Abstract
The intracellular distribution of plasminogen activator in growing, confluent, and transformed 3T3 cells was investigated by using sucrose density gradient centrifugation. In confluent cells, which do not release plasminogen activator extracellularly, most of the activity was found in a heavy membrane fraction. In growing and transformed 3T3 cells, which do release plasminogen activator extracellularly in large amounts, most of the activity was found in lighter, plasma membrane-enriched fractions. A correlation between its presence in the light membrane fractions and the ability of the cells to release the plasminogen activator extracellularly is made.
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- Avruch J., Wallach D. F. Preparation and properties of plasma membrane and endoplasmic reticulum fragments from isolated rat fat cells. Biochim Biophys Acta. 1971 Apr 13;233(2):334–347. doi: 10.1016/0005-2736(71)90331-2. [DOI] [PubMed] [Google Scholar]
- Bennett G., Leblond C. P. Formation of cell coat material for the whole surface of columnar cells in the rat small intestine, as visualized by radioautography with L-fucose-3H. J Cell Biol. 1970 Aug;46(2):409–416. doi: 10.1083/jcb.46.2.409. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bernacki R. J., Kim U. Concomitant elevations in serum sialytransferase activity and sialic acid content in rats with metastasizing mammary tumors. Science. 1977 Feb 11;195(4278):577–580. doi: 10.1126/science.835014. [DOI] [PubMed] [Google Scholar]
- Cejka J., Peterson W. E., Jr, Belamaric J., Kithier K. In vitro synthesis of beta2-microglobulin by human fetal tissues. Dev Biol. 1975 Mar;43(1):200–203. doi: 10.1016/0012-1606(75)90141-4. [DOI] [PubMed] [Google Scholar]
- Chang K. J., Bennett V., Cuatrecasas P. Membrane receptors as general markers for plasma membrane isolation procedures. The use of 125-I-labeled wheat germ agglutinin, insulin, and cholera toxin. J Biol Chem. 1975 Jan 25;250(2):488–500. [PubMed] [Google Scholar]
- Chou I. N., O'Donnell S. P., Black P. H., Roblin R. O. Cell density-dependent secretion of plasminogen activator by 3T3 cells. J Cell Physiol. 1977 Apr;91(1):31–37. doi: 10.1002/jcp.1040910104. [DOI] [PubMed] [Google Scholar]
- Deutsch D. G., Mertz E. T. Plasminogen: purification from human plasma by affinity chromatography. Science. 1970 Dec 4;170(3962):1095–1096. doi: 10.1126/science.170.3962.1095. [DOI] [PubMed] [Google Scholar]
- Devreotes P. N., Gardner J. M., Fambrough D. M. Kinetics of biosynthesis of acetylcholine receptor and subsequent incorporation into plasma membrane of cultured chick skeletal muscle. Cell. 1977 Mar;10(3):365–373. doi: 10.1016/0092-8674(77)90023-x. [DOI] [PubMed] [Google Scholar]
- Dvorak H. F., Orenstein N. S., Rypysc J., Colvin R. B., Dvorak A. M. Plasminogen activator of guinea pig basophilic leukocytes: probable localization to the plasma membrane. J Immunol. 1978 Mar;120(3):766–773. [PubMed] [Google Scholar]
- Graham J. M., Hynes R. O., Davidson E. A., Bainton D. F. The location of proteins labeled by the 125I-lactoperoxidase system in the NIL 8 hamster fibroblast. Cell. 1975 Apr;4(4):353–365. doi: 10.1016/0092-8674(75)90156-7. [DOI] [PubMed] [Google Scholar]
- HELMKAMP R. W., GOODLAND R. L., BALE W. F., SPAR I. L., MUTSCHLER L. E. High specific activity iodination of gamma-globulin with iodine-131 monochloride. Cancer Res. 1960 Nov;20:1495–1500. [PubMed] [Google Scholar]
- Jones P. A., Laug W. E., Benedict W. F. Fibrinolytic activity in a human fibrosarcoma cell line and evidence for the induction of plasminogen activator secretion during tumor formation. Cell. 1975 Oct;6(2):245–252. doi: 10.1016/0092-8674(75)90015-x. [DOI] [PubMed] [Google Scholar]
