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)

We studied the pretreatment serum levels of 6 tumor markers in gynecological patients with and without malignant disease. The tumor markers were carcinoembryonic antigen (CEA), tissue polypeptide antigen (TPA), ferritin, Schwangerschaftsprotein 1 (SP1), Schwangerschaftsprotein 3 (SP3) and cancer antigen 125 (CA125). The results were as follows: (1) Serum CA125 and TPA levels were raised in 81% and 57% of patients with ovarian serous cystadenocarcinoma; CEA and SP3, in 52% and 43% respectively of patients with ovarian mucinous cystadenocarcinoma; CA125, TPA and SP3, in 76%, 48% and 48% respectively of patients with other ovarian malignancies; and TPA and SP3, in 56% and 40% respectively of patients with endometrial carcinoma. (2) Serum levels of TPA, ferritin and CA125 were more often raised with advancing stages of malignant disease. (3) Serum TPA levels were elevated in 55% of patients with stage I endometrial carcinoma, and serum SP3 levels were elevated in 35% of patients with a stage I malignant ovarian neoplasm and in 45% of patients with endometrial carcinoma. (4) One of the 6 tumor markers showed a raised level in 84% of patients with gynecologic malignancy as against 56% in those with benign gynecologic diseases.
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PMID:Serum levels of six tumor markers in patients with benign and malignant gynecological disease. 340 Oct 42

The major sialoglycoprotein of the human red cell membrane, glycophorin A, was isolated and examined by rotary shadowing and transmission electron microscopy. The glycophorin A molecule appeared as a cloud-like structure with a short, dense core within a large cloud. Mild acid hydrolysis in 0.05 M H2SO4, 80 degrees C for 1 hr reduced the size of the cloud significantly but left the dense core intact indicating that the original cloud represented the sialylated oligosaccharide chains of glycophorin A with the dense core being the polypeptide chain and its associated linkage proteins. Incubating glycophorin A with cationized ferritin (CF) revealed that the CF was bound only to the cloud, a finding that supports the view that the cloud is comprised of the sialylated oligosaccharide chains of the glycophorin A molecule. SDS-polyacrylamide gel electrophoresis revealed that our preparation of glycophorin A, as well as commercial preparations, consisted of monomers, dimers and oligomers of glycophorin A with trace amounts of the minor glycophorins and linkage proteins. Knowledge of the ultrastructure of this important integral protein will enable one to design studies to determine its functional role in the membrane.
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PMID:Ultrastructure of a transmembrane glycoprotein, glycophorin A. 340 39

The significance of neuron-specific enolase (NSE) in the diagnosis and treatment monitoring of lung cancer was investigated in comparison with such established tumour markers as carcinoembryonic antigen (CEA), tissue polypeptide antigen (TPA), ferritin and calcitonin. We determined the serum concentrations of these tumour markers in 25 patients with small cell lung cancer (SCLC), 30 patients with non small cell lung cancer (NSCLC), and 38 patients with benign pulmonary diseases (BPD). In 14 patients with lung cancer, it was possible to follow up the behaviour of the tumour markers under treatment for up to 16 months. Calcitonin proved to have a surprisingly low sensitivity for SCLC. The utility of TPA and of ferritin was restricted, although the sensitivity was comparably high, by the high rate of false positive results. For NSCLC, CEA proved to be the best tumour marker. At present, NSE appears to be the tumour marker with the greatest specificity and sensitivity for SCLC. Its determination in the diagnosis, treatment and follow-up of SCLC makes good sense.
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PMID:Neuron-specific enolase in the diagnosis and therapy monitoring of lung cancer: a comparison with CEA, TPA, ferritin and calcitonin. 342 47

