Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Reexamination Certificate
2003-04-11
2004-03-30
Saidha, Tekchand (Department: 1652)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
C435S193000, C435S252300, C435S320100, C536S023200
Reexamination Certificate
active
06713283
ABSTRACT:
BACKGROUND
The present invention is related to tyrosylprotein sulfotransferases and polynucleotides which encode said tyrosylprotein sulfotransferases and methods of use thereof.
Tyrosine O-sulfation is a post-translation modification of membrane and secretory proteins that occurs in all multicellular eukaryotes (1-3). The enzyme required for this reaction, called tyrosylprotein sulfotransferase (TPST), catalyzes the transfer of sulfate from 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to tyrosines within highly acidic motifs of polypeptides (2,4). Evidence has previously indicated that the enzyme is a membrane-associated protein with a lumenally oriented active site localized in the trans-Golgi network (5,6).
Many proteins have been shown to contain tyrosine sulfate. Among these are several proteins involved in inflammation and hemostasis, including PSGL-1 (7), the &agr;-chain of complement factor C4 (8), coagulation Factors V (9) and VIII (10,11), platelet glycoprotein Ib&agr; (12,13), &agr;
2
-antiplasmin (14), and heparin cofactor II (15). Although the role of tyrosine O-sulfation is incompletely understood, it is clear that tyrosine O-sulfation plays a role in protein-protein interactions in several systems. Tyrosine O-sulfation is required for the optimal interaction between Factor VIII and Von Willebrand factor (10,11), PSGL-1 and P-selectin (7), GPIba with Von Willebrand factor and &agr;-thrombin (12,13), and complement factor C4 and C1s (8).
The kinetics of the TPST reaction has been studied using crude and partially-purified enzyme preparations from a variety of mammalian tissues (18,19). However, it has not been clear whether TPST activity is due to one enzyme or a family of enzymes. Two groups have previously reported attempts to purify TPST (20,21). However, neither group was able to sufficiently purify the protein to identify its amino acid sequence, nor have cDNAs encoding the enzyme previously been identified. As a result, there has remained a need in the field for complete identification of TPST and of cDNAs encoding TPST.
REFERENCES:
patent: 5032519 (1991-07-01), Paulson et al.
patent: 5541095 (1996-07-01), Hirschberg et al.
patent: 5714594 (1998-02-01), Weinshilboum et al.
patent: 5728819 (1998-03-01), Jacobs et al.
patent: 6060295 (2000-05-01), Moore
patent: 6071732 (2000-06-01), Moore
patent: 6204016 (2001-03-01), Moore
patent: 6207414 (2001-03-01), Moore
patent: 6207432 (2001-03-01), Moore
patent: 9732889 (1997-09-01), None
Kakuta et al., “Conserved Structural Motifs In the Sulfotransferase Family”,TIBS23:129-130, Apr. 1998.
Niehrs et al., “Protein Tyrosine Sulfation, 1993—An Update”,Chemico-Biological Interactions92:257-271, 1994.
Baeuerle et al., “Tyrosine Sulfation Is a trans-Golgi-Specific Protein Modification”,The Journal of Cell Biology105(6):2655-2664, Dec. 1987.
Rens-Domiano et al., “Characterization of Tyrosylprotein Sulfotransferase From Rat Liver And Other Tissues”,The Journal of Biologica Chemistry, 264(2):899-905, Jan. 15, 1989.
Niehrs et al., “Analysis Of The Substrate Specificity Of Tyrosylprotein Sulfotransferase Using Synthetic Peptides”,The Journal of Biological Chemistry, 265(15):8525-8532, May 25, 1990.
Lin et al., “Recognition Of Substrates By Tyrosylprotein Sulfotransferase”,The Journal of Biological Chemistry, 267(5):2876-2879, Feb. 15, 1992.
Huttner et al., “Protein Sulfation On Tyrosine”,Modern Cell Biology, 6:97-140, 1988.
William et al., “Purification Of Tyrosylprotein Sulfotransferase From Rat Submandibular Salivary Glands”,Archives of Biochemistry and Biophysics, 338(1):90-96, Feb. 1, 1997.
Niehrs et al., “Purification And Characterization Of Tyrosylprotein Sulfotransferase”,The EMBO Journal, 9(1):35-42, 1990.
