PMID- 9266697
OWN - NLM
STAT- MEDLINE
DCOM- 19970908
LR  - 20190620
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 247
IP  - 2
DP  - 1997 Jul 15
TI  - Cloning and expression of cDNA for a human Gal(beta1-3)GalNAc 
      alpha2,3-sialyltransferase from the CEM T-cell line.
PG  - 558-66
AB  - Complementary DNA encoding a human Gal(beta1-3)GalNAc alpha2,3-sialyltransferase 
      type II (hST3Gal II) was cloned from a CEM T-cell cDNA library using a 23-base 
      oligonucleotide probe. The sequence of this probe was established on the basis of 
      a slightly divergent sialylmotif L that was obtained by polymerase chain reaction 
      with degenerate oligonucleotide primers based on the conserved sialylmotif L of 
      mammalian Gal(beta1-3)GalNAc alpha2,3-sialyltransferases. It was thus confirmed 
      that a short oligonucleotide probe may be sensitive and highly specific. The 
      nucleotide and amino acid sequences of hST3Gal II show, respectively, 56.3% and 
      49.3% similarity to hST3Gal I [Kitagawa, H. & Paulson, J. C. (1994) J. Biol. 
      Chem. 269, 17872-17878] and 88.1% and 93.7% similarity to murine ST3Gal II [Lee, 
      Y. C., Kojima, N., Wada, E., Kurosawa, N., Nakaoka, T., Hamamoto, T. & Tsuji, S. 
      (1994) J. Biol. Chem. 269, 10028-10033]. hST3Gal II mRNA was highly expressed in 
      heart, liver, skeletal muscle and various lymphoid tissues but not in brain and 
      kidney. A soluble form of hST3Gal II expressed in COS-7 cells was tested in vitro 
      for substrate specificity and kinetic properties. Asialofetuin and asialo-bovine 
      submaxillary mucin appeared better substrates for hST3Gal II than for its murine 
      counterpart as previously reported [Kojima, N., Lee, Y.-C., Hamamoto, T., 
      Kurosawa, N. & Tsuji, S. (1994) Biochemistry 33, 5772-5776]. In previous studies, 
      we have shown hyposialylation of O-glycans attached to two major lymphocyte CD43 
      and CD45 cell surface molecules in human-immunodeficiency-virus-1(HIV-1)-infected 
      T-cell lines. Since comparable levels of hST3Gal I and hST3Gal II mRNA and 
      enzymatic activity were observed in parental and HIV-1-infected CEM T-cell 
      lysates, the sialylation defect associated with HIV infection of this cell line 
      is probably due to a mechanism different from a simple altered catalytic activity 
      of these sialyltransferases.
FAU - Giordanengo, V
AU  - Giordanengo V
AD  - Laboratoire de Virologie, Faculte de Medecine, Nice, France.
FAU - Bannwarth, S
AU  - Bannwarth S
FAU - Laffont, C
AU  - Laffont C
FAU - Van Miegem, V
AU  - Van Miegem V
FAU - Harduin-Lepers, A
AU  - Harduin-Lepers A
FAU - Delannoy, P
AU  - Delannoy P
FAU - Lefebvre, J C
AU  - Lefebvre JC
LA  - eng
SI  - GENBANK/X96667
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 0 (DNA Primers)
RN  - 0 (DNA, Complementary)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Proteins)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.6 (N-acetyllactosaminide alpha-2,3-sialyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - COS Cells
MH  - Cell Line
MH  - DNA Primers
MH  - DNA, Complementary
MH  - Humans
MH  - Kinetics
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - Polymerase Chain Reaction
MH  - RNA, Messenger/biosynthesis
MH  - Recombinant Proteins/biosynthesis/chemistry/metabolism
MH  - Sialyltransferases/biosynthesis/chemistry/*metabolism
MH  - T-Lymphocytes
MH  - Transfection
EDAT- 1997/07/15 00:00
MHDA- 1997/07/15 00:01
CRDT- 1997/07/15 00:00
PHST- 1997/07/15 00:00 [pubmed]
PHST- 1997/07/15 00:01 [medline]
PHST- 1997/07/15 00:00 [entrez]
AID - 10.1111/j.1432-1033.1997.00558.x [doi]
PST - ppublish
SO  - Eur J Biochem. 1997 Jul 15;247(2):558-66. doi: 10.1111/j.1432-1033.1997.00558.x.