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)

Malignant fibrous histiocytomas (MFH) belong to the most frequent soft tissue tumours in adults and have to be discriminated from other tumours with similar morphology. Various tumour markers aid the differential diagnosis. Twenty cases of MFH were studied immunohistochemically using antibodies to vimentin, TPA, desmin, lysozyme, alpha 1-antitrypsin, alpha 1-antichymotrypsin, S-100 protein, neurone-specific enolase (NSE), laminin, fibronectin and ferritin. Vimentin and lysozyme were found in the tumour cells of all, alpha 1-antitrypsin of 18, alpha 1-antichymotrypsin of 19, fibronectin of 16 and ferritin of 12 cases. Antibodies of TPA, desmin, S-100 protein, NSE and laminin did not reveal positive immunoreactivity. Exclusion of spindle-cell carcinoma can be made by positive vimentin and negative TPA reactivity, of melanoma by negative S-100 reactivity, and of leio- and rhabdomyosarcoma by lack of desmin immunoreactivity. Schwannomas contain S-100 protein, but lack lysozyme, alpha 1-antitrypsin, alpha 1-antichymotrypsin and fibronectin. Pleomorphic liposarcomas cannot be distinguished from MFH on the basis of immunohistochemical staining. Vimentin, alpha 1-antitrypsin, alpha 1-antichymotrypsin and fibronectin can, therefore, be regarded as useful markers in the differential diagnosis of MFH.
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PMID:[Immunohistochemical studies in the differential diagnosis of malignant fibrous histiocytoma]. 302 16

We generated a monoclonal anti-vimentin antibody, VIM-1, by mouse hybridoma technique, using an established myofibroblast line as a whole cell immunogen. The presence of vimentin polypeptides in the cultured myofibroblasts was confirmed by SDS-polyacrylamide gel electrophoresis and immunoblotting. By light microscopic immunocytochemistry, myofibroblasts in cultures as well as in frozen tissue sections showed a strong reaction with the anti-vimentin antibody, whereas these cells lacked either detectable desmin or cytokeratin. Our results support the fibroblastic origin of myofibroblasts. Immunoelectron microscopic study with ferritin-ABC technique demonstrated that VIM-1 reacted exclusively with 10-nm intermediate filaments, while other cellular structures revealed uniformly negative reaction against the antibody.
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PMID:Intermediate filaments of myofibroblasts. Immunochemical and immunocytochemical analyses. 360 3

Lipocytes have been classified as vitamin A-storing, desmin-positive cells. In hepatic fibrogenesis, lipocytes transform into myofibroblasts, which express alpha-smooth muscle actin (alpha-SMA) and produce increased amounts of collagen. We isolated a population of vitamin A-poor lipocytes (VAPL) from normal rat liver and examined the morphological and biochemical differences between VAPL and vitamin A-replete lipocytes (VARL). Desmin and alpha-SMA expression were determined by Western blot in quiescent cells and in cells activated by culture on uncoated plastic. Both cell types were alpha-SMA-negative; however, in contrast to VARL, freshly isolated VAPL did not contain desmin. Desmin expression was induced in VAPL on activation. With time in culture, both VAPL and VARL expressed alpha-SMA and produced collagen, indicative of transformation to myofibroblasts. Ferritin receptor expression was demonstrated in cultured VARL after 1 day and in VAPL after 5 days, indicating that this is an early marker of lipocyte activation. After 7 days, VARL and VAPL were indistinguishable in terms of desmin, ferritin receptor expression, and collagen production. This study demonstrates the first isolation and characterization of two distinct quiescent subpopulations of lipocytes from normal rat liver: desmin-negative VAPL and desmin-positive VARL. Both populations of cells can be activated to myofibroblasts, the phenotype associated with hepatic fibrogenesis.
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PMID:Vitamin A-poor lipocytes: a novel desmin-negative lipocyte subpopulation, which can be activated to myofibroblasts. 748 5

We report of a 39 years old patient with a large testicular tumor found during an examination for infertility. The tumor consisted of a spermatocytic seminoma (SS) and a differentiated teratoma (TD). Furthermore, two small foci of seminoma were seen in the surrounding testicular tissue, several testicular tubuli contained carcinoma in situ (CIS). The diagnosis was based on the results obtained with various immunohistochemical markers: keratin, vimentin, desmin, LCA, CD3, CD20, CD45R, ferritin, PLAP, AFP. On the basis of the macroscopic and histopathological features, we propose the following etiology: CIS progressed in an earlier phase to the (larger) TD and later to the (smaller) classical seminoma; likewise, in an earlier phase, SS developed from a still unknown precursor stage. Our case of a mixed tumor as well as other cases reported in the last years do not allow the explanation of a differing etiology for SS. On the contrary, it may be presumed that the origins of seminoma and teratoma on the one hand and SS on the other hand are less divergent than hitherto thought.
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PMID:[A combination of spermatocytic and classic seminoma, mature teratoma and carcinoma in situ of the testis. An attempt at an etiologic explanation]. 821 26

