PMID- 7958432
OWN - NLM
STAT- MEDLINE
DCOM- 19941129
LR  - 20190613
IS  - 0012-1606 (Print)
IS  - 0012-1606 (Linking)
VI  - 165
IP  - 2
DP  - 1994 Oct
TI  - A Drosophila homolog of cadherin associated with armadillo and essential for 
      embryonic cell-cell adhesion.
PG  - 716-26
AB  - We have identified a Drosophila homolog of vertebrate classic cadherins. A 
      monoclonal antibody to Drosophila alpha-catenin (D alpha-catenin) copurifies a 
      150-kDa glycoprotein (gp150) along with the alpha-catenin. To further 
      characterize this protein, we generated monoclonal antibodies to gp150 and 
      isolated its cDNAs using the antibodies. Predicted sequences of the encoded 
      product revealed that it is a transmembrane protein with similarity to vertebrate 
      classic cadherins, and so we designated this molecule DE-cadherin. The 
      extracellular domain has six cadherin-specific repeats, although the first repeat 
      seems to be cleaved off upon maturation, and the cytoplasmic domain shows 
      significant identity to that of vertebrate classic cadherins. DE-cadherin is 
      distinguishable from its vertebrate counterparts by a large insertion with local 
      sequence similarity to Fat, laminin A chain, Slit, and neurexin I at the proximal 
      region of the extracellular domain. Despite such differences, DE-cadherin is 
      functionally similar to vertebrate classic cadherins. For example, it is 
      associated with alpha-catenin and beta-catenin (Armadillo), and protected from 
      trypsin digestion only in the presence of Ca2+, as is the case for many of 
      classic cadherins. Transfection of S2 cells with the DE-cadherin cDNA enhances 
      their Ca(2+)-dependent cell aggregation. Antibodies to this molecule inhibited 
      aggregation of not only the transfectants but also early embryonic cells. 
      DE-cadherin is concentrated at the apical poles of epithelial cell-cell 
      junctions. All these results suggest that DE-cadherin is a homolog of vertebrate 
      classic cadherins and that the vertebrate and invertebrate share common 
      mechanisms for regulation of cell-cell adhesion.
FAU - Oda, H
AU  - Oda H
AD  - Department of Biophysics, Faculty of Science, Kyoto University, Japan.
FAU - Uemura, T
AU  - Uemura T
FAU - Harada, Y
AU  - Harada Y
FAU - Iwai, Y
AU  - Iwai Y
FAU - Takeichi, M
AU  - Takeichi M
LA  - eng
SI  - GENBANK/D28749
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Dev Biol
JT  - Developmental biology
JID - 0372762
RN  - 0 (ARM protein, Drosophila)
RN  - 0 (Armadillo Domain Proteins)
RN  - 0 (Cadherins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Glycoproteins)
RN  - 0 (Proteins)
RN  - 0 (Trans-Activators)
RN  - 0 (Transcription Factors)
SB  - IM
GS  - arm
MH  - Amino Acid Sequence
MH  - Animals
MH  - Armadillo Domain Proteins
MH  - Cadherins/*chemistry
MH  - Cell Adhesion
MH  - Cell Aggregation
MH  - Cloning, Molecular
MH  - DNA, Complementary/genetics
MH  - *Drosophila Proteins
MH  - Drosophila melanogaster/*chemistry/embryology
MH  - Glycoproteins/chemistry/genetics
MH  - Molecular Sequence Data
MH  - Multigene Family
MH  - Proteins/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - *Trans-Activators
MH  - Transcription Factors
EDAT- 1994/10/01 00:00
MHDA- 1994/10/01 00:01
CRDT- 1994/10/01 00:00
PHST- 1994/10/01 00:00 [pubmed]
PHST- 1994/10/01 00:01 [medline]
PHST- 1994/10/01 00:00 [entrez]
AID - S0012-1606(84)71287-5 [pii]
AID - 10.1006/dbio.1994.1287 [doi]
PST - ppublish
SO  - Dev Biol. 1994 Oct;165(2):716-26. doi: 10.1006/dbio.1994.1287.