Sequence analysis of a cDNA clone encoding the liver cell adhesion molecule, L-CAM.

Gallin, Warren J.; Sorkin, Barbara C.; Edelman, Gerald M.; Cunningham, Bruce A.

doi:10.1073/pnas.84.9.2808

Cited by 144 publications

(88 citation statements)

References 33 publications

(45 reference statements)

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“…Some of the properties of these cadherins are similar in a number of respects, such as the molecular weight, the Ca2+ requirement for their activity, and Ca2+ protection against protease (Shirayoshi et al, 1986). Amino acid sequences deduced from cDNA cloning have clearly shown that cadherins belong to a protein family (Gallin et al, 1987;Nagafuchi et al, 1987;Nose et al, 1987;Ringwald et al, 1987;Hatta et al, 1988;Miyatani et al, 1989;Shimoyama et al, 1989). The cadherin molecule is divided by a transmembrane domain into a large extracellular domain at the N-terminal side and a small cytoplasmic domain at the C-terminal side.…”

Section: Introductionmentioning

confidence: 99%

Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue.

1991

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To examine the diversity of the cadherin family, we isolated cDNAs from brain and retina cDNA preparations with the aid of polymerase chain reaction. The products obtained included cDNAs for two of three known cadherins as well as eight distinct cDNAs, of which deduced amino acid sequences show significant similarity with the known cadherin sequences. Larger cDNA clones were isolated from human cDNA libraries for six of the eight new molecules. The deduced amino acid sequences show that the overall structure of these molecules is very similar to that of the known cadherins, indicating that these molecules are new members of the cadherin family. We have tentatively designated these cadherins as cadherin-4 through -11. The new molecules, with the exception of cadherin-4, exhibit features that distinguish them as a group from previously cloned cadherins; they may belong to a new subfamily of cadherins. Northern blot analysis showed that most of these cadherins are expressed mainly in brain, although some are expressed in other tissues as well. These findings show that the cadherin family of adhesion molecules is much larger than previously thought, and suggest that the new cadherins may play an important role in cell-cell interactions within the central nervous system.

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Section: Introductionmentioning

confidence: 99%

Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue.

1991

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“…An XhoI/BamHI fragment containing the majority of the Ecadherin coding region was isolated from plasmid pEC320 (40). pBK-CMV expression vector (Stratagene) was modified by digestion with EcoRI and KpnI followed by polishing with mung bean nuclease and ligation to remove part of the polylinker.…”

Section: Construction Of E-cadherin Expressionmentioning

confidence: 99%

In the First Extracellular Domain of E-cadherin, Heterophilic Interactions, but Not the Conserved His-Ala-Val Motif, Are Required for Adhesion

Renaud-Young¹,

Gallin

2002

Journal of Biological Chemistry

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The classical cadherins, definitive proteins of the cadherin superfamily, are characterized functionally by their ability to mediate calcium-dependent cell aggregation in vitro. To test hypothetical mechanisms of adhesion, we have constructed two mutants of the chicken E-cadherin protein, one with the highly conserved HisAla-Val (HAV) sequence motif reversed to Val-Ala-His (VAH), the other lacking the first extracellular domain (EC1). The inversion of HAV to VAH has no effect on the capacity of E-cadherin to mediate adhesion. Deletion of EC1 completely eliminates the ability of E-cadherin to mediate homophilic adhesion, but the deletion mutant is capable of adhering heterophilically to both unmutated E-cadherin and to the HAV/VAH mutant. These results demonstrate that the conserved HAV sequence motif is not involved in cadherin-mediated adhesion as has been suggested previously and supports the idea that in the context of the cell surface, cadherin-mediated cell-cell adhesion involves an interaction of EC1 with other domains of the cadherin extracellular moiety and not the "linear zipper" model, which posits trans interactions only between EC1 on apposing cell surfaces.Classical cadherins were defined initially by their ability to mediate calcium-dependent cell-cell adhesion (1-5). Both the extracellular and the intracellular portions of the cadherin play critical roles in mediating adhesion (6). Perturbation and expression experiments have demonstrated that cadherin-mediated adhesion promotes a range of cellular processes subsequent to adhesion, including epithelial polarization (7, 8), blastula compaction (2), neurite outgrowth (9, 10), and formation of desmosomes (11, 12) and gap junctions (13-16).Classical cadherin proteins at the cell surface consist of five extracellular domains (ECs), 1 a transmembrane sequence, and a cytoplasmic domain (Fig. 1). Each cadherin extracellular domain shares a folding topology of seven ␤-strands arranged in two ␤-sheets forming a barrel with hydrophobic amino acid side chains largely sequestered within the interior (17-20). The amino and carboxyl termini emerge from opposite ends of each folded domain, maintaining an orientation with the amino terminus directed away from the cell. Conserved amino acid residues that are capable of coordinating calcium ions are present at the ends of each barrel (17)(18)(19)(20). Binding of calcium at these sites maintains the structural integrity of the cadherin ECs, giving the protein a rigid conformation that allows it to mediate cell-cell adhesion. A single amino acid substitution in a calcium binding site between EC1 and EC2 or between EC2 and EC3 can abolish adhesion and increase motility, whereas mutations in other calcium-binding elements do not affect these behaviors (21,22).Cadherins expressed on adjacent cells homoassociate through an antiparallel, trans, interaction of their extracellular regions. The bonds that they form across the intercellular space hold the plasma membranes of adjacent cells in close proximity. Adhesive strength...

