PMID- 10694442
OWN - NLM
STAT- MEDLINE
DCOM- 20000424
LR  - 20191210
IS  - 0014-4827 (Print)
IS  - 0014-4827 (Linking)
VI  - 255
IP  - 2
DP  - 2000 Mar 15
TI  - A C-terminal carbohydrate-binding domain in the endothelial cell regulatory 
      protein, pigpen: new function for an EWS family member.
PG  - 270-7
AB  - The potential for encoding information in carbohydrate (CHO) structures has long 
      been recognized. Selective CHO-binding proteins known as lectins and the 
      biological events they mediate are well known. However, many lectins were 
      originally discovered for biological activities other than saccharide binding, 
      and only subsequently was it realized that one or more of their key functions 
      were mediated by specific CHO recognition. Our previous observations suggested 
      that the nuclear protein pigpen had an affinity for CHO structures. This would 
      represent a new attribute for proteins of the EWS (Ewing's sarcoma) family, of 
      which pigpen is a member. In this study we demonstrate that a CHO-binding domain 
      resides in the C-terminus of the molecule and can be preferentially inhibited by 
      saccharides, most notably N-acetyl-d-galactosamine (GalNAc) and the 
      GalNAc-containing polysaccharide, chondroitin sulfate. Ligand blotting 
      experiments were subsequently performed with fractionated, 
      [(3)H]galactose-labeled cells to demonstrate the presence of chondroitin 
      sulfate-inhibitable endogenous CHO ligands for pigpen in endothelial nuclei. 
      Finally, microinjection of polysaccharide competitor into the nucleus of cultured 
      endothelial cells resulted in a loss of pigpen focal accumulations, suggesting 
      that the CHO-binding activity may be instrumental in subcellular localization of 
      the protein. In summary, our results show ligand preference and domain 
      specificity for pigpen's CHO affinity and provide initial evidence for 
      physiological ligands and function. They may also shed new light on the 
      mechanisms of oncogenic transformation involving EWS proteins.
CI  - Copyright 2000 Academic Press.
FAU - Alliegro, M C
AU  - Alliegro MC
AD  - Department of Cell Biology, Louisiana State University Medical Center, New 
      Orleans, Louisiana, 70112, USA. mallie@Isumc.edu
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Exp Cell Res
JT  - Experimental cell research
JID - 0373226
RN  - 0 (Carbohydrates)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Heterogeneous-Nuclear Ribonucleoproteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (RNA-Binding Protein EWS)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Ribonucleoproteins)
RN  - 0 (pigpen protein, bovine)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Binding, Competitive
MH  - Carbohydrates
MH  - Cattle
MH  - DNA-Binding Proteins
MH  - Endothelium, Vascular/*metabolism
MH  - Heterogeneous-Nuclear Ribonucleoproteins
MH  - *Nuclear Proteins/chemistry/genetics/metabolism
MH  - RNA-Binding Protein EWS
MH  - *RNA-Binding Proteins/chemistry/genetics/metabolism
MH  - Ribonucleoproteins/chemistry/genetics/metabolism
EDAT- 2000/03/01 09:00
MHDA- 2000/04/29 09:00
CRDT- 2000/03/01 09:00
PHST- 2000/03/01 09:00 [pubmed]
PHST- 2000/04/29 09:00 [medline]
PHST- 2000/03/01 09:00 [entrez]
AID - S0014-4827(99)94776-6 [pii]
AID - 10.1006/excr.1999.4776 [doi]
PST - ppublish
SO  - Exp Cell Res. 2000 Mar 15;255(2):270-7. doi: 10.1006/excr.1999.4776.