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Results for “protein markers”

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At least 19 recordsLinked to original sources
PubMed1977

Alpha1-antitrypsin, protein marker in oral contraceptive-associated hepatic tumors.

Tissue specimens from a series of 46 hepatic tumors occurring in young female oral contraceptive users were tested for alpha1-antitrypsin deposition, utilizing immunocytochemical and histochemical methods. In two instances serum alpha1-antitrypsin phenotyping was also performed. Immunoreactive alpha1-antitrypsin deposits were demonstrated in benign lesions, including 56% of cases of focal nodular hyperplasia and 68% of cases of liver-cell adenoma, and in 89% of cases of malignant hepatoma. There was good correlation between alpha1-antitrypsin deposits and variable amounts of finely granular, or globular, diastase-resistant periodic acid-Schiff positivity within tumor cells. While quantitative differences in alpha1-antitrypsin deposits between benign and malignant cell proliferations were not observed, a qualitative continuum that linked all tumors in the study group was found. The findings suggest that alpha1-antitrypsin deficiency is not related to the hepatic tumors developing in oral contraceptive users. The tumor tissue deposits of alpha1-antitrypsin observed represent a marker protein, the significance of which is undefined.

Carcinoma, Hepatocellular↗
PubMed1976

Isolation and characterization of rat olfactory marker protein.

The olfactory marker protein was isolated and characterized from rat olfactory bulbs. Its properties and those of the olfactory marker protein isolated from the mouse are described. The rat protein was less acidic (pI = 5.0) than the mouse protein (pI = 4.7). However, the amino acid compositions were very similar: in both proteins arginine plus lysine accounted for 13 mol% and glutamate plus aspartate for 30 mol% of the total residues. Molecular weights of both proteins estimated by sodium dodecyl sulfate gel electrophoresis were indistinguishable and estimated to be 16,500. The molecular weight of the native rat olfactory marker protein estimated by gel filtration techniques was 30,000, which is identical to the molecular weight of the native mouse and garfish olfactory marker proteins. This suggested a dimeric structure. The purified rat and mouse proteins behaved like species of 35,000 molecular weight on gel filtration.

Amino Acids↗
PubMed1977

Immunocytochemistry of the olfactory marker protein.

The olfactory marker protein has been localized, by means of immunohistochemical techniques in the primary olfactory neurons of mice. The olfactory marker protein is not present in the staminal cells of the olfactory neuroepithelium, and the protein may be regarded as indicative of the functional stage of the neurons. Our data indicate that the olfactory marker protein is present in the synaptic terminals of the olfactory neurons at the level of the olfactory bulb glomeruli. The postsynaptic profiles of both mitral and periglomerular cells are negative.

Animals↗
PubMed1979

Uptake of marker proteins by glycoprotein-containing cells of the pregnant rat uterus and placenta.

A study was made of cells in the pregnant rat uterus and placenta known to contain glycoprotein inclusions to investigate their ability to endocytose marker proteins (fluorescein conjugated serum and horseradish peroxidase) injected into the maternal circulation. The visceral endoderm showed marked uptake of both proteins, though in later pregnancy this was restricted to the area of yolk sac adjacent to the chorio-allantoic placenta. The intracellular distribution of the endocytosed marker proteins resembled that of the glycoprotein inclusions. In the earlier stages some of the giant cell inclusions contained glycoprotein, some showed staining with the Dunn-Thompson technique for haemoglobin, and some showed peroxidase activity. There was endocytosis of both marker proteins by giant cells, and apparently this occurred independently of ingestion of red blood cells. Uptake by the giant cells persisted to a later stage in the area round the margin of the chorio-allantoic placenta than in the other giant cells. Endocytosis occurred in the labyrinthine trophoblast, and the glycoprotein inclusions found in this situation may represent material being transmitted or digested. The glycoprotein-containing granulated metrial gland cells showed no evidence of endocytotic activity, but there was uptake of both marker proteins by the associated stromal cells.

Animals↗
PubMed2025

Construction and Isolation of Recombinant Vaccinia Virus by Homologous Recombination Using Fluorescent Protein Markers.