Sarcoidosis, once thought to be a variant of tuberculosis, is currently listed as a disease of unknown etiology. The present study was initiated by unpublished observations that Schaumann bodies-the laminated inclusions often encountered in sarcoid granulomas-cross-reacted with commercial polyclonal antibodies to Mycobacterium bovis, Mycobacterium duvalii and Mycobacterium paratuberculosis. Given the broad cross-reactivity of many mycobacterial antigens, those findings lacked specificity but warranted in depth probing of the immunoprofile of the bodies, particularly for specific mycobacterial antigens. Formalin-fixed tissue from eight patients with an established diagnosis of sarcoidosis was studied with panels of antibodies against both common cytoplasmic proteins and various mycobacterial antigens, using a labeled streptavidin-biotin-alkaline phosphatase technique. Our findings indicate that Schaumann bodies are indeed residual bodies of heterophagic mycobacterial derivation. They immunostained intensely for the lysosomal proteins muramidase and CD68, variably for some cytoskeletal proteins (tubulin, desmin, vimentin) and not at all for cytokeratin, muscle actin, alpha-1-antichymotrypsin and ferritin. Both cross-reactive and species specific antigenic determinants of M. tuberculosis complex were shown to be present. Affinity absorption with killed intact bacilli H37 Rv resulted in virtually equal loss of binding by all polyclonal antimycobacterial antibodies to cross-reactive ligands in Schaumann bodies. In addition, the bodies were clearly labeled with the monoclonal antibodies TB68 and TB71, known to recognize species specific epitopes of Mycobacterium tuberculosis complex. Although obtained on a small number of cases, our findings uphold Schaumann's original postulate that the laminated calcific inclusions represent remnants of "transformed tubercle bacilli".
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PMID:Cross-reactive and species specific Mycobacterium tuberculosis antigens in the immunoprofile of Schaumann bodies: a major clue to the etiology of sarcoidosis. 872 Apr 56

The role of ferritin in lipocyte activation is unknown. This study examined the effect of rat liver ferritin (RLF), human recombinant H-ferritin (HrHF), human recombinant L-ferritin (HrLF), apo-ferritin (apo-RLF), and hemin on lipocyte activation. Lipocytes were cultured on uncoated plastic and were incubated with these agents for 7 days, at concentrations ranging from 10(-14) to 10(-7) M (0.5 to 50 microM for hemin). Collagen/noncollagen protein production and lipocyte proliferation were determined by [3H]proline and [3H]thymidine incorporation, respectively, and the expression of alpha-smooth muscle actin (alpha-SMA) and desmin was determined by Western blot. RLF, at concentrations ranging from 10(-10) to 10(-7) M, decreased alpha-SMA expression by 65-88%. Apo-RLF, HrHF, and HrLF decreased alpha-SMA by 17-45% at 10(-7) and 10(-8) M. Hemin (10 or 50 microM) inhibited alpha-SMA by 37 and 54%, respectively. Desmin expression was not altered by ferritin or hemin. Collagen and noncollagen protein production were not altered by either RLF or apo-RLF. Lipocyte proliferation was decreased by 54, 32, and 40%, by 10(-7) M RLF, HrHF, and HrLF, respectively, whereas apo-RLF had no effect. Thus RLF inhibited lipocyte alpha-SMA expression, which may be due to an effect of sequestered iron, since neither apo-RLF, HrHF, nor HrLF had a potent effect on alpha-SMA expression and all are essentially iron-free. The inhibitory effect of iron-loaded RLF on alpha-SMA expression suggests that tissue ferritin does not initiate lipocyte activation in iron overload, but rather may have a suppressive action on this process.
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PMID:Rat liver ferritin selectively inhibits expression of alpha-smooth muscle actin in cultured rat lipocytes. 877 81

Marbling of cattle meat is dependent on the coordinated expression of multiple genes. Cattle dramatically increase their intramuscular fat content in the longissimus dorsi muscle between 12 and 27 months of age. We used the annealing control primer (ACP)-differential display RT-PCR method to identify differentially expressed genes (DEGs) that may participate in the development of intramuscular fat between early (12 months old) and late fattening stages (27 months old). Using 20 arbitrary ACP primers, we identified and sequenced 14 DEGs. BLAST searches revealed that expression of the MDH, PI4-K, ferritin, ICER, NID-2, WDNMI, telethonin, filamin, and desmin (DES) genes increased while that of GAPD, COP VII, ACTA1, CamK II, and nebulin decreased during the late fattening stage. The results of functional categorization using the Gene Ontology database for 14 known genes indicated that MDH, GAPD, and COP VII are involved in metabolic pathways such as glycolysis and the TCA cycle, whereas telethonin, filamin, nebulin, desmin, and ACTA1 contribute to the muscle contractile apparatus, and PI4-K, CamK II, and ICER have roles in signal transduction pathways regulated by growth factor or hormones. The final three genes, NID-2, WDNMI, and ferritin, are involved in iron transport and extracellular protein inhibition. The expression patterns were confirmed for seven genes (MDH, PI4-K, ferritin, ICER, nebulin, WDNMI, and telethonin) using real-time PCR. We found that the novel transcription repressor ICER gene was highly expressed in the late fattening stage and during bovine preadipocyte differentiation. This information may be helpful in selecting candidate genes that participate in intramuscular fat development in cattle.
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PMID:Identification of differentially expressed genes related to intramuscular fat development in the early and late fattening stages of hanwoo steers. 1792 10