BIOMAT Database Logo BIOMAT Database Logo

Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-sialyltransferase using lectin resistance selection. 1993

K Sasaki, and E Watanabe, and K Kawashima, and S Sekine, and T Dohi, and M Oshima, and N Hanai, and T Nishi, and M Hasegawa
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Japan.

This report describes the isolation of a cDNA encoding a novel human Gal beta (1-3/1-4)GlcNac alpha 2,3-sialyl-transferase involved in the biosynthesis of the sialyl Lewis x determinant (NeuAc alpha 2-3 Gal beta 1-4(Fuc alpha 1-3)GlcNAc). A cDNA library of the human melanoma cell line WM266-4 was constructed in an Epstein-Barr virus-based cloning vector. Selection of the B-cell line Namalwa expressing transfected cDNAs in the presence of the cytotoxic lectin Ricinus communis agglutinin 120 gave a cDNA encoding a protein with type II transmembrane topology, as found for mammalian glycosyltransferases. The use of this lectin, which is specific to galactose residues (especially the Gal beta 1-4GlcNAc structure), originates from our prediction that the modification of the Gal beta 1-4GlcNAc structure (a backbone of the sialyl Lewis x structure) by glycosyltransferases may increase the levels of resistance to this lectin. Comparison of this cDNA sequence with those of three other cloned sialyltransferases revealed two conserved regions shared by all four enzymes. Expression of the COOH-terminal catalytic domain of this protein showed alpha 2,3-sialyltransferase activity with substrate specificity different from that of CMP-N-acetylneuraminate:N-acetyllactosaminide alpha-2,3-sialyltransferase (Gal-beta 1-3(4)GlcNAc alpha 2,3-sialyltransferase, EC 2.4.99.6). Furthermore, expression of this cDNA in Namalwa cells increased the level of sialyl Lewis x antigens. The cloning approach based on lectin resistance may be useful for the isolation of cDNAs encoding other mammalian glycosyltransferases.

UI MeSH Term Description Entries
D008545 Melanoma A malignant neoplasm derived from cells that are capable of forming melanin, which may occur in the skin of any part of the body, in the eye, or, rarely, in the mucous membranes of the genitalia, anus, oral cavity, or other sites. It occurs mostly in adults and may originate de novo or from a pigmented nevus or malignant lentigo. Melanomas frequently metastasize widely, and the regional lymph nodes, liver, lungs, and brain are likely to be involved. The incidence of malignant skin melanomas is rising rapidly in all parts of the world. (Stedman, 25th ed; from Rook et al., Textbook of Dermatology, 4th ed, p2445) Malignant Melanoma,Malignant Melanomas,Melanoma, Malignant,Melanomas,Melanomas, Malignant
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D002240 Carbohydrate Sequence The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS. Carbohydrate Sequences,Sequence, Carbohydrate,Sequences, Carbohydrate
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004351 Drug Resistance Diminished or failed response of an organism, disease or tissue to the intended effectiveness of a chemical or drug. It should be differentiated from DRUG TOLERANCE which is the progressive diminution of the susceptibility of a human or animal to the effects of a drug, as a result of continued administration. Resistance, Drug
D005822 Genetic Vectors DNA molecules capable of autonomous replication within a host cell and into which other DNA sequences can be inserted and thus amplified. Many are derived from PLASMIDS; BACTERIOPHAGES; or VIRUSES. They are used for transporting foreign genes into recipient cells. Genetic vectors possess a functional replicator site and contain GENETIC MARKERS to facilitate their selective recognition. Cloning Vectors,Shuttle Vectors,Vectors, Genetic,Cloning Vector,Genetic Vector,Shuttle Vector,Vector, Cloning,Vector, Genetic,Vector, Shuttle,Vectors, Cloning,Vectors, Shuttle
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000094663 beta-Galactoside alpha-2,3-Sialyltransferase Sialyltransferases that catalyze the transfer of N-ACETYLNEURAMINIC ACID from CYTIDINE MONOPHOSPHATE N-ACETYLNEURAMINIC ACID to the 3-OH of the GALACTOSE residue of N-GLYCANS. Asialofetuin Sialyltransferase,CMP N-Acetylneuraminate-beta-Galactoside alpha-2,3-Sialyltransferase,CMP-ANGS-Transferase,CMP-Acetylneuraminate-Galactoside (alpha 2-3)-Sialyltransferase,CMP-Neu5Ac-GAl beta1-3GalNAc alpha-2,3-Sialyltransferase,CMP-Neu5Ac-Gal1-3GalNAc alpha-2,3-Sialyltransferase,CMP-NeuAc-Galactoside (alpha 2-3)-Sialyltransferase,CMPSialic Acid beta-Galactosyl-1-3-N-Acetylgalactosaminide alpha 2-3-Sialyltransferase,Gal beta1,3GalNAc alpha2,3-Sialyltransferase,alpha 2-3-Sialyltransferase,beta-D-Galactoside 3-alpha-Sialyltransferase,ST3Gal I,ST3Gal II,ST3Gal III,ST3Gal IV,ST3Gal VI,alpha-2,3-ST(O),2-3-Sialyltransferase, alpha,3-alpha-Sialyltransferase, beta-D-Galactoside,CMP ANGS Transferase,CMP N Acetylneuraminate beta Galactoside alpha 2,3 Sialyltransferase,CMP Neu5Ac GAl beta1 3GalNAc alpha 2,3 Sialyltransferase,CMP Neu5Ac Gal1 3GalNAc alpha 2,3 Sialyltransferase,CMPSialic Acid beta Galactosyl 1 3 N Acetylgalactosaminide alpha 2 3 Sialyltransferase,N-Acetylneuraminate-beta-Galactoside alpha-2,3-Sialyltransferase, CMP,Sialyltransferase, Asialofetuin,alpha 2 3 Sialyltransferase,alpha-2,3-Sialyltransferase, CMP N-Acetylneuraminate-beta-Galactoside,alpha-2,3-Sialyltransferase, CMP-Neu5Ac-GAl beta1-3GalNAc,alpha-2,3-Sialyltransferase, CMP-Neu5Ac-Gal1-3GalNAc,alpha-2,3-Sialyltransferase, beta-Galactoside,beta D Galactoside 3 alpha Sialyltransferase,beta Galactoside alpha 2,3 Sialyltransferase,beta1-3GalNAc alpha-2,3-Sialyltransferase, CMP-Neu5Ac-GAl
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