Genetic modification of vaccinia virus (VACV) is a fundamental and valuable research technique in elucidating the function of VACV genes, as well as the development as vaccine vectors for other infectious diseases, oncolytic therapeutics for cancers, and protein expression systems in mammalian cells. Because of the large size of poxvirus genome and noninfectious feature of the naked viral DNA, construction of recombinant VACV relies on intracellular homologous recombination between transfected DNA and replicating viral DNA in infected cells occurred in VACV infected cells. The efficiency of homologous recombination event for vaccinia virus is relatively low, and recombinant viruses only account for 0.1% of progeny viruses. Therefore, fluorescent protein markers are often included in the transfected DNA to facilitate the selection and screening of recombined viruses. Here we provide a detailed procedure for the design, generation, isolation, and detection of recombinant VACV by homologous recombination using fluorescent protein markers.

Vaccinia virus↗
PubMed1977

Structural protein markers in the avian oncoviruses.

The proteins of purified avian oncoviruses were analyzed by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and isoelectric focusing. Certain members of the avian leukosis-sarcoma viruses (ALSV) had group-specific antigens with altered electrophoretic properties. (i) The p27 protein of Rous-associated virus 0 (RAV-0) had a lower electrophoretic mobility in SDS gels and a lower isoelectric point than the p27 of other ALSV. (ii) The p19 proteins of RAV-1, RAV-2, and the Bryan high-titer strain of Rous sarcoma virus had higher mobilities in SDS gels than did the corresponding protein of other viruses. This altered electrophoretic mobility was correlated with specific differences in the tryptic peptides of radioiodinated p19s. (iii) The p15 protein of RAV-7 had a lower mobility in SDS gels than did the p15 of other ALSV. These markers were used in a study of the structural proteins of subgroup E RAV-60 produced after infection of chicken embryo cells by exogenous ALSV. Although exogenous group-specific protein markers could often be identified in the subgroup E isolates, one RAV-60 had a p27 that comigrated with the p27 of RAV-0. The p19s of two other RAV-60 isolates had electrophoretic properties that were different than those of p19s from either RAV-0 or the exogenous viruses. These results support the hypothesis that RAV-60 is generated by recombination between endogenous and exogenous oncoviruses and indicate that at least the p27 encoded by RAV-0 is closely related to a protein specified by endogenous viral information in chicken cells.

Autoradiography↗
PubMed1976

Alpha1-antitrypsin and alpha-fetoprotein. Protein markers in endodermal sinus (yolk sac) tumors.

A combined immunocytochemical and quantitative serum and tissue study was performed on a group of endodermal sinus (yolk sac) tumors, localizing and measuring both alpha1-antitrypsin (AAT) and alpha-fetoprotein (AFP) in tumor tissue and patient sera. Utilizing indirect immunofluorescent and triple-sandwich immunoperoxidase methods, both proteins were demonstrated within intra- and extracellular periodic acid-Schiff-positive hyaline globules characteristic of the tumor, as well as within the cytoplasm of tumor epithelial cells lining endodermal sinuses, where AAT deposition predominated. Tumor tissue extracts confirmed the presence of significant quantities of both proteins, and pretreatment serum elevations of both showed a parallel decline during therapy. In this study, AAT is characterized as a tumor protein marker for the first time, and a parallelism between AAT and AFP is demonstrated in both serum and tumor tissue. These findings represent additional supportive evidence for the yolk sac origin of endodermal sinus tumors in man.

Child↗
PubMed1978

Mid-G1 marker protein(s) in 3T3 mouse fibroblast cells.

Quiescent 3T3 mouse fibroblast cells in a state of growth arrest due to serum deprivation were exposed to [14C]isoleucine. The cell cultures were then stimulated by the addition of 10% fetal calf serum. At various times after stimulation, the 14C-labeled cells were exposed to [3H]isoleucine. Cytoplasmic extracts from the double-labeled cells were subjected to sodium dodecyl sulfate/slab gel electrophoresis. By these procedures it was found that the relative rate of synthesis of a protein species of Mr 50,000 increased after stimulation of quiescent cells, reached a maximum at 5 hr, and then decreased before the 3T3 cells began to enter the S phase. The characteristic peaking profile of mid-G1 protein synthesis exhibited by the Mr 50,000 polypeptide can serve as a useful marker for the progression of events in G1 prior to exit into S.