The tumour markers carcinoembryonic antigen (CEA), ferritin, cancer antigen 125 (CA 125) and tissue polypeptide antigen (TPA) were measured by radioimmunoassay in sera from 80 patients with ovarian cancer pre-operatively, postoperatively, during cytostatic chemotherapy and on follow up. Discriminant analysis was applied to obtain retrospective classification of 60 patients into a group showing a favourable course of the disease (no recurrence, tumour regression) and into a group with an unfavourable course (recurrence, progression of the tumour). The classification was based on the introduction of the Cutting Score. By means of this bio-mathematical model it was possible to make at least a short-term prognostic statement in a further 20 patients. It is suggested that invasive diagnostic procedures may not be required in patients who are found to have normal tumour marker levels.
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PMID:[Predictive value of a tumor marker combination for the monitoring of ovarian cancer]. 346 Feb 73

The serum levels of CA 125 and CA 19-9 were determined by an immunoradiometric assay employing the monoclonal antibody OC 125 and anti-CA 19-9 antibody in 88 patients with ovarian carcinoma. When a cut-off value of CA 125 was set below 35 U/ml in the control group, serum elevated levels of CA 125 were found in 86.7% of the patients with surgically demonstrable ovarian serous cystadenocarcinoma, in 100% (4/4 cases) of clear-cell carcinoma, in 50% (2/4 cases) of endometrioid carcinoma, in 100% (5/5 cases) of undifferentiated carcinoma, and in 80% of the recurrent cases. Using a cut-off value of 37 U/ml, serum elevated levels of CA 19-9 were detected in 68.2% of mucinous cystadenocarcinoma, in 28.9% of serous cystadenocarcinoma, in 75% (3/4 cases) of metastatic ovarian carcinoma, and in 37.5% of the recurrent cases. A statistical analysis of the combination assay using CA 125, CA 19-9, tissue polypeptide antigen (TPA), immunosuppressive acidic protein (IAP), ferritin and CEA was carried out by multivariate method (discriminatory analysis) in 45 patients with ovarian carcinoma and 50 healthy subjects. As a result before treatment, positive rates of a single tumor marker were 79.7% with CA 125, 42.7% with CA-19-9, 73.1% with IAP, 61.7% with TPA, 64.3% with ferritin and 25.4% with CEA, respectively. A combination assay of these markers was useful for detecting identification of ovarian carcinoma, by which it gave a higher accuracy of ovarian cancer detection.
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PMID:Clinical use of CA 125 and its combination assay with other tumor marker in patients with ovarian carcinoma. 347 96

To evaluate the predictive value of the serial determination of various tumor markers, we measured carcinoembryonic antigen, ferritin, cancer antigen 125, and tissue polypeptide antigen in 109 patients with ovarian cancer before surgery, during postoperative chemotherapy, and follow-up. From these patients two groups were randomly selected. Group 1 (30 patients) had a favorable course, and Group 2 (30 patients) had an unfavorable course. Using the discriminant analysis we calculated a linear discriminant function and a cut-off score. The two groups were thereby separated according to their scores (characteristic values) from their marker values. The scores accurately reflected the clinical course in 55 of the 60 patients (91.7%). This discriminant function was then used to make a prognosis in 49 patients. In 21 patients an elevated characteristic value (greater than or equal to cut-off score) indicated disease progression 5 months before clinical confirmation was possible. The remaining 28 patients scored below the cut-off point. From six to 65 months (mean, 26.2) after surgery all are free of recurrence. It is concluded that invasive procedures, second-look laparotomy, for instance, may not be necessary in following up ovarian cancer patients with normal tumor marker profiles.
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PMID:The predictive value of a combination of tumor markers in monitoring patients with ovarian cancer. 348 57

Bacterioferritins are type-b cytochromes which resemble ferritin. Amino acid analysis combined with chemical modification and partial sequence analysis characterize bacterioferritin of Escherichia coli in terms of its primary structure. It is a protein composed of one kind of polypeptide chain that commences with methionine and terminates with glutamic acid. The length of the polypeptide chain is, tentatively, 146 residues. Besides the N-terminal methionine residue there are three more methionine residues, which yield four CNBr peptides, which have been aligned. The identity of the following positions in the sequence has been ascertained: residues 1-25, 30-37, 83-88, 127-132 and 143-146. No homology with ferritin was found.
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PMID:Preliminary results for the primary structure of bacterioferritin of Escherichia coli. 390 32

