T-cadherin, a novel cadherin cell adhesion molecule in the nervous system lacks the conserved cytoplasmic region

Ranscht, Barbara; Dours-Zimmermann, Marı́a T.

doi:10.1016/0896-6273(91)90291-7

Cited by 304 publications

(249 citation statements)

References 54 publications

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“…With the exception of T-cadherin, all members of the cadherin superfamily contain a transmembrane domain, linking the extracellular portion of the molecule with intracellular signaling pathways. T-cadherin is anchored to the plasma membrane by a GPI anchor (24). Like classical or type-I cadherins, the extracellular portion of T-cadherin contains five ectodomains.…”

Section: Discussionmentioning

confidence: 99%

T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin

Hug

Wang

Ahmad

et al. 2004

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

782

589

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Acrp30͞adiponectin is reduced in the serum of obese and diabetic individuals, and the genetic locus of adiponectin is linked to the metabolic syndrome. Recombinant adiponectin, administered to diet-induced obese mice, induced weight loss and improved insulin sensitivity. In muscle and liver, adiponectin stimulates AMP-activated protein kinase activation and fatty acid oxidation. To expression-clone molecules capable of binding adiponectin, we transduced a C2C12 myoblast cDNA retroviral expression library into Ba͞F3 cells and panned infected cells on recombinant adiponectin linked to magnetic beads. We identified T-cadherin as a receptor for the hexameric and high-molecular-weight species of adiponectin but not for the trimeric or globular species. Only eukaryotically expressed adiponectin bound to T-cadherin, implying that posttranslational modifications of adiponectin are critical for binding. An adiponectin mutant lacking a conserved N-terminal cysteine residue required for formation of hexamer and high-molecularweight species did not bind T-cadherin in coimmunoprecipitation studies. Although lacking known cellular functions, T-cadherin is expressed in endothelial and smooth muscle cells, where it is positioned to interact with adiponectin. Because T-cadherin is a glycosylphosphatidylinositol-anchored extracellular protein, it may act as a coreceptor for an as-yet-unidentified signaling receptor through which adiponectin transmits metabolic signals.A dipose tissue is not only a storage depot for lipid but also a regulator of metabolism, through hormones known as adipokines. One adipokine is adiponectin (also denoted Acrp30, for adipocyte complement-related protein of 30 kDa), a molecule secreted exclusively by differentiated adipocytes (1). Adiponectin, which has homology to C1q, is found in the serum as three distinct oligomers, namely trimer, hexamer, and a highmolecular-weight (HMW) species (2). Adiponectin levels are decreased in the serum of obese and diabetic people (3) and animal models of obesity and diabetes. Replenishment by any of several methods induces weight loss and correction of insulin resistance (4-6). The mechanisms by which adiponectin influences metabolism are not fully understood but involve increasing fatty-acid oxidation in muscle through AMP-activated protein kinase (AMPK) activation, as well as synergizing with insulin in the liver to increase glycogen stores and to inhibit gluconeogenesis (6, 7). In tissue culture and isolated muscle, the trimeric isoform and a trimeric globular C-terminal subdomain activate AMPK (7,8), whereas the hexamer and HMW isoforms activate NF-B (9). Adiponectin also has been implicated in the inflammatory process of the metabolic syndrome, and reduced adiponectin levels have been correlated with impaired forearm blood flow, possibly linking endothelial dysfunction with adiponectin levels (10).Analysis of the transmembrane pathways linking adiponectin to downstream signaling events has yielded conflicting results. Two recently described receptors that bind ad...

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Section: Discussionmentioning

confidence: 99%

T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin

Hug

Wang

Ahmad

et al. 2004

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

782

589

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“…Best studied are N-(neural), E-(epithelial), and P-(placental) cad- herin and L-CAM (liver CAM, Takeichi, 1990Takeichi, , 1991. More recently, B-(brain, Napolitano et al, 19911, R-(retinal, Inuzuka et al, 1991), T-(truncated, Ranscht and Dours-Zimmermann, 1991), and M-(muscle, Donalies et al, 1991) cadherin have been described. Each molecule shows a distinct pattern of tissue distribution and developmental regulation.…”

Section: Introductionmentioning

confidence: 99%

Expression pattern of M‐cadherin in normal, denervated, and regenerating mouse muscles

Irintchev

Zeschnigk

Starzinski‐Powitz

et al. 1994

Developmental Dynamics

319

266

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“…They named these cadherins numerically from cadherin-4 to cadherin-13, and so far seven of them have been completely sequenced (11)(12)(13)28); cadherin-4 is the human homologue of R-cadherin (29), and cadherin-13, which lacks a cytoplasmic domain, seems to be the human homologue of T-cadherin (30). Cadherin-5, -6, -8, -11, and -12 have similar structures and high amino acid homology with each other, suggesting that they form a subgroup of cadherins called type II cadherins.…”

Section: The Nucleotide Sequence(s) Reported In This Paper Has Been Smentioning

confidence: 99%

Identification of Human Cadherin-14, a Novel Neurally Specific Type II Cadherin, by Protein Interaction Cloning

Shibata¹,

Shimoyama²,

Gotoh³

et al. 1997

Journal of Biological Chemistry

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Cadherins, a family of Ca 2؉ -dependent cell-cell adhesion molecules, mediate neural cell-cell interactions and may play important roles in neural development. By searching for molecules that interact with ␤-catenin, a cytoplasmic regulator of cadherins, we have identified a new member of the cadherin family, which we named human cadherin-14. Cadherin-14 had high amino acid sequence homology with the type II subgroup of cadherins and was broadly expressed in the central nervous system. Cadherin-14 is a novel neurally specific cell-cell adhesion molecule and may regulate neural morphogenesis.

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T-cadherin, a novel cadherin cell adhesion molecule in the nervous system lacks the conserved cytoplasmic region

Cited by 304 publications

References 54 publications

T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin

T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin

Expression pattern of M‐cadherin in normal, denervated, and regenerating mouse muscles

Identification of Human Cadherin-14, a Novel Neurally Specific Type II Cadherin, by Protein Interaction Cloning

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