude that the new Ferritin Flex assay, which is based on the new 3rd International Standard, should be used for ferritin measurement in the routine medical laboratories in the future.

Adult↗
PubMed1983

[Gynecological cancer and ferritin--a study on the carcinofetoplacental ferritin].

Serum and tissue ferritins were quantitated by a radioimmunoassay kit (SPAC KIT, Daiichi Radioisotope Lab.) and a diagnostic implication of serum ferritins in patients with gynecological diseases was evaluated. In order to investigate the potential use of tumor marker as a feto-placental antigen (protein), ferritin from ovarian cancer was compared with ferritins from normal adult and feto-placental organs. Serum ferritin levels were significantly higher (p less than 0.01) in patients with ovarian adenocarcinoma, Krukenberg's tumor, cervical squamous cell carcinoma and other malignant diseases than in normal women. Among adult organs the kidney and spleen showed the highest and the heart the lowest ferritin content. The ferritin contents of the kidney and spleen were 78.4 micrograms and 76.2 micrograms/g wet weight, respectively and that of the heart was 5.7 micrograms/g wet weight. The ferritin contents of other adult organs ranged from 10 to 25 micrograms/g wet weight. On the other hand the placenta showed the highest and the heart and stomach the lowest ferritin content among feto-placental organs. The ferritin content of the placenta was 7 micrograms/g wet weight. The ferritin contents of other fetal organs were only half as in the placenta. The ferritin contents of ovarian cancers ranged 6 to 8 micrograms/g wet weight and was almost identical to that of the placenta.

Adenocarcinoma↗
PubMed1989

Crosslinks between intramolecular pairs of ferritin subunits: effects on both H and L subunits and on immunoreactivity of sheep spleen ferritin.

Ferritin is a multisubunit protein, controlling iron storage, with a protein coat composed of 24 subunits (up to three distinct types) in different proportions depending on cell type. Little is known about the subunit interactions in ferritin protein coats composed of heterologous subunits, despite the relevance to ferritin structure and ferritin function (iron uptake and release). Synthetic crosslinking is a convenient way to probe subunit contacts. Crosslinks between subunit pairs in ferritin protein coats are also a natural post-translational modification which coincides with different iron content in ferritin from sheep spleen; ferritin from sheep spleen also contains H and L subunits. Crosslinks synthesized by the reaction of ferritin low in natural crosslinks with difluorodinitrobenzene (F2DNB) reproduced the effects of the natural crosslinks on iron uptake and release. We now extend our observations on the structural effects of natural and synthetic crosslinks to include immunoreactivity of the assembled protein, with monoclonal antibodies as a probe. We also demonstrate, for the first time, ferritin peptides involved in an apparent H- and L-subunit contact: two peptides decreased 4X in cyanogen bromide peptide maps after F2DNB crosslinking were residues L-96-138 and H-66-96; the major DNP-dipeptide was Lys-DNP-Lys. Using the structure of an all L-subunit ferritin as a model, the most likely site for the H-L DNP crosslink is L-Lys 104 (C helix) and H-Lys 67 (B helix). The B helix forms the internal subunit dimer interface, a putative site of iron core nucleation. Alteration by crosslinks of the B helix could, therefore, explain the effect of crosslinks on ferritin iron uptake, release, and iron content.

Amino Acid Sequence↗
PubMed1992

Ferritin mRNAs on rat liver membrane-bound polysomes synthesize ferritin that does not translocate across membranes.

Ferritin is a typical intracellular protein but small amounts are also present in serum and other biological fluids. The source and physiological significance of serum ferritin are still obscure. The presence of ferritin mRNAs on polysomes bound to endoplasmic reticulum (ER) could be relevant for the secretion of ferritin. By Northern blot analysis we found significant amounts of both L and H subunit mRNAs on rat liver membrane-bound polysomes. Immunoprecipitation of translational products of membrane-bound polysomes with anti-rat liver ferritin antibody showed that ferritin is actually synthesized on ER membranes. Analysis of RNA extracted from salt-washed rat liver microsomes demonstrated that ferritin mRNAs are translated by polysomes tightly bound to ER membranes. Following iron treatment, both the amount of H and L subunit mRNAs and ferritin synthesis increased sharply in both free and bound polysomal fractions. Translation of membrane-bound polysomes in the presence of microsomal membranes indicated that ferritin is not processed by signal sequence cleavage or glycosylation and is not translocated into ER membranes. Ferritin mRNAs found on membrane-bound polysomes are associated with ER in a specific way, however, their products do not seem to follow the classic secretory pathway and therefore the significance of the large amount of ferritin mRNAs in the bound ribosome fraction remains unclear.