As much as 4% of the total protein in pure liver ferritin from mice with short-term parenteral iron overload produces a minor band migrating anodally to the major (alpha) band of holoferritin with non-denaturing polyacrylamide gel electrophoresis. The components in this minor band and the alpha band have been isolated to purity by preparative electrophoretic fractionation. The protein in the minor band is ferritin, since it contains ferric iron and fulfills defining criteria at the level of biochemistry, immunology and ultrastructure. Native polyacrylamide electrophoresis with pore-size-gradient gels shows that the ferritin molecules in the minor band have a slightly smaller diameter than the holoferritin in the alpha band. Isoelectric focusing reveals that the smaller ferritin has an identical number and range of charge isomers (pI 4.9-5.3) as the larger ferritin, but the relative amount of each size class within some isoferritin bands differs. The smaller ferritin molecules are structurally intact and are made from polypeptide subunits with Mr 18 000; the larger ferritin molecules have subunits with Mr 22 000. The minor species of hepatic ferritin thus has a smaller molecular size because it is made mainly from smaller subunits. No minor electrophoretic band can be detected in liver ferritin obtained from mice with normal iron levels. These results demonstrate that siderosis induces the formation of molecular size polymorphism (macroheterogeneity) in mouse liver ferritin. The new smaller hepatic ferritin could serve to redistribute excess iron into the main storage organs during the early response to iron overload, since it appears to be identical to one of the two types of serum ferritin molecules present in these siderotic mice.
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PMID:Molecular size heterogeneity of ferritin in mouse liver. 392 2

Collagen VI is a large, disulfide-bonded protein complex which is widely distributed in connective tissue. The constituent polypeptide chains (Mr = 110,000-140,000) consist of collagenous and noncollagenous segments, are degraded to chains of about half the size when collagen VI is solubilized by pepsin, and assemble to a unique pattern of oligomers. As revealed by electron microscopy, the triple-stranded protomer consists of a triple helix 105 nm in length flanked on each side by globular domains of similar size (diameter about 7 nm). Protomers are assembled to dimers by an antiparallel staggered alignment of triple-helical segments. This leads to inner regions, 75 nm in length, of two slightly supercoiled triple helices flanked by globular domains. At both sides 30-nm-long outer triple-helical segments emerge that are terminated by globules. Tetramers are formed from laterally aligned dimers that cross with their outer triple-helical segments in a scissors-like fashion. The same structures, except with much smaller globular domains, are found in pepsin-treated collagen VI. Disulfide-linked collagen VI produced by cultured fibroblasts has a size similar to that of genuine collagen VI found in tissue extracts. Larger forms of collagen VI are assembled from tetramers by end-to-end aggregation which because of an overlap of the outer segments brings all globular domains close together. This arrangement predicts microfibrillar structures in tissues with a periodicity of 100-110 nm and a diameter of 5-10 nm. Structures consistent with this proposal were indeed found by immunoelectron microscopy of placenta and aorta using the ferritin technique. Large, lateral aggregates of collagen VI microfibrils may in addition exist in cell cultures and tissues ("zebra collagen," "Luse bodies") and are presumably maintained by contacts between globular domains.
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PMID:Structure and macromolecular organization of type VI collagen. 393 30

In 225 primary breast carcinomas the concentrations of carcinoembryonic antigen (CEA), ferritin, and tissue polypeptide antigen (TPA) were determined by radioimmunometric assays both in serum and in cytosol. The relationship of the three markers with the receptor content of the tumor was evaluated. No relationships were found between the serum level of each marker and the receptor status. In the cytosol, ferritin was higher in receptor-negative than in receptor-positive cases, whereas CEA and TPA showed significantly higher values in receptor-positive than in receptor-negative patients. Moreover, a direct relationship was found between estrogen receptor and both CEA and TPA and between progesterone receptor and TPA. Even if the significance of these findings is still unclear, from our data it can be concluded that there exists a noncasual relationship between the receptor status and the cytosol content of CEA and, particularly, TPA.
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PMID:Carcinoembryonic antigen, ferritin, and tissue polypeptide antigen in serum and tissue. Relationship with the receptor content in breast carcinoma. 394 25


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