Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Androgenetic alopecia (a.A.) occurs quite frequently. Up to 79% of women suffer at least temporarily from varying degrees of intermittent diffuse hair loss in the centro-parietal and/or fronto-temporal regions. A.A. is caused by an androgen excess acting on the hair follicle for prolonged periods of time in the presence of a genetic predisposition. However, often hyperandrogenemia cannot be demonstrated in such patients. 125 women with clinically typical a.A. were investigated prospectively under standardized conditions. Patient age ranged from 18 to 68 years (mean +/- SD: 34 +/- 11.6). Atypical uterine bleeding such as menorrhagia, hypermenorrhea and polymenorrhea were found in 69 women. The hair loss varied between 50 and 400 hairs per day (124 +/- 125). Additional signs of hyperandrogenism, i.e. seborrhea (n = 83), acne (n = 52) and hirsutism (n = 28), were often observed. Basal levels of total and free testosterone (T and FT), dihydro-T (DHT) DHEA-sulfate (DS), delta 4-androstendione (A), 17 alpha-hydroxy-progesterone (17P), cortisol (F), progesterone (P), 17 beta-estradiol (E2), sex hormone binding globuline (SHBG), prolactin (PRL), thyreoidea-stimulating hormone (TSH), ferritin (Fe), vitamin B12 (B12) and folat (Fo) were determined by RIA. FT was also measured by equilibrium dialyses. Different methods of determining bound and unbound T were used; their diagnostic value is discussed in detail. In addition, a combined ACTH/TRH-stimulation test was performed in all patients. Pathologic changes of one parameter were detectable in 26.4% of patients, while 67.2% revealed deviations of two or more indices. Excluding clinically relevant borderline values, only 6.4% of patients were without any abnormalities. The incidence rate of pathologic parameters was as follows: FT in % = 52%, Fe = 42%, PRL = 34%, E2 = 34%, FT in pg = 29%, DHT = 28%, SHBG = 26%, TSH = 20.8%, DS = 19%, T = 14%, 17P = 11%, Fo = 7%, A = 6%, F = 6%, B12 = 5%. Group and individual case analyses revealed significant correlations between (1) the levels of the various androgens, PRL and TSH and (2) the E2, SHBG and FT values; these, in turn, were correlated to (3) the occurrence of certain bleeding anomalies (amount, duration, interval) and corresponding ferritin deficiency. Therapy was directed at normalizing the disturbed estrogen-androgen-balance. Using low-dose antiandrogens, estrogens, prolactin suppressants, corticoids, iron-II-preparations as well as estrogen-containing hair lotions hair loss was arrested in 74 of 104 treated women, while regrowth of hair was accomplished in 16 patients. 14 women did not respond to therapy.
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PMID:[Hormonal diagnosis in so-called androgenetic alopecia in the female]. 337 87

The percent absorption of iron from four dietary sources was compared in 2018 human subjects with three indicators of iron status, serum ferritin concentration, percent saturation of plasma transferrin and iron absorption from a reference dose of ferrous sulfate. Higher correlation coefficients (r) were obtained by comparing dietary iron absorption with the reference dose absorption rather than with serum ferritin; for example, r = +0.61 and r = -0.38, respectively, for a meat and vegetable meal. However, in practice serum ferritin is almost as efficient as the reference dose absorption in estimating dietary iron absorption, because the 95% confidence limits calculated from the regression equations were very similar. The values of r calculated for iron absorption versus transferrin saturation were comparable to those obtained with the other indicators only in the range of transferrin saturation values below 25%, whereas in more iron-replete subjects (transferrin saturation greater than 25%), this correlation virtually disappeared. This indicates that, although both serum ferritin and transferrin saturation reflect iron status in iron-depleted subjects, the control of iron absorption in iron-replete subjects is more dependent on iron stores as reflected in the serum ferritin concentration than the percent saturation of transferrin.
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PMID:Relationships among iron absorption, percent saturation of plasma transferrin and serum ferritin concentration in humans. 341 18

Volunteers attending blood donor sessions who fail the copper sulfate screening test merit an explanation of why they are considered ineligible to donate. During a 30-month period, 0.24 percent of men and 2.8 percent of women attending blood donor sessions in the northern region of England failed this test. Their hematologic status was determined by performing complete blood counts on a venous blood specimen and measuring ferritin as an indication of iron stores in a representative sample of approximately 10 percent. Normal blood counts were found in some donors, while others had severe degrees of anemia, and such discrepancies could be clarified only by hemoglobin determinations. Iron deficiency was very common in deferred donors, including 36 of the 88 with normal blood counts in whom ferritin assays were performed. Microcytic blood cells, a hallmark of iron deficiency, were found to be a relatively insensitive measure of low iron stores, except at low levels of hemoglobin. By a check of a venous sample, the hematologic status of most volunteers failing the copper sulfate screening test can be ascertained, and appropriate review, investigation, and treatment can be undertaken.
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PMID:Volunteer blood donors who fail the copper sulfate screening test. What does failure mean, and what should be done? 342 Jun 76

