Expression system for the secretion of intracellular proteins

Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C435S069100, C435S252300, C435S320100, C435S471000

Reexamination Certificate

active

06881832

ABSTRACT:
Mammalian signal peptides can be used to aid in the secretion of mammalian proteins that are normally not secreted. By inactivating signals normally present in the 3′ UTRs of mRNAs encoding proteins that are normally not secreted from mammalian cells, the proportion of such mRNA molecules directed to free and cytoskeletal bound polysomes can be reduced.

REFERENCES:
patent: 0 226 057 (1988-05-01), None
patent: 0 266 057 (1988-05-01), None
patent: 0 279 582 (1988-08-01), None
patent: 0 279 582 (1988-08-01), None
patent: WO 9113151 (1991-09-01), None
patent: WO 9304165 (1993-03-01), None
Scott FL et al. J. Biol. Chem. 271(3):1605-1612, 1996.*
Sleep D et al. (Biotechnology 8(1):42-46, 1990.*
Kordula T., et al. Biochem J. 293:187-193, 1993.*
Smith DB and Johnson KS. Gene 67:31-40, 1988.*
Demolder, J., et al., “Efficient synthesis of secreted murine interleukin-2 bySaccharomyces cerevisiae: influence of 3′-untranslated regions and codon usage,”Elsevier Science Publishers B. V., Gene111 207-213, (1992).
Yang, C., et al., “The Expression and Characterization of Human Recombinant Proinsulin-Like Growth Factor II and a Mutant That Is Defective in the O-Glycosylation of Its E Domain,”Endocrinology USA 137:2766-2773, The Endocrine Society, (1996).
Lia, Y., et al., “Processing of fusion protein by endoprotease in COS-1 cells for secretion of mature peptide by using a chimeric expression vector,”Proc. Natl. Acad. Sci. USA 90:8957-8961, National Academy Science, (1993).
Aviv, H. et al., “Biosynthesis and Stability of Globin mRNA in Cultured Erythroleukemic Friend Cells,”Cell 8:495-503 (1976).
Blobel, G. and Dobberstein, B., “Transfer of Proteins Across Membranes: I. Presence of Proteolytically Processed and Unprocessed Nascent Immunoglobuin Light Chains On Membrane-Bound Ribosomes of Murine Myeloma,”J. Cell Biol. 67:835-851 (1975).
Bock, S.C. et al., “Cloning and expression of the cDNA for human antithrombin III,”Nucl. Acids Res. 10:8113-8125 (1982).
Bonnieu, A. et al., “Sequence Determinants of c-myc mRNA Turn-over: Influence of 3′ and 5′ Non-coding Regions,”Oncogene Res. 3:155-166 (1988).
Bonnieu, A. et al., “AUUUA motifs are dispensable for rapid degradation of the mouse c-myc RNA,”Oncogene 5:1585-1588 (1990).
Devlin, J. et al., “Expression of Granulocyte Colony-Stimulating Factor by Human Cell Lines,”J. Leukoc. Biol. 41:302-306 (1987).
Garcia, C.K. et al., “Molecular Characterization of a Membrane Transporter for Lactate, Pyruvate, and Other Monocarboxylates: Implications for the Cori Cycle,”Cell 76:865-873 (1994).
Hesketh, J. et al., “Targeting of c-myc and β-globin coding sequences to cytoskeletal-bound polysomes by c-myc 3′ untranslated region,”Biochem. J. 298:143-148 (1994).
Hesketh, J.E., “Intracellular Sorting of Macromolecules,”Biochem. Soc. Trans. 24:521-527 (1996).
Hovland, R. et al., “The mRNAs for cyclin A, c-myc and ribosomal proteins L4 and S6 are associated with cytoskeletal-bound polysomes in HepG2 cells,”Biochem. J. 310:193-196 (1995).
Hovland, R. et al., “The Compartmentalization of Protein Synthesis: Importance of Cytoskeleton and Role in mRNA Targeting,”Int. J. Biochem. Cell Biol. 28:1089-1105 (1996).
Huang, Z.-M. and Yen, T.S.B., “Hepatitis B Virus RNA Element That Facilitates Accumulation of Surface Gene Transcripts in the Cytoplasm,”J. Virol. 68:3193-3199 (1994).
Kim, Y.-J. et al., “Molecular Cloning and Expression of Human Galβ1,3GalNAc α2,3-Sialytransferase (hST3Gal II),”Biochem. Biophys. Res. Commun. 228:324-327 (1996).
Kislauskis, E.H. et al., “Sequences Responsible for Intracellular Localization of β-Actin Messenger RNA Also Affect Cell Phenotype,”J. Cell Biol. 127:441-451 (1994).
Lee, Y.-C. et al., “An Efficient Expression Vector for Extracellular Secretion in Mammalian Cells,”Mol. Cells 6:552-556 (1996).
Lin, F.-K. et al., “Monkey erythropoietin gene: cloning, expression and comparison with the human erythropoietin gene,”Gene 44:201-209 (1986).
Maeda, Y. et al., “Efficient Production of Active TNF By Albumin Signal Peptide,”Biochem. Mol. Biol. Int. 42:825-832 (1997).
Mahon, P. et al., “Localisation of metallothionein isoform mRNAs in rat hepatoma (H4) cells,”FEBS Lett. 373:76-80 (1995).
Michel, M.-L. et al., “Expression of Amplified Hepatitis B Virus Surface Antigen Genes in Chinese Hamster Ovary Cells,”Bio/Technology 3:561-566 (1985).
Pryme, I.F. et al., “Compartmentation of the Protein Synthetic Machinery of CHO Cells into Free, Cytoskeletal-bound and Membrance-bound Polysomes,”The Genetic Engineer and Biotechnologist 16:137-144 (1996).
Shak, S. et al., “Recombinant human DNase I reduces the viscosity of cystic fibrosis sputum,”Proc. Natl. Acad. Sci. USA 87:9188-9192 (1990).
Vedeler, A. et al., “The characterization of free, cytoskeletal and membrane-bound polysomes in Krebs II ascites and 3T3 cells,”Mol. Cell. Biochem. 100:183-193 (1991).
Veyrune, J.-L. et al., “A localisation signal in the 3′ untranslated region of c-myc mRNA targets c-myc mRNA and β-globin reporter sequences to the perinuclear cytoplasm and cytoskeletal-bound polysomes,”J. Cell Sci. 109:1185-1194 (1996).
Wilson, I.A. et al., “Differential localization of the mRNA of the M and B isoforms of creatine kinase in myoblasts,”Biochem. J. 308:599-605 (1995).
Zambetti, G. et al., “Targeting of a chimeric human histone fusion mRNA to membrane-bound polysomes in HeLa cells,”Proc. Natl. Acad. Sci. USA 84:2683-2687 (1987).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Expression system for the secretion of intracellular proteins does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Expression system for the secretion of intracellular proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Expression system for the secretion of intracellular proteins will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3415469

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.