Abstract
Synthesis and secretion of avidin was studied in cultured chicken embryo fibroblasts infected with transforming retroviruses (Rous sarcoma virus, its mutants temperature-sensitive for transformation, OK-10 virus) or a nontransforming retrovirus (RAV-1). Avidin was detectable in both transformed and untransformed cultures, and was identical to chicken egg white avidin by several criteria: biotin-binding, heat-induced biotin exchange, subunit size (mol. wt. 15 600), immunoprecipitation of metabolically labeled proteins and immunoblotting. Transformation increased the production of avidin up to 50-fold, but several experiments suggested that the induction was not a direct consequence of virus-induced cell transformation. The production of avidin seemed to relate to cellular damage both in cultures of virus-transformed and of normal fibroblasts. It may represent a response to cellular damage and viral transformation may activate the process.
Full text
PDF




Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Biquard J. M., Vigier P. Characteristics of a conditional mutant of Rous sarcoma virus defective in ability to transform cells at high temperature. Virology. 1972 Feb;47(2):444–455. doi: 10.1016/0042-6822(72)90280-2. [DOI] [PubMed] [Google Scholar]
- Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
- Elo H. A., Räisänen S., Tuohimaa P. J. Induction of an antimicrobial biotin-binding egg white protein (avidin) in chick tissues in septic Escherichia coli infection. Experientia. 1980 Mar 15;36(3):312–313. doi: 10.1007/BF01952296. [DOI] [PubMed] [Google Scholar]
- GREEN N. M. AVIDIN. 3. THE NATURE OF THE BIOTIN-BINDING SITE. Biochem J. 1963 Dec;89:599–609. doi: 10.1042/bj0890599. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Green N. M. Avidin. Adv Protein Chem. 1975;29:85–133. doi: 10.1016/s0065-3233(08)60411-8. [DOI] [PubMed] [Google Scholar]
- Green N. M. Evidence for a genetic relationship between avidins and lysozymes. Nature. 1968 Jan 20;217(5125):254–256. doi: 10.1038/217254a0. [DOI] [PubMed] [Google Scholar]
- Groudine M., Weintraub H. Activation of cellular genes by avian RNA tumor viruses. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5351–5354. doi: 10.1073/pnas.77.9.5351. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Groudine M., Weintraub H. Rous sarcoma virus activates embryonic globin genes in chicken fibroblasts. Proc Natl Acad Sci U S A. 1975 Nov;72(11):4464–4468. doi: 10.1073/pnas.72.11.4464. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hammarström S., Samuelsson B., Bjursell G. Prostaglandin levels in normal and transformed baby-hamster-kidney fibroblasts. Nat New Biol. 1973 May 9;243(123):50–51. [PubMed] [Google Scholar]
- Hatanaka M. Transport of sugars in tumor cell membranes. Biochim Biophys Acta. 1974 Apr 29;355(1):77–104. doi: 10.1016/0304-419x(74)90008-0. [DOI] [PubMed] [Google Scholar]
- Hertz R., Fraps R. M., Sebrell W. H. ENDOCRINOLOGICAL ASPECTS OF AVIDIN FORMATION IN THE AVIAN OVIDUCT. Science. 1944 Jul 14;100(2585):35–36. doi: 10.1126/science.100.2585.35. [DOI] [PubMed] [Google Scholar]
- Hsu S. M., Raine L., Fanger H. Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures. J Histochem Cytochem. 1981 Apr;29(4):577–580. doi: 10.1177/29.4.6166661. [DOI] [PubMed] [Google Scholar]
- Kawai S., Hanafusa H. The effects of reciprocal changes in temperature on the transformed state of cells infected with a rous sarcoma virus mutant. Virology. 1971 Nov;46(2):470–479. doi: 10.1016/0042-6822(71)90047-x. [DOI] [PubMed] [Google Scholar]
- Korpela J., Kulomaa M., Tuohimaa P., Vaheri A. Induction of avidin in chickens infected with the acute leukemia virus OK 10. Int J Cancer. 1982 Oct 15;30(4):461–464. doi: 10.1002/ijc.2910300412. [DOI] [PubMed] [Google Scholar]
- Kulomaa M. S., Elo H. A., Niemelä A. O., Tuohimaa P. J. Similarity of biotin-binding activity and immunoreactivity in chicken oviduct and non-oviduct avidin. Biochim Biophys Acta. 1981 Sep 29;670(2):207–213. doi: 10.1016/0005-2795(81)90011-8. [DOI] [PubMed] [Google Scholar]