Infusion into rats of the polycation hexadimethrine (HDM) leads to onset of massive proteinuria, which recovers when the infusion is stopped. Several lines of evidence indicate that the proteinuria results from binding of HDM to polyanions of the glomerular filter, with neutralization of shielding of their charges. To determine the mechanism of this proteinuria, we measured the glomerular sieving coefficients of anionic and neutral forms of albumin and IgG in control and proteinuric rats. Surprisingly, these studies revealed a marked defect in size dependence, but not in charge dependence, of glomerular permselectivity in hexadimethrine-treated animals, indicating that binding of HDM induces a structural change in the glomerular filter. In vitro studies of binding of tritiated HDM and cationized ferritin to glomerular basement membrane (GBM) indicate that the binding is not dependent on proteoglycans such as heparan sulfate, nor on sialoproteins such as podocalyxin, but is dependent on charged carboxyl groups of GBM.
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PMID:Charged compounds of the glomerular filter and their role in normal and disordered permselectivity. 343 10

The effect of a 6-week combined treatment with ferrous sulfate (80 mg Fe++ three times daily) and ascorbic acid (75 mg three times daily) on the empty iron stores in 20 patients after gastrointestinal surgery was examined from changes of serum ferritin. One group of 20 patients with similar clinical characteristics served as controls. The treatment replaced the empty iron stores. Since mean serum ferritin concentrations increased from 9 +/- 8 to 29 +/- 11 micrograms/l (P less than 0.001) in males and from 8 +/- 8 to 26 +/- 10 micrograms/l (P less than 0.001) in the females. Also blood hemoglobin and serum iron concentrations increased significantly (P less than 0.01). Among the controls there were no marked changes in serum ferritin, blood hemoglobin or serum iron concentrations. However, the increase of serum ferritin caused by this combined treatment was similar with that caused previously by pure ferrous sulfate treatment. Thus, it is considered that the combined treatment with ferrous sulfate (80 mg Fe++ three times daily) and ascorbic acid (75 mg three times daily) restores the empty iron stores in patients after gastrointestinal surgery, but that the increase is not augmented by the ascorbic acid. Thus, a pure iron therapy is recommended to fill up the empty iron stores in these patients.
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PMID:Ascorbic acid does not augment the restoration effect of iron treatment for empty iron stores in patients after gastrointestinal surgery. 352 35

Anionic sites have been demonstrated in the basement membranes of peritubular capillaries. The anionic barrier function of peritubular capillary wall has been ascribed to these sites. Fenestrated capillaries in other organs have anionic sites in the endothelial cell glycocalyx and at the luminal surface of the fenestral diaphragms. The purpose of this study was to map anionic sites at the luminal surface of peritubular capillaries and to assess whether a concentration gradient for albumin exists across the endothelium. Partial chemical characterization of these anionic sites was done by in vivo enzymatic degradation. The difference in distribution of albumin following enzyme digestion was also studied. The binding of cationized ferritin to the luminal surface indicated that the rat peritubular capillaries have anionic sites along the entire luminal surface of the endothelial cell, including the fenestral diaphragms. Partial biochemical characterization of these sites shows that the sites in the glycocalyx are mainly from neuraminic acid, while the fenestral diaphragms have mainly heparan sulfate proteoglycans. Intravascular albumin extended to the endothelial luminal plasmalemma and to the luminal surface of fenestral diaphragms. Digestion with heparitinase was associated with the leakage of albumin outside the capillary wall. These findings suggest that the anionic surface of fenestrae constitutes a charge barrier of the peritubular capillaries.
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PMID:The anionic sites at luminal surface of peritubular capillaries in rats. 356 Jun 45

The fine structure of the Staphylococcus aureus cell wall was determined by electron microscopy with the new technique of rapid freezing and substitution fixation. The surface of the cell wall was covered with a fuzzy coat which consisted of fine fibers or an electron-dense mass. Morphological examination of the cell wall, which was treated sequentially with sodium dodecyl sulfate, trypsin, and trichloroacetic acid, revealed that this coat was partially removed by trypsin digestion and was completely removed by trichloroacetic acid extraction but was not affected by sodium dodecyl sulfate treatment, suggesting that the fuzzy coat consists mostly of a complex of teichoic acids and proteins. This was confirmed by the application of the concanavalin A-ferritin technique for teichoic acid and antiferritin immunoglobulin G technique for protein A.
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PMID:Structure of the Staphylococcus aureus cell wall determined by the freeze-substitution method. 358 61