Lin et al., “Characterization of a Tyrosylprotein Sulfotransferase in Human Liver,”Biochem Parmacol., 40(3):629-635, Aug. 1, 1990.
Hilbert et al., “Cloning and Expression of the cDNA Encoding the Human Homologue of the DNA Repair Enzyme,Escherichia coliEndonuclease III,”Journal of Biological Chemistry, 272(10):6733-6740, Mar. 7, 1997.
Database EMEST 15, EMBL Databases, Accession No. AA445921, Hilleier et al., “Homo sapienscDNA clone 774175 5′ Similar to WP:F42G9.8,” XP002111846, Jun. 5, 1997.
Niehrs et al., “Conversion of Recombinant Hirudin to the Natural Form by In Vitro Tyrosine Sulfation. Differential Substrate Specificities of Leech and Bovine Tyrosylprotein Sulfotransferases,”Journal of Biological Chemistry, 265(16):9314-9318, Jun. 5, 1990.
Wilkins et al., “Tyrosine Sulfation of P-selectin Glycoprotein Ligand-1 is Required for High Affinity Binding to P-selectin,”Journal of Biological Chemistry, 270(39):22677-22680, Sep. 29, 1995.
Friederich et al., “Inhibition of Tyrosine Sulfation in the Trans-Golgi Retards the Transport of a Constitutively Secreted Protein to the Cell Surface,”The Journal of Cell Biology, 107(5):1655-1667, Nov. 5, 1988.
Database EMEST16, EMBL Databases, Accession No: AA187441, Jan. 19, 1997, Hillier et al., “Homo sapienscDNA Clone 625544 5′ Similar to WP:F42G9.8 CE07235”, XP002126066.
Database EMEST 20, EMBL Databases, Accession No: AA183558, Feb. 16, 1997, Marra et al., “Mus Musculus cDNA Clone 567635 5′ Similar to WP:F42G9.8 CE07235”, XP002126067.
Ouyang et al., “Tyrosylprotein Sulfotransferase: Purification and Molecular Cloning of an Enzyme that Catalyzes Tyrosine O-Sulfation, a Common Postranslational Modification of Eukaryotic Proteins,”Proceedings of the National Academy of Sciences of USA, 95(19):11134-11139, Sep. 15, 1998.
Database EHHUM1, EMBL Databases, Accession No.: AF061254, May 6, 1998, Beisswanger et al.,Homo sapiensTyrosylprotein Sulfotransferase-2 mRNA, Complete CDS, EP002126086.
Database EMHUM1, EMBL Databases, Accession No.: Aj006198, Jun. 23, 1998, E. Bennett,Homo SapiensmRNA for Tyrosyl Sulfotransferase-2, XP002126068.
Database TRINV, EMBL Databases, Accession No.: Q20351, Nov. 1, 1996, Wilson et al., “COSMID F42G9.8,” XP002126069.
Database EMHUM1, EMBL Databases, Accession No.: Z95115, Apr. 30, 1997, A. Bridgeman, “Human DNA Sequence From BAC 445C9 on Chromosome 22q12.1,” EP002126070.
Database EMEST18, EMBL Databases, Accession No,: AA277588, Apr. 2, 1997, Marra et al., “Soares Mouse NML Mus Musculus cDNA Clone 737385 5′ Similar to WP:F42G9.8 CE07235,” XP002126071.
Database EMEST 10, EMBL Databases, Accession No.: C09275, Sep. 13, 1996, Y Kohara, “C. elegans cDNA Clone yk166cl: 5′ End, Single Read,” XP002126072.
PCT Search Report of PCT/US99/01756.
Wilson et al., “2.2 Mb of contiguous nucleotide sequence from chromosome III ofC. elegans,” Naturevol. 368, pp. 32-38, Mar. 3, 1994.
Freiberg et al., “Molecular basis of symbiosis between Rhizobium and legumes,”Nature, vol. 387, pp. 394-401, Mar. 22, 1997.
Dunlap Codding & Rogers P.C.
Saidha Tekchand
The Board of Regents of the University of Oklahoma
LandOfFree
Tyrosylprotein sulfotransferases does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Tyrosylprotein sulfotransferases, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Tyrosylprotein sulfotransferases will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3191592