Structure of the gene for the liver cell adhesion molecule, L-CAM.

Sorkin, Barbara C.; Hemperly, John J.; Edelman, Gerald M.; Cunningham, Bruce A.

doi:10.1073/pnas.85.20.7617

Cited by 47 publications

(22 citation statements)

References 44 publications

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“…The results of Southern blots were the same, showing two bands for both clones 8 and 9, excluding the existence of a 5' non-coding region separated by one intron. We must notice that the studies of the organization of uvomorulin and Pcadherin (Hatta et al, 1991) confirm the existence of exon 1 encoding the complete 5' untranslated region and reveal a high conservation of the exon structure between mouse uvomorulin and chicken L-CAM (Sorkin et al, 1988). The existence of genes showing similarity of sequence has been reported previously in Xenopus; both insulin (Shuldiner et al, 1991) and XeFGF (Isaacs et al, 1992) are present as two slightly diverging genes; in both cases the two copies of the gene are expressed differentially during development.…”

Section: Discussionmentioning

confidence: 83%

N‐cadherin transcripts in Xenopus laevis from early tailbud to tadpole

Simonneau

Broders

Thiery

1992

Developmental Dynamics

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Cadherins are Ca+ +-dependent cell adhesion molecules which play a key role in morphogenesis and histogenesis. T w o mRNAs clones (8 and 9) corresponding to two N-cadherin pseudo-allelic genes are present in Xenopus Zaeuis. We report here that these transcripts share a highly homologous coding region but diverge in the non-coding region. We have determined the pattern of N-cadherin expression at the mRNA level by in situ hybridization with a riboprobe complementary to the EC5 domain of Xenopus Ncadherin clone 8. This part of the sequence is the least conserved in the cadherin gene family, minimizing the risk of cross-hybridization to other cadherins. N-cadherin transcripts are not detectable in the first stages of development. Expression first appears in the neural plate and reaches its maximum level in the CNS at tailbud stage. From early tadpole, it diminishes, so that a very weak signal is detected in the premetamorphic frog brain. N-cadherin expression is not uniform within the CNS, with some areas such as the roof of the rhombencephalon and the olfactory bulbs expressing higher levels of the transcripts. N-cadherin is present in several mesodermal derivatives such as the notochord, the pronephros, and the heart. It is, however, virtually absent from the myotomes and appears in skeletal muscles at later stages of differentiation. All placodes express high levels of N-cadherin. The non-neural ectoderm and the endoderm are always negative. In the brain and the heart, high levels of hybridization are observed with probes corresponding to both copies of the N-cadherin pseudo-allelic genes in their 5' non-coding region, indicating that both alleles are transcribed. o 1992 Wiley-Liss, Inc.

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Section: Discussionmentioning

confidence: 83%

N‐cadherin transcripts in Xenopus laevis from early tailbud to tadpole

Simonneau

Broders

Thiery

1992

Developmental Dynamics

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“…To extend the sequence of the chicken L-CAM gene, genomic libraries were screened using probes from the 5' ends of the previously isolated L-CAM clones ACL1 and pEC330/1 (34 (Fig. 3) that was distinct from the L-CAM mRNA.…”

Section: Resultsmentioning

confidence: 99%

“…We had previously determined the structure of all but the 5' end of the chicken L-CAM gene (34). The protein is encoded by 16 exons that range in size from 115 to >1000 base pairs (bp) and that extend over <10 kilobases (kb).…”

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confidence: 99%

Genes for two calcium-dependent cell adhesion molecules have similar structures and are arranged in tandem in the chicken genome.

Sorkin

Gallin

Edelman

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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Genomic sequences immediately upstream of the translational start site for the chicken liver cell adhesion molecule (L-CAM) gene contain a second closely related gene, which, because of its location, we have designated the K-CAM gene. Less than 700 base pairs separate the presumed poly(A) site in the K-CAM gene from the translation initiation site for L-CAM. The sizes of exons 4-15 of the K-CAM gene are almost identical to those in the L-CAM gene and the exon/intron junctions occur at exactly equivalent positions in both genes. Exon 16, which includes the 3' untranslated region, is much shorter in the K-CAM gene and intron sizes and sequences are not generally conserved between the two genes. Probes from the K-CAM gene hybridized to a 3-kilobase mRNA that was present at high levels in embryonic skin, at lower levels in kidney, heart, and gizzard, and at still lower levels in brain and liver, as determined by Northern blotting. The sequence of the predicted gene product was nearly identical to that of the chicken B-cadherin cDNA, although the distribution of the K-CAM gene transcript differed from that reported for the cadherin. The proximity and identical overall structure of the K-CAM and L-CAM genes strongly suggest that they arose by gene duplication and raise the possibility that genes for other calcium-dependent CAMs may be located in clusters. Moreover, the tandem arrangement of the genes may have important implications for the regulation of their expression.

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“…The À0.7 kb BamHI fragment (encoding the entire eGFP) was inserted into the Bg1II site of pDS3 (Iba et al, 1984) to generate PDS3-GFP. A 0.94 kb fragment containing the 5 0 part of exon 16 of E-cadherin (L-CAM) cDNA (Sorkin et al, 1988) was amplified by PCR with chicken DNA as a template and ligated into TA cloning vector pCR2.1 (Invitrogen, CA, USA). The EcoRV-SpeI fragment of the resultant plasmid was subcloned into the EcoRV-SpeI site of pBluescriptSK(+) to generate pBSK-ECAD.…”

Section: Plasmid Constructionmentioning

confidence: 99%