PMID- 7768179
OWN - NLM
STAT- MEDLINE
DCOM- 19950705
LR  - 20231213
IS  - 0950-1991 (Print)
IS  - 0950-1991 (Linking)
VI  - 121
IP  - 2
DP  - 1995 Feb
TI  - Expression of a dominant negative inhibitor of intercellular communication in the 
      early Xenopus embryo causes delamination and extrusion of cells.
PG  - 371-81
AB  - A chimeric construct, termed 3243H7, composed of fused portions of the rat gap 
      junction proteins connexin32 (Cx32) and connexin43 (Cx43) has been shown to have 
      selective dominant inhibitory activity when tested in the Xenopus oocyte pair 
      system. Co-injection of mRNA coding for 3243H7 together with mRNAs coding for 
      Cx32 or Cx43 completely blocked the development of channel conductances, while 
      the construct was ineffective at blocking intercellular channel assembly when 
      coinjected with rat connexin37 (Cx37). Injection of 3243H7 into the right 
      anterodorsal blastomere of 8-cell-stage Xenopus embryos resulted in disadhesion 
      and delamination of the resultant clone of cells evident by embryonic stage 8; a 
      substantial number, although not all, of the progeny of the injected cell were 
      eliminated from the embryo by stage 12. A second construct, 3243H8, differing 
      from 3243H7 in the relative position of the middle splice, had no dominant 
      negative activity in the oocyte pair assay, nor any detectable effects on Xenopus 
      development, even when injected at four-fold higher concentrations. The 
      3243H7-induced embryonic defects could be rescued by coinjection of Cx37 with 
      3243H7. A blastomere reaggregation assay was used to demonstrate that a 
      depression of dye-transfer could be detected in 3243H7-injected cells as early as 
      stage 7; Lucifer yellow injections into single cells also demonstrated that 
      injection of 3243H7 resulted in a block of intercellular communication. These 
      experiments indicate that maintenance of embryonic cell adhesion with concomitant 
      positional information requires gap junction-mediated intercellular 
      communication.
FAU - Paul, D L
AU  - Paul DL
AD  - Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.
FAU - Yu, K
AU  - Yu K
FAU - Bruzzone, R
AU  - Bruzzone R
FAU - Gimlich, R L
AU  - Gimlich RL
FAU - Goodenough, D A
AU  - Goodenough DA
LA  - eng
PT  - Journal Article
PL  - England
TA  - Development
JT  - Development (Cambridge, England)
JID - 8701744
RN  - 0 (Connexin 43)
RN  - 0 (Connexins)
RN  - 0 (DNA Primers)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - Blastocyst/*physiology
MH  - Blotting, Western
MH  - Cell Adhesion/physiology
MH  - Chimera
MH  - Connexin 43/genetics
MH  - Connexins/genetics/*physiology
MH  - DNA Primers
MH  - Embryonic Induction/*genetics
MH  - Female
MH  - Gap Junctions/*physiology
MH  - Gene Expression
MH  - Genetic Techniques
MH  - Microinjections
MH  - Molecular Sequence Data
MH  - Oocytes/physiology
MH  - Phenotype
MH  - Xenopus laevis/*embryology/genetics
MH  - Gap Junction beta-1 Protein
EDAT- 1995/02/01 00:00
MHDA- 1995/02/01 00:01
CRDT- 1995/02/01 00:00
PHST- 1995/02/01 00:00 [pubmed]
PHST- 1995/02/01 00:01 [medline]
PHST- 1995/02/01 00:00 [entrez]
AID - 10.1242/dev.121.2.371 [doi]
PST - ppublish
SO  - Development. 1995 Feb;121(2):371-81. doi: 10.1242/dev.121.2.371.