- Kulomaa M. S., Elo H. A., Tuohimaa P. J. A radioimmunoassay for chicken avidin. Comparison with a [14C]biotin-binding method. Biochem J. 1978 Nov 1;175(2):685–690. doi: 10.1042/bj1750685. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Langer P. R., Waldrop A. A., Ward D. C. Enzymatic synthesis of biotin-labeled polynucleotides: novel nucleic acid affinity probes. Proc Natl Acad Sci U S A. 1981 Nov;78(11):6633–6637. doi: 10.1073/pnas.78.11.6633. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mandella R. D., Meslar H. W., White H. B., 3rd Relationship between biotin-binding proteins from chicken plasma and egg yolk. Biochem J. 1978 Nov 1;175(2):629–633. doi: 10.1042/bj1750629. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Meslar H. W., Camper S. A., White H. B., 3rd Biotin-binding protein from egg yolk. A protein distinct from egg white avidin. J Biol Chem. 1978 Oct 10;253(19):6979–6982. [PubMed] [Google Scholar]
- Nordback I., Wigham T., Kulomaa M., Tuohimaa P. Progesterone-independent avidin in chick oviduct fibroblast culture. Endocrinology. 1981 Aug;109(2):596–601. doi: 10.1210/endo-109-2-596. [DOI] [PubMed] [Google Scholar]
- O'Malley B. W., McGuire W. L., Kohler P. O., Korenman S. G. Studies on the mechanism of steroid hormone regulation of synthesis of specific proteins. Recent Prog Horm Res. 1969;25:105–160. doi: 10.1016/b978-0-12-571125-8.50006-5. [DOI] [PubMed] [Google Scholar]
- Pfeifer S., Kallio A., Vaheri A., Pettersson R., Oker-Blom N. Stable bone-marrow-derived cell line producing transforming avian acute leukemia virus OK 10. Int J Cancer. 1980 Feb 15;25(2):235–242. doi: 10.1002/ijc.2910250211. [DOI] [PubMed] [Google Scholar]
- Pfeifer S., Pettersson R. F., Kallio A., Oker-Blom N., Vaheri A. Avian acute leukemia virus OK10 has an 8.2-kilobase genome and modified glycoprotein gp 78. J Virol. 1981 Nov;40(2):533–540. doi: 10.1128/jvi.40.2.533-540.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pfeifer S., Zabielski J., Ohlsson R., Frykberg L., Knowles J., Pettersson R., Oker-Blom N., Philipson L., Vaheri A., Vennström B. Avian acute leukemia virus OK 10: analysis of its myc oncogene by molecular cloning. J Virol. 1983 May;46(2):347–354. doi: 10.1128/jvi.46.2.347-354.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schönhöfer P. S., Rücker W., Dembinska-Kiec A., Peters H. D., Peskar B. A., von Figura K. Prostaglandins and fibroblast functions in vitro. Agents Actions Suppl. 1979;(5):39–51. [PubMed] [Google Scholar]
- Thomas D. R., Philpott G. W., Jaffe B. M. The relationship between concentration of prostaglandin E and rates of cell replication. Exp Cell Res. 1974 Mar 15;84(1):40–46. doi: 10.1016/0014-4827(74)90377-2. [DOI] [PubMed] [Google Scholar]
- Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vaheri A., Mosher D. F. High molecular weight, cell surface-associated glycoprotein (fibronectin) lost in malignant transformation. Biochim Biophys Acta. 1978 Sep 18;516(1):1–25. doi: 10.1016/0304-419x(78)90002-1. [DOI] [PubMed] [Google Scholar]
- Vaheri A., Ruoslahti E. Disappearance of a major cell-type specific surface glycoprotein antigen (SF) after transformation of fibroblasts by Rous sarcoma virus. Int J Cancer. 1974 May 15;13(5):579–586. doi: 10.1002/ijc.2910130502. [DOI] [PubMed] [Google Scholar]
- Vartio T., Zardi L., Balza E., Towbin H., Vaheri A. Monoclonal antibodies in analysis of cathepsin G-digested proteolytic fragments of human plasma fibronectin. J Immunol Methods. 1982 Dec 30;55(3):309–318. doi: 10.1016/0022-1759(82)90090-4. [DOI] [PubMed] [Google Scholar]
- White H. B., 3rd, Dennison B. A., Della Fera M. A., Whitney C. J., McGuire J. C., Meslar H. W., Sammelwitz P. H. Biotin-binding protein from chicken egg yolk. Assay and relationship to egg-white avidin. Biochem J. 1976 Aug 1;157(2):395–400. doi: 10.1042/bj1570395. [DOI] [PMC free article] [PubMed] [Google Scholar]


