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Query: UMLS:C0027651 (tumor)
 685,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Prolactin binding in ovariectomy-responsive and ovariectomy-nonresponsive carcinoma in the Wistar/Furth rat is compared. The time course of binding of prolactin at 4, 24, ad 37 degrees for mammary tumor (MTW9) coimplanted with MtTW10, a mammosomatotropic pituitary tumor (MTW9-MtT) or with MTW9 maintained with daily perphenazine injections (MTW9-P) was measured. Maximum binding to membranes of both tumors occurred at 4 degrees after about 30 hours incubation. The binding was inhibited by polypeptide hormones that possess lactogenic activity. Mammary tumors from animals maintained on perphenazine had a 4-fold greater binding capacity than did tumors from MtT-supported animals. When perphenazine therapy was halted the binding capacity of MTW9-P membranes was unaffected. This result held when MTW9-P animals were ovariectomized. Resection of MtT resulted in tumor regression, a fall to normal of serum prolactin, and a nearly 3-fold increase in prolactin binding. Scatchard plots of prolactin binding data yield an apparent affinity constant, K(a) of 1.2 X 10(9) liters/mole for both tumors.
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PMID:Prolactin binding in ovariectomy-responsive and ovariectomy-nonresponsive rat mammary carcinoma. 1 19

Mammary tumor cell growth factor(s) has been identified in extracts of platelets from both male and female rats, as well as in extracts prepared from pooled outdated human platelets. When assayed by the growth promotion of MTW9/PL rat mammary tumor cells in culture, platelet extracts alone were able to support growth 50--75% as well as whole serum. The mitogenic activity from crude human platelet lysates was shown to be trypsin sensitive, relatively stable to extremes of pH, labile to heat treatment at 70 degrees, non-dialysable, ammonium sulfate precipitable, not removed by 56 degrees charcoal treatment, and of apparent molecular weight of 30,000 to 50,000 daltons as estimated by G-100 Sephadex chromatography. The platelet derived mammary growth factor activity was not replaced or potentiated by thrombin or known hormones and growth factors such as prolactin, insulin, 17-beta-estradiol, progesterone, hydrocortisone, L-thyroxine, and mouse epidermal growth factor. The experimental report demonstrates that platelets are a rich source growth factor activity for rat epithelial mammary tumor cells, and that the activity appears to be a polypeptide(s) different from other mitogenic activities known to influence growth of mammary tissue.
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PMID:Platelet derived growth factor(s) for a hormone-responsive rat mammary tumor cell line. 3 Jul 82

A correlated morphological study, employing endocrine cell stains, immunofluorescence, and electron microscopy, was performed on biopsy specimens taken from a pancreatic tumor and liver metastases in a woman with hypoglycemic symptoms and high fasting insulin levels. The study revealed the tumor to be composed of two different endocrine cell populations, irrespective of the primary or metastatic growth. The first cell type fulfilled all the morphological characteristics of the islet B cells. The second was argyrophil (with the Grimelius silver method) and showed the morphological pattern of polypeptide-hormone-producing cells. With the lack of a detectable symptomatology, normal blood levels of the hormones other than insulin, and the negative results of a large number of immunofluorescence tests, we were unable to indetify the specific nature of the second type of cells.
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PMID:Endocrine tumor of the pancreas composed of argyrophil and B cells. A correlated light, immunofluorescent, and ultrastructural study. 4 81

Type C RNA viruses initially isolated from a lymphosarcoma of a gibbon ape and from a fibrosarcoma of a woolly monkey are very closely related immunologically. However, recent studies have shown that these viruses are distinguishable in a radioimmunoassay for the 12,000-molecular-weight polypeptide (p12) of the woolly monkey virus. In the present report, an immunoassay has been developed for the p12 polypeptide of the gibbon ape type C virus. This assay is shown to further distinguish the woolly monkey and gibbon ape viruses. In type-specific assays for the p12 polypeptides of these viruses, two new type C viruses isolated from gibbons in a second colony, characterized by high incidence of hemopoietic neoplasia, are immunologically distinguishable from the original gibbon ape virus. The p12 type-specific immunoassays described in the present report may be of importance in studying the natural history of these viruses and their relationship to tumors of primates.
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PMID:Antigenic characterization of type C RNA virus isolates of gibbon apes. 4 80

Purified reverse transcriptase from avian myeloblastosis virus or Rous sarcoma virus consists of two subunits of average mol wt of 100,000 and 60,000. The lower-molecular-weight subunit, alpha, has been isolated from avian myeloblastosis virus, Rous sarcoma virus and a temperature-sensitive mutant of Rous sarcoma virus, LA337. Subunit alpha manifests both the DNA polymerase and RNase H activities associated with purified reverse transcriptase of avian RNA tumor viruses. The thermal inactivation of these enzymatic activities of alpha subunit from the wild-type virus. The results show that both DNA polymerase and RNase H activities associated with the alpha subunit of LA337 are five to seven times more thermolabile then the corresponding alpha subunit from the wild-type virus. It is concluded that (i) both the polymerase and nuclease activities reside on the same polypeptide chain, and (ii) at least the lower-molecular-weight subunit alpha is coded for by the viral RNA.
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PMID:Studies on reverse transcriptase of RNA tumor viruses. I. Localization of thermolabile DNA polymerase and RNase H activities on one polypeptide. 4 81