Animals↗
PubMedDate not supplied

Ferritin: the role of aluminum in ferritin function.

We previously showed that human brain ferritin (HBF) binds aluminum (Al) in vivo and in vitro and HBF isolated from Alzheimer's brain had more Al bound compared to aged matched controls (7). To further understand the role ferritin may play in Al neurotoxicity, we have studied in vitro the effect of Al on the function of human ferritin isolated from Alzheimer's (AD) and normal brain tissue, and compared the results with other mammalian ferritins. Al causes a concentration-dependent decrease in the initial rate of iron loading into apo-horse spleen and human brain ferritin and the rates were similar for ferritin isolated from both AD and normal brains. The rates of iron release of mammalian ferritins from different tissues were determined: horse spleen much greater than human liver greater than rat brain greater than human brain = rat liver ferritin. The rates of iron release of AD and normal human brain ferritin were similar and were unaffected by preloading with Al. Several mammalian ferritins were compared for their total iron uptake: horse spleen = human liver greater than human brain (normal) = human brain (AD) ferritin. In 20 mM HEPES (pH 6.0) buffer holoferritin is more resistant to precipitation by Al than apoferritin suggesting that holoferritin is a better chelator for nonferrous metal ions.

Aluminum↗
PubMed2003

Anthracyclines induce accumulation of iron in ferritin in myocardial and neoplastic cells: inhibition of the ferritin iron mobilization pathway.

Anthracyclines are potent antitumor agents that cause cardiotoxicity at high cumulative doses. Because anthracycline cardiotoxicity is attributed to their ability to avidly bind iron (Fe), we examined the effect of anthracyclines on intracellular Fe trafficking in neoplastic cells and differentiated cardiomyocytes. In both cell types, incubation with doxorubicin (DOX) resulted in a significant (p < 0.004) accumulation of Fe in the storage protein, ferritin. Pulse-chase experiments using control cells demonstrated that within 6 h, the majority of (59)Fe donated from transferrin was incorporated into ferritin. Over longer incubation periods up to 18 to 24 h, (59)Fe was subsequently mobilized from ferritin into other compartments in control cells. However, anthracyclines inhibited ferritin-(59)Fe redistribution during the 18- to 24-h period, resulting in a significant (p < 0.0003) 3- to 5-fold accumulation of ferritin-(59)Fe compared with control cells. The increase in ferritin-(59)Fe after a 24-h incubation with DOX could not be correlated with increased ferritin expression, suggesting that (59)Fe accumulation occurred in pre-existing ferritin. In addition to DOX, other redox-cycling agents (i.e., menadione and paraquat) also increased ferritin-(59)Fe levels. Moreover, the intracellular superoxide scavenger, Mn(III) tetrakis(4-benzoic acid)-porphyrin complex, partially prevented the ability of DOX and menadione at inducing this effect. Hence, superoxide generation by these compounds could play a role in causing ferritin-(59)Fe accumulation. This study is the first to demonstrate the effect of anthracyclines at inhibiting Fe mobilization from ferritin, resulting in marked Fe accumulation within the molecule. This response may have consequences in terms of the cytotoxic effects of anthracyclines.

Anthracyclines↗
PubMed2005

Erythrocyte ferritin concentration: analytical performance of the immunoenzymatic IMx-Ferritin (Abbott) assay.

Together with serum ferritin, erythrocyte ferritincan be a valuable diagnostic tool for evaluating the degree of impaired iron metabolism in different diseases. We collected peripheral blood samples from 64 subjects (22 healthy volunteers, 20 patients with hereditary hemochromatosis, and 22 patients on regular hemodialysis with secondary anemia) to evaluate whether an immunoenzymatic method generally used for serum ferritin can also be used to determine erythrocyte ferritin levels under various conditions of body iron status. Serum and erythrocyte ferritin levels were assayed in parallel using a microparticle enzyme immunoassay (MEIA) IMx-Ferritin kit and an IMx analyzer. The inter-assay imprecision of the serum and erythrocyte ferritin assays was 4.9% and 5.05%, the intra-assay imprecision was 2.2% and 2.3%, and the mean recovery was 102% (range 96-105%) and 101% (range 99-105%), respectively. Both serum and erythrocyte ferritin assays showed a detection limit of 1 microg/L and good linearity (R(2) = 0.99) in the intervals 13.9-443 and 3.9-135.6 microg/L, respectively. Our findings demonstrate that the IMx-Ferritin assay currently used to measure serum ferritin levels can also be adopted to measure erythrocyte ferritin insofar as it clearly discriminates high and low erythrocyte ferritin levels in cases of both iron overload and deficiency.