The distribution and functional significance of charged groups on the outer and inner faces of the S layer from Bacillus stearothermophilus NRS 1536/3c was investigated. Chemical modification of the exposed amino or carboxyl groups was performed on whole cells, isolated S layers self-assembled in vitro, and cell wall fragments (S layer attached to the peptidoglycan-containing sacculus). Without chemical modification, S layer self-assembly products could be labeled with polycationic ferritin, while S layers on whole cells could not. Following treatment with glutaraldehyde, whole cells were uniformly labeled with polycationic ferritin. Whole cells treated with glutaraldehyde and glycine methyl ester in the presence of carbodiimide did not bind polycationic ferritin significantly above background. Treatment of cell wall fragments with amino-specific, homobifunctional cross-linkers or with carbodiimide alone rendered the S layer protein nonextractable with sodium dodecyl sulfate. After amidation of the accessible carboxyl groups, the modified, guanidine hydrochloride-extractable S layer protomers did not self-assemble into regularly structured lattices. N-Amidination with ethylacetimidate did not interfere with the self-assembly of the isolated protomers. N-Acetylation resulted in a considerable destabilization of the S layer lattice, as seen by the release of a large amount of modified protomers during the reaction. N-Succinylation led to a complete disintegration of the protein lattice. These results indicated that only the inner face of the S layer carried a net negative charge. On both faces, free amino and carboxyl groups of adjacent protomers were arranged in proximity so as to contribute by electrostatic interactions to the cohesion of the protomers in the two-dimensional array. The native charge of the protomers was required for both the in vitro self-assembly of the isolated subunits and the maintenance of the structural integrity of the S layer lattice. Among other functions, the biological significance of the S layers may be in masking the electronegative charge of the cell wall proper.
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PMID:Charge distribution on the S layer of Bacillus stearothermophilus NRS 1536/3c and importance of charged groups for morphogenesis and function. 358 71

This study was designed to determine whether iron contents are altered in hexachlorobenzene (HCB)-induced porphyria, and whether there is any relation between these alterations and the effects of the drug on several enzymes of the haem pathway. To this end, the effect of HCB administration on total, non-haem and haem iron levels was studied. Further, the effects of the addition of: both heated and non-heated HCB-porphyric liver preparations, iron as sulfate, ferritin and haemin and alpha alpha'-bipyridyl and 8-hydroxyquinoline were studied on the following enzymes: delta-aminolaevulinic acid synthase, delta-aminolaevulinic acid dehydratase, porphobilinogenase and porphyrinogen carboxy-lyase. Total and non-haem iron levels increased significantly as a result of HCB intoxication, but there was a non-significant decrease in haem iron content. The increased iron levels did not appear to be directly involved in the increased activities of delta-aminolaevulinic acid synthase and delta-aminolaevulinic acid dehydratase observed in HCB-induced porphyria, since it was not possible to detect any activation in heating and crossed assays nor by the addition of inorganic iron, protein-iron or haemin. Results from heating and crossed assays suggested the existence of an activator for porphobilinogenase and an inhibitor for porphyrinogen carboxy-lyase, while results obtained with chelating agents suggested that iron could partly account for the activation of porphobilinogenase. Iron was not directly involved with the decreased activity of porphyrinogen carboxy-lyase, since neither iron chelators nor different types of iron produced physiologically significant effects.
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PMID:Studies on the role of iron in the alterations observed in hexachlorobenzene-induced porphyria. 359 48

A partial amino acid sequence for three different subunits of the iron storage protein, ferritin, has been determined. Ferritin (Mr approximately 480,000) was isolated from porcine spleen and dissociated into its component subunits (Mr approximately 20,000). The subunits, in turn, were separated into three fractions by reversed-phase HPLC. The fractions appeared to be of equal size by sedimentation velocity, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and size-exclusion chromatography in 6 M guanidinium chloride. All three fractions were shown to be monomeric and to have no covalently attached carbohydrate (J. F. Collawn et al. (1984) Arch. Biochem. Biophys. 233, 260-266). Determination of the amino acid sequence of the C-terminal 70-80 residues from each of the fractions demonstrated three different sequences. Comparison with human liver H and L subunit sequences indicates that two of the porcine ferritin subunits are H-type subunits and one is an L-type subunit. Application of the Chou-Fasman algorithm on the three partial sequences suggests that these respective regions from each of the three subunits would probably adopt the same conformation.
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PMID:Isolation and partial amino acid sequence of three subunit species of porcine spleen ferritin: evidence of multiple H subunits. 368 79


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