Cloning and Expression of a Novel, Tissue Specifically Expressed Member of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Family*

@article{Hagen1998CloningAE,
  title={Cloning and Expression of a Novel, Tissue Specifically Expressed Member of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Family*},
  author={Kelly G. Ten Hagen and Fred K. Hagen and Marlene M. Balys and Thomas M. Beres and B C Van Wuyckhuyse and Lawrence A. Tabak},
  journal={The Journal of Biological Chemistry},
  year={1998},
  volume={273},
  pages={27749 - 27754}
}
We report the cloning and expression of the fifth member of the mammalian UDP-GalNAc:polypeptideN-acetylgalactosaminyltransferase (ppGaNTase) family. Degenerate polymerase chain reaction amplification and hybridization screening of a rat sublingual gland (RSLG) cDNA library were used to identify a novel isoform termed ppGaNTase-T5. Conceptual translation of the cDNA reveals a uniquely long stem region not observed for other members of this enzyme family. Recombinant proteins expressed… 

Figures and Tables from this paper

Cloning and Characterization of a New Human UDP-N-Acetyl-α-d-galactosamine:PolypeptideN-Acetylgalactosaminyltransferase, Designated pp-GalNAc-T13, That Is Specifically Expressed in Neurons and Synthesizes GalNAc α-Serine/Threonine Antigen*
TLDR
A novel human pp-GalNAc-T13 is cloned and analyzed from an NT2 cell cDNA library, and it is revealed to be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons.
Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family.
TLDR
Real-time PCR data indicate the contribution of each isoform to the overall ppGaNTase expression within each tissue and highlight the particular isoforms and tissues that will be the targets of future studies on the functions of the pp GaNTase family.
Functional Characterization and Expression Analysis of Members of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Family from Drosophila melanogaster*
TLDR
The cloning and functional characterization of eight members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase gene family from Drosophila melanogaster provides additional insight into the use of this model system to dissect the biological role of this enzyme family in vivo during both fly and mammalian development.
Characterization of a UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase That Displays Glycopeptide N-Acetylgalactosaminyltransferase Activity*
TLDR
The cloning, expression, and characterization of a novel member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (ppGaNTase) family that transfers Gal NAc to a GalNAc-containing glycopeptide is reported, suggesting thatO-glycosylation of multisite substrates may proceed in a specific hierarchical manner and underscores the potential complexity of the processes that regulate O-glyCosylation.
Cloning and expression of a brain-specific putative UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase gene.
TLDR
It was found that human pt-GalNAc-T was identical to the gene WBSCR17, which is reported to be in the critical region of patients with Williams-Beuren Syndrome, a neurodevelopmental disorder, and to be predominantly expressed in brain and heart.
Cloning and Characterization of a Ninth Member of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Family, ppGaNTase-T9*
TLDR
Northern blot analysis revealed that the gene encoding this enzyme is expressed in a broadly distributed manner across many adult tissues, lending further support to the existence of a hierarchical network of differential enzymatic activity within the diversely regulated ppGaNTase family, which may play a role in the various processes governing development.
Cloning and Characterization of a Close Homologue of Human UDP-N-acetyl-α-d-galactosamine:Polypeptide N-Acetylgalactosaminyltransferase-T3, Designated GalNAc-T6
TLDR
The results demonstrate the existence of genetic redundancy of a polypeptide GalNAc-transferase that does not provide full functional redundancy.
Identification of a novel human UDP-GalNAc transferase with unique catalytic activity and expression profile.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 25 REFERENCES
cDNA Cloning and Expression of a Novel UDP-N-acetyl-d-galactosamine:PolypeptideN-Acetylgalactosaminyltransferase*
The cDNA for a fourth member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, termed ppGaNTase-T4, has been cloned from a murine spleen cDNA library and expressed
Cloning and expression of mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3.
TLDR
A novel isoform of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, designated ppGaNTase-T3, has been cloned from a mouse testis cDNA library and expressed in COS7 cells, suggesting that more than one isoform may be required to complete the O-glycosylation of endogenous substrates.
cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.
TLDR
GalNAc-T3 was expressed as a soluble protein without the hydrophobic transmembrane domain in insect cells using a Baculo-virus vector, and the expressed GalNAC-transferase activity showed substrate specificity different from that previously reported for GalNAc -T1 and -T2.
cDNA Cloning and Expression of a Family of UDP-N-acetyl-dgalactosamine:PolypeptideN-Acetylgalactosaminyltransferase Sequence Homologs fromCaenorhabditis elegans *
TLDR
The substantial diversity of these isoforms in C. elegans suggests that mucin O-glycosylation is catalyzed by a complex gene family, which is conserved among evolutionary-distinct organisms.
Substrate Specificities of Three Members of the Human UDP-N-Acetyl-α-d-galactosamine:Polypeptide N-Acetylgalactosaminyltransferase Family, GalNAc-T1, -T2, and -T3*
TLDR
It is demonstrated that individual GalNAc-transferases have distinct activities and the initiation of O-glycosylation in a cell is regulated by a repertoire of GalNAC-transferase.
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Identification and separation of two distinct transferase activities.
TLDR
The results support the existence of multiple Gal-NAc-transferase activities and suggest that these are differentially expressed in different organs, and the identification of acceptor peptides that can be used to discriminate GalNAc, O-linked glycosylation in cells and organs and in pathological conditions.
T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl-transferase gene by site-directed recombination.
TLDR
Thymocyte O-linked oligosaccharide formation persisted in the absence of a functional targeted polypeptide GalNAc-T allele as determined by O-glycan-specific lectin binding, indicating a complexity in vertebrate O- glycan biosynthesis that involves multiple polypepton-Ts.
Identification of essential histidine residues in UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1.
TLDR
Analysis of N-glycosylation sequons revealed that positions N-95 and N-552 are occupied by N-linked sugars in COS7 cells, suggesting that UDP-GalNAc binding changes the accessibility or reactivity of an essential histidine residue.
...
1
2
3
...