K Sasaki, and E Watanabe, and K Kawashima, and S Sekine, and T Dohi, and M Oshima, and N Hanai, and T Nishi, and M Hasegawa
Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase.
July 1993, Biochemical and biophysical research communications,
K Sasaki, and E Watanabe, and K Kawashima, and S Sekine, and T Dohi, and M Oshima, and N Hanai, and T Nishi, and M Hasegawa
Determination of the specificities of rat liver Gal(beta 1-4)GlcNAc alpha 2,6-sialyltransferase and Gal(beta 1-3/4)GlcNAc alpha 2,3-sialyltransferase using synthetic modified acceptors.
July 1993, The Journal of biological chemistry,
K Sasaki, and E Watanabe, and K Kawashima, and S Sekine, and T Dohi, and M Oshima, and N Hanai, and T Nishi, and M Hasegawa
Glycolipid acceptor specificity of a human Gal beta(1-3/1-4) GlcNAc alpha 2,3-sialyltransferase.
December 1995, Biochemical and biophysical research communications,
K Sasaki, and E Watanabe, and K Kawashima, and S Sekine, and T Dohi, and M Oshima, and N Hanai, and T Nishi, and M Hasegawa
Cloning and expression of the Gal beta 1, 3GalNAc alpha 2,3-sialyltransferase.
October 1992, The Journal of biological chemistry,
K Sasaki, and E Watanabe, and K Kawashima, and S Sekine, and T Dohi, and M Oshima, and N Hanai, and T Nishi, and M Hasegawa
Molecular cloning and expression of chick Gal beta 1,3GalNAc alpha 2,3-sialyltransferase.
May 1995, Biochimica et biophysica acta,
K Sasaki, and E Watanabe, and K Kawashima, and S Sekine, and T Dohi, and M Oshima, and N Hanai, and T Nishi, and M Hasegawa
Purification of a Gal beta 1 to 4GlcNAc alpha 2 to 6 sialyltransferase and a Gal beta 1 to 3(4)GlcNAc alpha 2 to 3 sialyltransferase to homogeneity from rat liver.
November 1982, The Journal of biological chemistry,
K Sasaki, and E Watanabe, and K Kawashima, and S Sekine, and T Dohi, and M Oshima, and N Hanai, and T Nishi, and M Hasegawa
[The alpha-gal epitope (Gal alpha 1-3 Gal beta 1-4 GlcNAc-R) in xenotransplantation].
July 2003, Sheng li ke xue jin zhan [Progress in physiology],
K Sasaki, and E Watanabe, and K Kawashima, and S Sekine, and T Dohi, and M Oshima, and N Hanai, and T Nishi, and M Hasegawa
Molecular cloning and expression of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase from mouse brain.
September 1993, European journal of biochemistry,
K Sasaki, and E Watanabe, and K Kawashima, and S Sekine, and T Dohi, and M Oshima, and N Hanai, and T Nishi, and M Hasegawa
Cloning and expression of cDNA for a new type of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase.
April 1994, The Journal of biological chemistry,
K Sasaki, and E Watanabe, and K Kawashima, and S Sekine, and T Dohi, and M Oshima, and N Hanai, and T Nishi, and M Hasegawa
Release of sialyltransferases from rat liver Golgi membranes by a cathepsin D-like proteinase: comparison of the release of Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase, Gal beta 1-3(4)GlcNAc alpha 2-3 sialyltransferase and lactosylceramide alpha 2-3 sialyltransferase (SAT-1).
February 1995, Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology,
Copied contents to your clipboard!