Cell Cycle↗
PubMed1977

Radioimmunoassay for murine lactoferrin, a protein marker of myeloid and mammary epithelial secretory cell differentiation.

A radioimmunoassay was developed for murine lactoferrin (LF), a non-heme, iron-binding glycoprotein which appears to be a specific biochemical marker of differentiation in several cell types. Lactoferrin was labeled with 125I by the chloramine-T method to yield a product having 20 muCi/mug protein and an isotope incorporation of 0.6 atoms of 125I per molecule. Separation of bound and free lactoferrin was accomplished by either of two procedures, a double-antibody technique or precipitation in the presence of 50% saturated ammonium sulfate. The entire assay, including counting, was accomplished in less than 2 days and had a lower limit of sensitivity and a range of 1 ng/ml and 1-32 ng/ml, respectively, using rabbit antiserum in a dilution of about 1:10,000. The binding between LF and rabbit antiserum exhibited two association constants having values of 1.8 x 10(11) and 1 x 10(9) l/mole. The assay was specific for lactoferrin and no cross-reactivity was observed with transferrin, a similar non-heme, iron-binding glycoprotein. Human lactoferrin specifically reacted with anti-mouse lactoferrin, but the binding was approximately 8000 times weaker than observed with mouse lactoferrin. Values for lactoferrin in milk and bone marrow granulocytes were obtained which agreed with levels obtained using other methods.

Animals↗
PubMed2026

Apoptosis protein markers in comorbid type 2 diabetes mellitus and depression; relationships with cognitive performance, incident dementia, and white matter hyperintensities.

Type 2 diabetes mellitus (T2DM) and major depressive disorder (MDD) are reciprocal risk factors, and both elevate dementia risk. Dysregulation of programmed cell death is implicated in T2DM, MDD, and neurodegeneration, but proteomic markers of apoptosis have yet to be studied as dementia predictors in people with T2DM and/or MDD. This study examines apoptosis markers in comorbid T2DM and MDD, and their associations with cognitive, dementia, and neuroimaging outcomes. The retrospective sample (n = 15,765) consisted of UK Biobank participants (MDD only n = 1230; T2DM only n = 3644; comorbid T2DM + MDD n = 721). Individuals with T2DM + MDD comorbidity had poorer cognitive performance, and a higher 15-year dementia incidence (HR = 4.44, 95% CI = [3.23,6.11]). Among 60 apoptosis-related proteins identified by Kyoto Encyclopedia of Genes and Genomes pathway enrichment, 41 were significantly up-regulated in comorbid T2DM + MDD relative to controls, and 4 were higher in the comorbid group than both T2DM alone and MDD alone. Tumor necrosis factor ligand superfamily member 10 (TNFSF10), growth arrest and DNA damage-inducible protein GADD45 beta, tumor necrosis factor ligand superfamily member 6, and RAC-gamma serine/threonine-protein kinase were associated with dementia risk. Nine proteins (e.g. apoptosis-inducing factor 1, mitochondrial, caspase-2, mitogen-activated protein kinase kinase kinase 5, TNFSF10), were associated with white matter hyperintensity volumes in comorbid T2DM + MDD after FDR correction, but none were associated with cognitive performance, atrophy, or white matter microstructural changes. These findings identify peripheral apoptosis markers that were further elevated in comorbid T2DM + MDD compared to either alone, pointing to an important pathophysiological element underlying adverse outcomes in the context of mood and metabolic comorbidity.

Humans↗
PubMed1978

I. An ultrastructural investigation on erythrocytes and lymphocytes coated with proteins: use of CrCl3 as an electron-dense marker.

Proteins (human immunoglobulin G and protein A of Staphylococcus aureus) coupled to the surface of erythrocytes (sheep, mice, man and chicken) and to mouse spleen lymphocytes by chromic chloride technique acquire electron-dense properties and may be visualized in electron microscopy. Sheep red blood cells coated with rabbit anti-erythrocyte antibodies and treated with chromic chloride showed continuous electron-opaque labelling of the cell membrane due to chelation of rabbit IgG with chromium atoms.

Animals↗