Adult↗
PubMed2003

The effect of UVB irradiation on ferritin subunit synthesis, ferritin assembly and Fe metabolism in cultured canine lens epithelial cells.

Ferritin is a multimeric protein consisting of heavy and light chains assembled in different tissue-specific ratios, which can protect cells from oxidative stress by storing reactive iron (Fe). Because the lens is constantly exposed to UV irradiation, we studied its effects on ferritin synthesis and Fe metabolism in cultured lens epithelial cells with and without ascorbic acid (Asc). UVB caused a large increase in accumulation of newly synthesized ferritin chains; this increase was additive to that induced by Asc. In contrast to the Asc-induced increase in Fe storage, Fe storage in ferritin was unaltered by UVB. Although UVB increased accumulation of newly synthesized ferritin chains, total ferritin levels were unaltered. In contrast, Asc, which induced a quantitatively similar increase in accumulation of newly synthesized ferritin chains, doubled the total amount of ferritin. Because UVB did not change Fe storage in ferritin or the size of the labile Fe pool, it was hypothesized and then determined that these newly synthesized chains did not assemble into functional holoferritin. Numerous studies detail the effects of various treatments on de novo ferritin synthesis; however, this study provides a cautionary note regarding the conclusions of such studies in the absence of data indicating assembly of functional ferritin molecules.

Animals↗
PubMed2003

High ferritin and low glycosylated ferritin may also be a marker of excessive macrophage activation.

OBJECTIVE: A high serum ferritin concentration with a low percentage of glycosylated ferritin (< 20%) have been reported to be a specific marker of active adult Still's disease (ASD). However, high ferritin levels are found during hemophagocytosis syndrome (HS). We investigated the ferritin level and the percentage of glycosylation in a HS series of various causes. METHODS: Diagnosis of HS was confirmed by erythrophagocytosis pictures on a bone marrow cytology or biopsy in all patients. Serum ferritin concentration was determined on a heterogenous immunoassay module. Glycosylated ferritin was separated using concanavalin A (Con-A) sepharose 4B chromatography. The nonglycosylated ferritin unbound to Con-A was recovered in the supernatant and quantified with the same procedure. Percentages of glycosylated ferritin less than 20% are considered to be usual in ASD, between 20 and 40% usual in inflammatory syndrome, and between 50 and 80% normal. RESULTS: In all cases tested during the acute phase of the disease, ferritin blood level was high and the percentage of glycosylated ferritin was low, less than 20%. CONCLUSION: The combination of high ferritin level and low percentage of glycosylation may be a marker of excessive macrophage activation.

Adult↗
PubMed1980

Serum ferritin in patients with cancer: determination with antibodies to HeLa cell and spleen ferritin.

Some malignant tissues and cell lines contain acidic isoferritins and it has been suggested that the assay of such isoferritins in serum may be of value in the diagnosis of malignancy. This paper describes a radioimmunoassay for acidic ferrtin purified from HeLa cells. Examiniation of purified heart, kidney, liver and spleen ferritin showed that the assay was highly specific for acidic isoferritins. Ferritin concentrations have been measured with antibodies to HeLa cell and spleen ferritin in extracts of normal and tumour tissue. Although the tumours contained more HeLa type ferritin than the corresponding normal tissue the HeLa/spleen type ferritin ratio was low. HeLa-type ferritin concentrations have been compared with values obtained with anti-spleen ferritin in over 1000 sera from normal subjects and patients with cancer and leukaemia. HeLa-type ferritin as not detected ( less than 2 micrograms/l) in most normal sera. Concentrations of up to 53 micrograms/l were found in sera from patients with malignant disease but the HeLa/spleen type ferritin ratio was always very low. There appears to be little application for antibodies to HeLa cell or heart ferritin in the diagnosis or monitoring of cancer.

Breast Neoplasms↗