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)

In the introduction the author explains the term marker and its synthesis. Demands on markers are as follows: 1. strict specificity, 2. correlation with the clinical stage, 3. prognostic information. The authors discusses in more detail the problem of human choriogonadotropin, alpha-fetoprotein, basic fetoprotein and specific beta-1-glycoprotein in germinal testicular tumours. The author mentions placental alkaline phosphatase, ferritin, lactic dehydrogenase in the above tumours, in carcinoma of the prostate prostatic specific antigen, in carcinoma of the bladder oncofoetal antigens.
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PMID:[Introduction to the problem of markers in urologic oncology]. 213 39

Absorptive cells of the intestinal epithelium endocytose proteins from both apical and basolateral membrane domains. In absorptive cells of suckling rat ileum, luminal protein tracers first enter an apical tubulovesicular endosomal system, then enter larger apical endosomal vesicles and multivesicular bodies (MVB), and finally are delivered to a giant supranuclear lysosomal vacuole. To determine whether proteins endocytosed from the basolateral domain in vivo enter the same endosomal or lysosomal compartments as those taken up from the apical side, we simultaneously applied cationized ferritin (CF) apically (by intra-luminal injection) and horseradish peroxidase (HRP) basally (by intravenous injection), and examined absorptive cells after 3 min to 60 min using light, electron and fluorescence microscopy. At early times, CF and HRP entered separate endosomal compartments at apical and basolateral poles. At no time did HRP enter the apical tubulovesicular system, and CF never entered early basolateral endosomes. After 15 min, however, both tracers appeared together in large late endosomes and MVB located apically, above the giant vacuole. From 15 to 60 min both tracers accumulated in the giant vacuole. Membranes of some apical late endosomes, all apical MVB, the giant vacuole, and occasional sub-nuclear vesicles contained immunoreactive Igp120, a glycoprotein specific to late compartments of the endosome-lysosome system. These results show that highly polarized intestinal epithelial cells have separate apical and basolateral early endosomal compartments, presumably to maintain distinct membrane domains while allowing endocytosis and recycling of membrane from both surfaces. Apical and basolateral endocytic pathways, and presumably vesicles delivering hydrolytic enzymes and lysosomal membrane components, converge at the apical late endosome.
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PMID:Convergence of apical and basolateral endocytic pathways at apical late endosomes in absorptive cells of suckling rat ileum in vivo. 227 98

The cell surface of Clostridium symbiosum HB25 is covered by a squarely arranged surface layer (S-layer) glycoprotein. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the sodium dodecyl sulfate-soluble whole-cell extract showed the presence of several high-molecular-weight protein bands in a narrow range (approximate Mr, 140,000) which, upon periodic acid-Schiff staining, gave a positive reaction. After proteolytic degradation of the purified S-layer glycoprotein, a single glycopeptide fraction was obtained by gel permeation chromatography. Hydrolysis, treatment with aqueous hydrofluoric acid, and 1H and 13C nuclear magnetic resonance studies showed that the glycoprotein glycan is a high-molecular-weight polymer (approximate Mr, 15,000) of tetrasaccharide repeating units with the component sugars N-acetylgalactosamine (GalNAc), N-acetylmannosamine (ManNAc), and N-acetylbacillosamine (BacNAc; 2-N-acetyl-4-amino-2,4,6-trideoxy glucose) linked by monophosphate diesters. The following structure is proposed: [----6)-alpha-D-ManpNAc-(1----4)-beta-D-GalpNAc-(1----3)-alpha-D-+ ++BacpNAc- (1----4)-alpha-D-GalpNAc-(1----PO3)----]n. The nuclear magnetic resonance data provided evidence for a charge interaction between the free amino group of BacNAc and the phosphate group of adjacent glycan chains. Since polycationic ferritin did not label the cell surface of intact cells, an electrostatic interaction can also be expected in vivo, leading to a charge-neutral outer surface, which is characteristic of all other S layers from members of the family Bacillaceae studied so far.
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PMID:Characterization of the surface layer glycoprotein of Clostridium symbiosum HB25. 233 5