- Kaplan J., Moskowitz M. Studies on the turnover of plasma membranes in cultured mammalina cells. I. Rates of synthesis and degradation of plasma membrane proteins and carbohydrates. Biochim Biophys Acta. 1975 May 6;389(2):290–305. doi: 10.1016/0005-2736(75)90322-3. [DOI] [PubMed] [Google Scholar]
- Knipe D. M., Baltimore D., Lodish H. F. Maturation of viral proteins in cells infected with temperature-sensitive mutants of vesicular stomatitis virus. J Virol. 1977 Mar;21(3):1149–1158. doi: 10.1128/jvi.21.3.1149-1158.1977. [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]
- LaMont J. T., Gammon M. T., Isselbacher K. J. Cell-surface glycosyltransferases in cultured fibroblasts: increased activity and release during serum stimulation of growth. Proc Natl Acad Sci U S A. 1977 Mar;74(3):1086–1090. doi: 10.1073/pnas.74.3.1086. [DOI] [PMC free article] [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]
- Lodish H. F., Small B. Membrane proteins synthesized by rabbit reticulocytes. J Cell Biol. 1975 Apr;65(1):51–64. doi: 10.1083/jcb.65.1.51. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Loskutoff D. J., Edgington T. E. Synthesis of a fibrinolytic activator and inhibitor by endothelial cells. Proc Natl Acad Sci U S A. 1977 Sep;74(9):3903–3907. doi: 10.1073/pnas.74.9.3903. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Morrison T. G. Site of synthesis of membrane and nonmembrane proteins of vesicular stomatitis virus. J Biol Chem. 1975 Sep 10;250(17):6955–6962. [PubMed] [Google Scholar]
- Olden K., Yamada K. M. Mechanism of the decrease in the major cell surface protein of chick embryo fibroblasts after transformation. Cell. 1977 Aug;11(4):957–969. doi: 10.1016/0092-8674(77)90307-5. [DOI] [PubMed] [Google Scholar]
- Ossowski L., Unkeless J. C., Tobia A., Quigley J. P., Rifkin D. B., Reich E. An enzymatic function associated with transformation of fibroblasts by oncogenic viruses. II. Mammalian fibroblast cultures transformed by DNA and RNA tumor viruses. J Exp Med. 1973 Jan 1;137(1):112–126. doi: 10.1084/jem.137.1.112. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Quigley J. P. Association of a protease (plasminogen activator) with a specific membrane fraction isolated from transformed cells. J Cell Biol. 1976 Nov;71(2):472–486. doi: 10.1083/jcb.71.2.472. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rifkin D. B., Loeb J. N., Moore G., Reich E. Properties of plasminogen activators formed by neoplastic human cell cultures. J Exp Med. 1974 May 1;139(5):1317–1328. doi: 10.1084/jem.139.5.1317. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Robin R., Chou I. N., Black P. H. Proteolytic enzymes, cell surface changes, and viral transformation. Adv Cancer Res. 1975;22:203–260. doi: 10.1016/s0065-230x(08)60178-5. [DOI] [PubMed] [Google Scholar]
- Roblin R. O., Young P. L., Bell T. E. Concomitant secretion by transformed SVWI38-VA13-2RA cells of plasminogen activator(s) and substance (s) which prevent their detection. Biochem Biophys Res Commun. 1978 May 15;82(1):165–172. doi: 10.1016/0006-291x(78)90591-0. [DOI] [PubMed] [Google Scholar]
- Unkeless J., Dano K., Kellerman G. M., Reich E. Fibrinolysis associated with oncogenic transformation. Partial purification and characterization of the cell factor, a plasminogen activator. J Biol Chem. 1974 Jul 10;249(13):4295–4305. [PubMed] [Google Scholar]
- Vitetta E. S., Uhr J. W. Immunoglobulins and alloantigens on the surface of lymphoid cells. Biochim Biophys Acta. 1975 Jun 30;415(2):253–271. doi: 10.1016/0304-4157(75)90004-0. [DOI] [PubMed] [Google Scholar]
- Wigler M., Weinstein I. B. Tumour promotor induces plasminogen activator. Nature. 1976 Jan 22;259(5540):232–233. doi: 10.1038/259232a0. [DOI] [PubMed] [Google Scholar]
- Young R. W. Renewal systems in rods and cones. Ann Ophthalmol. 1973 Aug;5(8):843–854. [PubMed] [Google Scholar]
