anti-Udp-N-Acetyl-alpha-D-Galactosamine:polypeptide N-Acetylgalactosaminyltransferase 1 (GalNAc-T1) (Galnt1) Antibodies

Mouse (Murine) Udp-N-Acetyl-alpha-D-Galactosamine:polypeptide N-Acetylgalactosaminyltransferase 1 (GalNAc-T1) (Galnt1) interaction partners

1. the ppGalNAc-T4 was highly expressed in MC3T3-E1 cells during osteogenesis for the first time; ppGalNAc-T1 and -T4 affected the expression of different osteogenic factors, suggesting distinct roles ppGalNAc-T isoforms play in regulating osteogenesis in vitro

2. Study show that in Galnt1 null mouse, there is compromised cardiac function that mimics human congenital heart disease suggesting that Galnt1 expression is required for normal heart valve development.

3. The GALNT1 is the glycosyltransferase enzyme family covering a single known glycosidic linkage.

4. Polypeptide GalNAcT-1 plays a predominant role in leukocyte recruitment in vivo by attaching functionally relevant O-linked glycans to L-selectin ligands.

5. each ppGalNAc T isoform may be uniquely sensitive to peptide sequence and overall charge, which together dictates the substrate sites that will be glycosylated

6. Growth factor stimulation regulates O-glycosylation initiation in a Src-dependent fashion by GalNac-T redistribution from golgi to the endoplasmic reticulum.

7. ppGalNAcT-1 to be indispensable for O-glycosylation at specific sites of the bone glycoproteins OPN and BSP.

8. These findings reveal that the initiation of protein O glycosylation by ppGalNAcT-1 provides a distinctive repertoire of advantageous functions that support vascular responses and humoral immunity.

Human Udp-N-Acetyl-alpha-D-Galactosamine:polypeptide N-Acetylgalactosaminyltransferase 1 (GalNAc-T1) (Galnt1) interaction partners

1. We have elucidated a novel miR-30-GALNT1/2 axis whose dysregulation increases the proportion of inactive proBNP secreted by the heart and impairs the compensatory actions of BNP during the progression of heart failure.

2. the GalNAc-T13 isoform is predicted to function similarly to GalNAc-T1 against peptide substrates in vivo, in contrast to a prior report, but is unique by being selectively expressed in the brain.

3. Expression of GALNT3 was reduced in CAD patients, and down regulation of GALNT3 contributed to endothelial injury by promoting apoptosis and up-regulating the expression of MMP-2 and MMP-14 genes via p38 MAPK activation.

4. appears to be responsive to the inhibition of GALNT1 and SHH signaling

5. Study demonstrates that down-regulation of GALNT1 is sufficient to suppress malignant phenotype of HCC cells by decreasing EGFR signaling.

6. High ppGalNAc T1 expresdsion is associated with bladder cancer.

7. The GALNT1 is the glycosyltransferase enzyme family covering a single known glycosidic linkage.

8. Utilizing unnatural glycopeptide substrates for GalNAc-T3 we demonstrated that the GalNAc-specific sugar recognition of the lectin domain regulates further glycosylation.

9. each ppGalNAc T isoform may be uniquely sensitive to peptide sequence and overall charge, which together dictates the substrate sites that will be glycosylated

10. Growth factor stimulation regulates O-glycosylation initiation in a Src-dependent fashion by GalNac-T redistribution from golgi to the endoplasmic reticulum.

11. the present analysis fails to replicate an earlier reported association of a GALNT1 variant with risk of ovarian cancer

12. First simultaneous kinetic description of O-glycosylation events by recombinant UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase I at all putative O-glycosylation sites within human mucin MUC1 containing 5 tandem repeats.

13. The results indicated that IL-4-treated LS174T cells are able to produce mucins with a higher degree of O-glycosylation than untreated counterparts.

14. GalNAc T10 has a large and pronounced glycopeptide preference for Ser/Thr-O-GalNAc only at the +1 position from the acceptor site, whereas T1 and T2 have significantly reduced and variable preferences for Ser/Thr-O-GalNAc.

15. A direct link between miR-129 and the two putative targets GALNT1 and SOX4 in bladder cancer.

16. Data show that the sequences and O-glycosylation patterns direct the addition of the first and second sugar residues by ppGalNAc-T and C1GalT which act in a site directed fashion.