Previous studies have shown that the Xenopus laevis egg envelope exists in three forms with differing ultrastructural, macromolecular, and sperm penetrability properties. The coelomic envelope (CE) is derived from eggs released from the ovary into the body cavity of the female, the vitelline envelope (VE) from eggs which have passed through the oviduct, and the fertilization envelope (FE) from fertilized eggs. In the present study, the physicochemical characteristics of these three envelope types were differentiated. Investigation of envelope solubility, deformability, sulfhydryl reactivity, and hydrophobic dye and ferritin binding capacity demonstrated that profound physicochemical changes occur in envelope conversions CE----VE----FE. The physical strength of the envelopes, as evidenced by deformability studies, ranked FE greater than CE greater than VE. These differences were not accountable by differences in the number of disulfide bonds, although the CE sulfhydryl groups were significantly less accessible than those in the VE or FE. All three envelope forms were hydrophilic in nature, exhibiting little ability to bind 1-anilino-8-naphthalenesulfonic acid. The CE bound greater amounts of ferritin in comparison to the VE and FE, indicating the presence of a basic domain, presumably in the 43-kDa glycoprotein, which is lost upon proteolysis to 41 kDa during the CE----VE conversion. The envelope integrity of all three forms was maintained by both noncovalent and covalent (disulfide) bonds. Measurements of the effect of pH on envelope solubilization indicated the involvement of an ionizable group with pKa of 8.0 in maintaining envelope structure.
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PMID:Physicochemical characterization of progressive changes in the Xenopus laevis egg envelope following oviductal transport and fertilization. 233 86

Eleven potential biochemical markers were measured in serum from 33 patients with malignant and 13 with benign colorectal disease: four isoenzymes (creatine kinase-BB, homoarginine-sensitive alkaline phosphatase, salivary-type amylase, and macro-creatine kinase type 2), five specific proteins (ferritin, alpha 1-acid glycoprotein, C-reactive protein, alpha 1-antitrypsin, and ceruloplasmin), one oncofetal antigen (carcinoembryonic antigen, CEA), and one hormone (beta human choriogonadotropin). The sensitivity of individual markers for the detection of early-stage malignancy (n = 11) ranged from 0% to 64% (CEA 18%); for late-stage colon malignancy (n = 12) from 8% to 83% (CEA 83%). Specificity in patients (n = 10) with benign intestinal disease ranged from 80% to 100% (CEA 100%). The five most-sensitive markers--C-reactive protein, alpha 1-glycoprotein, CEA, macrocreatine kinase type 2, and homoarginine-sensitive alkaline phosphatase--were selected for use as a "colon panel." In retrospective comparison, use of the colon panel instead of CEA alone increased sensitivity by 17% and 64% for late-and early-stage cancer, respectively; specificity, however, decreased by 30%, but should improve with serial testing.
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PMID:Multiple markers of malignancy in sera of patients with colorectal carcinoma: preliminary clinical studies. 241 37

The morphologic display of testicular cancer is a heterogenous cellular pattern. A biological heterogeneity is also true for the expression of tumor markers. The biosynthesis of tumor marker proteins alpha-fetoprotein (AFP), ferritin, Schwangerschaftsprotein (SP 1) glycoprotein, tissue polypeptide antigen and of hormones (beta-human chorionic gonadotropin (HCG) = significantly present in nonseminoma germ cell tumors--does, however, define only a small number of cancer cells. To better visualize the majority of cancer cells, lectin binding was studied. During the oncogenic transformation a distinct change of cell membrane glycoproteins has been observed. Reactions of WGA/PNA lectins which get attached to glycoproteins with cancer tissue sample from seminomas (n = 20) and nonseminomas (n = 20) were analyzed. The results were correlated to AFP/beta-HCG positive (negative) immunohistology to establish further subgroups of biological homogeneity. The binding of WGA lectin appears relatively more frequent in both seminoma and nonseminoma than that of PNA. Lectin binding of WGA and/or PNA can be stained in 3/11 AFP- and beta-HCG-negative nonseminoma tissues while lectin staining is positive in 7/18 beta-HCG-negative seminomas. The fact that lectin binding is dependent on the spermatozoogenesis and on androgens in normal testis tissues asks for more detailed studies in this field.
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PMID:[Lectin binding in immunohistologically AFP/HCG positive and negative testicular carcinoma]. 243 37

The content of normal serum proteins, acute phase (C-reactive protein, pregnancy-associated alpha 2-glycoprotein) and tissue proteins (ferritin, nonspecific tissue esterase) was studied in the sputum of 256 patients with different pulmonary pathology, over time using immunochemical methods. Protein elimination with the sputum was shown to depend upon the nature and gravity of bronchitis and pulmonary destruction. Analysis of the qualitative composition of the sputum proteins and their content can be used in pulmonology for differential diagnosis and assessment of a course of pulmonary diseases.
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PMID:[Clinical significance of the immunochemical study of serum and tissue proteins of the sputum in pulmonary pathology]. 247 Jan 61

