Transcription of the Spec 1-like gene of Lytechinus is selectively inhibited in response to disruption of the extracellular matrix.
The influence of the extracellular matrix (ECM) on differential gene expression during sea urchin development was explored using cell-type-specific cDNA probes. The ECM of three species of sea urchin, Strongylocentrotus purpuratus, Lytechinus variegatus and Lytechinus pictus, was disrupted with the lathrytic agent beta-aminopropionitrile (BAPN), which inhibits collagen deposition in the ECM and arrests gastrulation (Wessel & McClay, Devl Biol. 121: 149, 1987). The levels of several mRNAs (Spec 1, Spec 2, CyIIa actin, CyIIIa actin and collagen in S. purpuratus, and metallothionine, ubiquitin and LpS3 in L. pictus and L. variegatus) were compared in BAPN-treated and control embryos. These mRNAs accumulated normally during BAPN treatment, even though the embryos did not gastrulate. To determine if the expression of any gene product is sensitive to ECM disruption, a differential cDNA screen compared poly (A+) RNA from BAPN-arrested and control embryos in Lytechinus. A cDNA clone was isolated from this screen that represented a 2.1 kb mRNA that did not accumulate during BAPN treatment. Removal of BAPN resulted in the accumulation of this transcript coincident with the onset of gastrulation. This cDNA clone encodes a L. variegatus homologue of LpS1, recently demonstrated to be an ancestral homologue of the aboral ectoderm-specific Spec 1-Spec 2 gene family in S. purpuratus. Nuclear run-on assays in L. pictus suggested that transcriptional activity of LpS1 was selectively inhibited by BAPN treatment. Thus, although the accumulation of many gene products occurred independently of the embryonic collagenous matrix, the accumulation of LpS1 and LvS1 appeared to be mediated by the ECM.
Wessel
G M
GM
Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030.
Zhang
W
W
Tomlinson
C R
CR
Lennarz
W J
WJ
Klein
W H
WH
D000199:Actins / Q000235:genetics; D000629:Aminopropionitrile / Q000494:pharmacology; D000818:Animals; D002135:Calcium-Binding Proteins / Q000235:genetics*; D002454:Cell Differentiation / Q000187:drug effects; D003094:Collagen / Q000235:genetics / Q000378:metabolism; D015342:DNA Probes; D004475:Ectoderm / Q000378:metabolism; D004707:Endoderm / Q000166:cytology; D005109:Extracellular Matrix / Q000187:drug effects / Q000502:physiology*; D005775:Gastrula / Q000187:drug effects / Q000502:physiology; D015870:Gene Expression; D008648:Mesoderm / Q000378:metabolism; D009024:Morphogenesis; D012333:RNA, Messenger / Q000378:metabolism; D012617:Sea Urchins / Q000196:embryology* / Q000235:genetics; D014158:Transcription, Genetic; D014336:Troponin / Q000235:genetics; D019209:Troponin C
D000199:Actins; D002135:Calcium-Binding Proteins; D015342:DNA Probes; D012333:RNA, Messenger; D014336:Troponin; D019209:Troponin C; D000629:Aminopropionitrile; D003094:Collagen