Radioimmunoassays were developed for the 19,000, 15,000, and 12,000 molecular weight polypeptides of avian myeloblastosis virus and for the 19,000 and 12,000 polypeptides of RAV-0, a subgroup E avian tumor virus. Each polypeptide was shown to possess both group- and type-specific antigenic determinants, in contrast to the 27,000 mol wt polypeptide, which contained only group-specific determinants. The corresponding low-molecular-weight polypeptides of subgroup A, B, and E viruses were shown to be immunologically indistinguishable. The findings that low-molecular-weight polypeptides of subgroup C and D viruses reacted very differently in immunoassays for the respective polypeptides of avian myeloblastosis virus or RAV-0 suggest that subgroups C and D may have evolved differently form subgroups A, B, and E.
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PMID:Analysis of antigenic determinants of structural polypeptides of avian type C tumor viruses. 4 60

Of a series of 97 invasive carcinomas of the cervix, 5 were found to have argyrophil tumor cells, and 3 of these 5 tumors were studied by electron microscopy. The ages of the 5 patients ranged from 36 to 49 years, with a mean age of 42.4 years. The morphologic features of these five tumors were well consistent with those described on a variety of endocrine polypeptide neoplasms such as thyroid medullary carcinomas, carcinoids, pancreatic islet-cell tumors, and oat cell carcinomas of the lung. Microscopically, the 5 tumors were characterized by the formation of solid-sheets, ribbons, streams, and rosettes. They were characterized electron microscopically by the presence of neurosecretory-type granules, the abundance of intracytoplasmic microfilaments, the absence of tonofibrils, and the paucity of desmosomal attachments. On the basis of the microscopic, electron microscopic and cytochemical characteristics, it is suggested that the tumors are a specific type of cervical carcinoma derived from the argyrophil cells, normally found among the linings of the endocervical glands and the cervical squamous epithelium. We believe these 5 tumors should be regarded as an endocrine tumor, another member of apudomas.
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PMID:Argyrophil cell carcinomas (apudomas) of the uterine cervix. Light and electron microscopic observations of 5 cases. 5 Jun 65

Here we describe the 500-fold purification of an mRNA encoding an immunoglobulin lambda light chain derived from the mouse myeloma tumor, RPC-20. Purification involves the isolation of membrane-bound polysomes, oligo(dT)-cellulose chromatography, and sucrose gradient centrifugation under conditions favoring denaturation of polynucleotide complexes. The mRNA purified in this way directs the cell-free synthesis of a polypeptide which is five or six amino acids longer than the mature form of RPC-20 light chain. In addition to directing the synthesis of a precursor-like polypeptide, the mRNA migrates on electrophoresis as a band containing approximately 1150 nucleotides, about 500 more than required to encode the mature form of the light chain.
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PMID:Purification and translation of an immunoglobulin lambda chain messenger RNA from mouse myeloma. 5 5

The purification of a blocking factor from the sera of tumor-bearing mice is described. Whole serum with blocking activity-the ability to inhibit specific cell-mediated anti-tumor immunity in microcytotoxicity tests-was fractionated on immunoadsorbent columns containing Sepharose-bound syngeneic normal mouse immunoglobulins and immunoglobulins from tumor-immune donors. The blocking serum was derived from mice which had carried a transplanted methylocholanthrene-induced sarcoma for 21 to 28 days. Elution of the immunoadsorbents recovered the blocking activity in a single fraction. This fraction was blocking activity in a single fraction. This fraction was radiolabeled and analyzed by SDS gel electrophoresis and Sephadex G-200 column chromatography. The active component of the blocking serum was shown to be a polypeptide of m.w. 56,000. Specificity testing implied that the factor was likely to be either tumor antigen or an antigen-specific suppressor molecule.
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PMID:Purification and partial characterization of a tumor-specific blocking factor from sera of mice with growing chemically induced sarcomas. 6 92

Rauscher leukemia virus RNA-directed DNA polymerase has been purified to near homogeneity (greater than 90% pure) using affinity chromatography on polycytidylate-agarose with over 85% recovery of input enzymatic activity. The purified enzyme has a molecular weight of approximately 70,000 and appears to consist of a single polypeptide chain. The enzyme is free of DNase, but has RNase H activity. Analysis of the requirements for optimal rates of DNA synthesis by this enzyme using synthetic and natural template-primers has revealed template-specific variations in such requirements. During these studies it was observed that DNA synthesis catalyzed by Rauscher leukemia virus DNA polymerase is inhibited by the addition of inorganic phosphate. An analysis of the mechanism of phosphate inhibition was carried out using the synthetic template-primer poly(A)-(dT)10. It appears that by some mechanism, possibly involving the substrate binding site of the enzyme, phosphate ions inhibit DNA synthesis with a more acute effect on the rate of chain growth than on that of initiation. The extension of these studies to DNA synthesis catalyzed by a variety of mammalian type C viral reverse transcriptases revealed that low levels ( less than or equal to 2 mM) of inorganic phosphate strongly inhibited DNA synthesis. The susceptibility to phosphate inhibition appears unique to mammalian type C viral enzymes since the type B viral enzyme, Escherichia coli DNA polymerase I, avian myeloblastosis virus and Mason Pfizer monkey tumor virus reverse transcriptase and cellular DNA polymerases alpha and gamma are not inhibited by inorganic phosphate. This phenomenon of phosphate inhibition of various DNA polymerases, therefore, provides a new basis for the differentiation of the sources and nature of these enzymes.
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PMID:Purification and properties of Rauscher leukemia virus DNA polymerase and selective inhibition of mammalian viral reverse transcriptase by inorganic phosphate. 6 68


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