In four patients with trisomy 21 (three constitutional, one acquired) with a morphological undifferentiated leukemia, diagnosis of erythroid leukemia was established by both immunophenotyping and ultrastructural studies. Indeed, a majority of blasts from three patients expressed several erythroid markers such as carbonic anhydrase 1, spectrin beta chain, and glycophorin A. In addition, band 3 and hemoglobin were immunologically detected in a fraction of the blast cells from two cases. At ultrastructural level, a majority or all blast cells exhibited erythroid differentiation features such as theta granules and ferritin molecules. However, platelet glycoproteins GP Ib, GP IIb, and GP IIIa were also immunologically detected in a fraction (from 14-82%) of the blasts. Since the ultrastructural study indicated that some promegakaryoblasts were also present in three patients, double labeling between erythroid markers (glycophorin A or carbonic anhydrase I) and platelet glycoprotein (Ib or IIIa) was performed and showed a clear overlap between the two kinds of markers. A similar approach was performed at ultrastructural level and indicated that blast cells with ultrastructural erythroid features of differentiation may have three distinct phenotypes, i.e., presence of glycophorin A without platelet glycoproteins or, conversely, the presence of platelet glycoproteins without glycophorin A and coexpression of glycophorin A and platelet glycoproteins. Expression of glycophorin A correlated directly with the differentiation level of the erythroid blasts, whereas platelet glycoproteins were essentially expressed in the more primitive leukemic erythroid cells. The GP Ib synthesized by these blasts was subsequently studied. The GP Ib alpha mRNA analyzed by Northern blot from these erythroid cells was identical in size with that from megakaryocytic cells as was the molecular weight of the GP Ib molecule from both after immunoprecipitation by a monoclonal antibody. Therefore, "in vivo" erythroid leukemic cells may express the main platelet glycoproteins including GP Ib.
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PMID:Expression of platelet glycoproteins by erythroid blasts in four cases of trisomy 21. 252 26

M cells of intestinal epithelia overlying lymphoid follicles endocytose luminal macromolecules and microorganisms and deliver them to underlying lymphoid tissue. The effect of luminal secretory IgA antibodies on adherence and transepithelial transport of antigens and microorganisms by M cells is unknown. We have studied the interaction of monoclonal IgA antibodies directed against specific enteric viruses, or the hapten trinitrophenyl (TNP), with M cells. To produce monospecific IgA antibodies against mouse mammary tumor virus (MMTV) and reovirus type 1, Peyer's patch cells from mucosally immunized mice were fused with myeloma cells, generating hybridomas that secreted virus-specific IgA antibodies in monomeric and polymeric forms. One of two anti-MMTV IgA antibodies specifically bound the viral surface glycoprotein gp52, and 3 of 10 antireovirus IgA antibodies immunoprecipitated sigma 3 and mu lc surface proteins. 35S-labeled IgA antibodies injected intravenously into rats were recovered in bile as higher molecular weight species, suggesting that secretory component had been added on passage through the liver. Radiolabeled or colloidal gold-conjugated mouse IgA was injected into mouse, rat, and rabbit intestinal loops containing Peyer's patches. Light microscopic autoradiography and EM showed that all IgA antibodies (antivirus or anti-TNP) bound to M cell luminal membranes and were transported in vesicles across M cells. IgA-gold binding was inhibited by excess unlabeled IgA, indicating that binding was specific. IgG-gold also adhered to M cells and excess unlabeled IgG inhibited IgA-gold binding; thus binding was not isotype-specific. Immune complexes consisting of monoclonal anti-TNP IgA and TNP-ferritin adhered selectively to M cell membranes, while TNP-ferritin alone did not. These results suggest that selective adherence of luminal antibody to M cells may facilitate delivery of virus-antibody complexes to mucosal lymphoid tissue, enhancing subsequent secretory immune responses or facilitating viral invasion.
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PMID:Binding and transepithelial transport of immunoglobulins by intestinal M cells: demonstration using monoclonal IgA antibodies against enteric viral proteins. 254 Nov 37

A survey of recent knowledge on structure and importance of lactoferrin and ferritin is given. Lactoferrin is a symmetrically constructed glycoprotein which appears in the milk and in the body fluids and develops a bacteriostatic efficiency on account of the ability to Fe-binding together with other factors such as the IgA. In a particularly high concentration it is contained in the colostral milk of the woman. In the milk of the cattle the content is small. In the neutrophil granulocytes it is of importance for the functional ability in the phagocytosis. The ferritins are spherically constructed molecules which possess channels through which Fe-ions (up to 4,500 pro molecule) can be taken up or taken off. The ferritin content in the serum is correlated with the Fe-content of the liver and is dependent upon age as well as the Fe-supply. It decreases in Fe-deficiency: it increases in iron overload, in infectious diseases, in inflammation as well as in tumour development.
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PMID:[Recent knowledge of the structure and function of lactoferrin and ferritin]. 266 92


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