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“…Such a molecular weight discrepancy is commonly found for transmembrane glycoproteins (e.g., L-CAM, Gallin et al, 1987). Consistent with the known transmembrane nature of dg2/3 ) hydropathy plots (Hopp and Woods, 1981) identified a single region of 35 amino acids showing characteristics of a transmembrane sequence (Fig.…”

Section: Sequencing Of Cdna Clonesmentioning

confidence: 52%

“…The extracellular domains of Percentage identity between extrac¢lhilar domain sequences can be found by refering to the figure at the intersection of rows and columns corresponding to any pair of sequences. Bovine N-cadherin, Liaw et al (1990); chick N-cadherin, Hatta et al (1988); mouse P-cadherin, Nose et al (1987); mouse E-cadherin, Nagafuchi et al (1987); chick L-CAM, Gallin et al (1987); bovine dgl, Koch et al (1990). (Fig.…”

Section: Sequence Homologies With Cadherins and Dglmentioning

confidence: 99%

“…Derived amino acid sequences of these proteins reveal a homologous family of transmembrane glycoproteins with a single membrane spanning domain, and a highly conserved cytoplasmic domain (Ringwald et al, 1987;Gallin et al, 1987;Nose et al, 1987;Nagafuchi et al, 1987;Hatta et al, 1988;Miyatani et al, 1989;Shimoyama et al, 1989;Walsh et al, 1990;Liaw et ai., 1990).…”

mentioning

confidence: 99%

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Cloning and sequence analysis of desmosomal glycoproteins 2 and 3 (desmocollins): cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains.

Collins

Legan

Kenny

et al. 1991

The Journal of Cell Biology

183

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Abstract. Desmosomal glycoproteins 2 and 3 (dg2 and 3) or desmocollins have been implicated in desmosome adhesion. We have obtained a 5.0-kb-long clone for dg3 from a bovine nasal epidermal hgtl 1 cDNA library. Sequence analysis of this clone reveals an open reading frame of 2,517 bases encoding a polypeptide of 839 amino acids. The sequence consists of a signal peptide of 28 amino acids, a precursor sequence of 104 amino acids, and a mature protein of 707 amino acids. The latter has the characteristics of a transmembrane glycoprotein with an extracellular domain of 550 amino acids and a cytoplasmic domain of 122 amino acids.The sequence of a partial clone from the same library shows that dg2 has an alternative COOH terminus that is extended by 54 amino acids. Genomic DNA sequence data show that this arises by splicing out of a 46-bp exon that encodes the COOH-terminal 11 amino acids of dg3 and contains an in-frame stop codon.The extraceUular domain of dg3 shows 39.4% protein sequence identity with bovine N-cadherin and 28.4% identity with the other major desmosomal glycoprotein, dgl, or desmoglein. The cytoplasmic domain of dg3 and the partial cytoplasmic domain of rig2 show 23 and 24% identity with bovine N-cadherin, respectively.The results support our previous model for the transmembrane organization of dg2 and

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Sequence analysis of a cDNA clone encoding the liver cell adhesion molecule, L-CAM.

Cited by 144 publications

References 33 publications

Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue.

Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue.

In the First Extracellular Domain of E-cadherin, Heterophilic Interactions, but Not the Conserved His-Ala-Val Motif, Are Required for Adhesion

Cloning and sequence analysis of desmosomal glycoproteins 2 and 3 (desmocollins): cadherin-like desmosomal adhesion molecules with heterogeneous cytoplasmic domains.

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