Tissue-specific expression of beta-galactoside alpha-2,6-sialyltransferase. Transcript heterogeneity predicts a divergent polypeptide - PubMed (original) (raw)
. 1989 Oct 15;264(29):17389-94.
Affiliations
- PMID: 2793863
Free article
Tissue-specific expression of beta-galactoside alpha-2,6-sialyltransferase. Transcript heterogeneity predicts a divergent polypeptide
T P O'Hanlon et al. J Biol Chem. 1989.
Free article
Abstract
The beta-galactoside alpha-2,6-sialyltransferase represents a member of a family of sialyltransferases which catalyze the terminal addition of sialic acid to maturing carbohydrate chains. We surveyed rat tissues using cDNA probes complementary to coding and noncoding domains of the rat liver alpha-2,6-sialyltransferase. In addition to the expected differences in the level of sialyltransferase mRNA among the tissues, there were dramatic qualitative differences as well. Hepatic sialyltransferase probes hybridize to mRNAs of varying size on Northern blots. A tissue-dependent pattern of expression of these transcripts is documented. Evidence is presented that the multiple transcripts are generated from a common gene sequence. At least one instance of alternate splicing in the generation of the kidney sialyltransferase transcripts is predicted by S1 nuclease analysis. We report the isolation of a rat kidney cDNA clone, RKA, that substantiates this tissue-specific alternate splicing event. The RKA insert, although less than full-length, apparently encodes a polypeptide divergent from the reported hepatic alpha-2,6-sialyltransferase (1). RNA blot analysis indicates that the RKA-type transcripts represent a significant proportion of sialyltransferase RNA in rat kidney. Another class of kidney cDNA clones, RKE, is colinear with the hepatic sialyltransferase sequence. RNA blots probed for the divergent and common regions suggest that complex processing pathways are operative in the tissue-specific expression of sialyltransferase mRNA.
Similar articles
- Analysis of kidney mRNAs expressed from the rat beta-galactoside alpha 2,6-sialyltransferase gene.
O'Hanlon TP, Lau JT. O'Hanlon TP, et al. Glycobiology. 1992 Jun;2(3):257-66. doi: 10.1093/glycob/2.3.257. Glycobiology. 1992. PMID: 1498423 - Tissue-specific alternative splicing of the beta-galactoside alpha 2,6-sialyltransferase gene.
Wen DX, Svensson EC, Paulson JC. Wen DX, et al. J Biol Chem. 1992 Feb 5;267(4):2512-8. J Biol Chem. 1992. PMID: 1733948 - Rat beta-galactoside alpha 2,6-sialyltransferase genomic organization: alternate promoters direct the synthesis of liver and kidney transcripts.
Wang X, O'Hanlon TP, Young RF, Lau JT. Wang X, et al. Glycobiology. 1990 Sep;1(1):25-31. doi: 10.1093/glycob/1.1.25. Glycobiology. 1990. PMID: 1983783 - Characterization of mouse sialyltransferase genes: their evolution and diversity.
Takashima S. Takashima S. Biosci Biotechnol Biochem. 2008 May;72(5):1155-67. doi: 10.1271/bbb.80025. Epub 2008 May 7. Biosci Biotechnol Biochem. 2008. PMID: 18460788 Review. - Promoter structure and transcriptional regulation of human beta-galactoside alpha2, 3-sialyltransferase genes.
Taniguchi A. Taniguchi A. Curr Drug Targets. 2008 Apr;9(4):310-6. doi: 10.2174/138945008783954998. Curr Drug Targets. 2008. PMID: 18393824 Review.
Cited by
- Blood-Borne ST6GAL1 Regulates Immunoglobulin Production in B Cells.
Irons EE, Punch PR, Lau JTY. Irons EE, et al. Front Immunol. 2020 Apr 23;11:617. doi: 10.3389/fimmu.2020.00617. eCollection 2020. Front Immunol. 2020. PMID: 32391003 Free PMC article. - Regulation of ST6GAL1 sialyltransferase expression in cancer cells.
Dorsett KA, Marciel MP, Hwang J, Ankenbauer KE, Bhalerao N, Bellis SL. Dorsett KA, et al. Glycobiology. 2021 Jun 3;31(5):530-539. doi: 10.1093/glycob/cwaa110. Glycobiology. 2021. PMID: 33320246 Free PMC article. Review. - Altered mRNA expression of glycosyltransferases in human colorectal carcinomas and liver metastases.
Petretti T, Kemmner W, Schulze B, Schlag PM. Petretti T, et al. Gut. 2000 Mar;46(3):359-66. doi: 10.1136/gut.46.3.359. Gut. 2000. PMID: 10673297 Free PMC article. - Potential tumor markers for human gastric cancer: an elevation of glycan:sulfotransferases and a concomitant loss of alpha1,2-fucosyltransferase activities.
Chandrasekaran EV, Xue J, Piskorz C, Locke RD, Tóth K, Slocum HK, Matta KL. Chandrasekaran EV, et al. J Cancer Res Clin Oncol. 2007 Sep;133(9):599-611. doi: 10.1007/s00432-007-0206-0. Epub 2007 May 11. J Cancer Res Clin Oncol. 2007. PMID: 17492468 - Immune regulation by the ST6Gal sialyltransferase.
Hennet T, Chui D, Paulson JC, Marth JD. Hennet T, et al. Proc Natl Acad Sci U S A. 1998 Apr 14;95(8):4504-9. doi: 10.1073/pnas.95.8.4504. Proc Natl Acad Sci U S A. 1998. PMID: 9539767 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases