PMID- 10438950
OWN - NLM
STAT- MEDLINE
DCOM- 19990909
LR  - 20191210
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 163
IP  - 4
DP  - 1999 Aug 15
TI  - AND-34, a novel p130Cas-binding thymic stromal cell protein regulated by adhesion
      and inflammatory cytokines.
PG  - 2104-12
AB  - We have characterized a novel cDNA whose steady state mRNA levels rise in the
      thymus 2 to 6 h following the induction of CD4+CD8+ thymocyte apoptosis by in
      vivo cross-linking of CD3 epsilon. This cDNA, AND-34-1, contains an open reading 
      frame (ORF) encoding a protein with an amino-terminal Src homology 2 (SH2) domain
      and a carboxyl-terminal domain homologous to GDP-exchange factors (GEFs).
      Northern analysis demonstrates widespread expression of the AND-34 gene. Anti-CD3
      epsilon treatment induces up-regulation of the AND-34 mRNA levels in total thymic
      RNA but not in RNA from purified thymocytes, suggesting that this transcript is
      derived from a thymic stromal cell population. IL-1 and TNF increase AND-34
      transcript levels in thymic cortical reticular, thymic nurse, and fibroblast cell
      lines. In the thymic cortical reticular cell line, IL-1 and TNF induce a protein 
      of the predicted 93-kDa size reactive with anti-AND-34 peptide antisera. Fifteen 
      minutes of serum stimulation of vanadate-pretreated AND-34-1-transfected NIH3T3
      fibroblasts induces tyrosine phosphorylation of AND-34 as well as coprecipitating
      95-, 125-, and 130-kDa proteins. One of these tyrosine phosphorylated proteins is
      identified as p130Cas (Crk-associated substrate), a signaling molecule previously
      known to bind to a GDP-exchange factor (C3G) and inducibly associate with the
      focal adhesion complex. Consistent with such an association, AND-34 tyrosine
      phosphorylation is induced following adherence of trypsinized fibroblasts to
      fibronectin or poly-L -lysine-coated surfaces.
FAU - Cai, D
AU  - Cai D
AD  - Department of Medicine, Section of Hematology and Oncology, Boston Medical
      Center, MA 02118, USA.
FAU - Clayton, L K
AU  - Clayton LK
FAU - Smolyar, A
AU  - Smolyar A
FAU - Lerner, A
AU  - Lerner A
LA  - eng
SI  - GENBANK/AF179566
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Bcar1 protein, mouse)
RN  - 0 (Bcar3 protein, mouse)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Crk-Associated Substrate Protein)
RN  - 0 (Cytokines)
RN  - 0 (Guanine Nucleotide Exchange Factors)
RN  - 0 (Interleukin-1)
RN  - 0 (Peptide Fragments)
RN  - 0 (Phosphoproteins)
RN  - 0 (Proteins)
RN  - 0 (Retinoblastoma-Like Protein p130)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - 0 (ras-GRF1)
RN  - 42HK56048U (Tyrosine)
SB  - AIM
SB  - IM
MH  - 3T3 Cells
MH  - Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Cell Adhesion/immunology
MH  - Cell Cycle Proteins/chemistry
MH  - Crk-Associated Substrate Protein
MH  - Cytokines/*physiology
MH  - *Guanine Nucleotide Exchange Factors
MH  - Interleukin-1/physiology
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mice, Transgenic
MH  - Molecular Sequence Data
MH  - Peptide Fragments/chemistry
MH  - Phosphoproteins/*metabolism
MH  - Phosphorylation
MH  - Polymerase Chain Reaction
MH  - Precipitin Tests
MH  - Protein Binding/immunology
MH  - Proteins/chemistry/genetics/isolation & purification/*metabolism
MH  - Retinoblastoma-Like Protein p130
MH  - Sequence Homology, Amino Acid
MH  - Stromal Cells/immunology/metabolism
MH  - Thymus Gland/cytology/immunology/*metabolism
MH  - Tumor Necrosis Factor-alpha/physiology
MH  - Tyrosine/metabolism
MH  - ras-GRF1
EDAT- 1999/08/10 00:00
MHDA- 1999/08/10 00:01
CRDT- 1999/08/10 00:00
PHST- 1999/08/10 00:00 [pubmed]
PHST- 1999/08/10 00:01 [medline]
PHST- 1999/08/10 00:00 [entrez]
AID - ji_v163n4p2104 [pii]
PST - ppublish
SO  - J Immunol. 1999 Aug 15;163(4):2104-12.