Cell Cycle-dependent Coupling of the Calcitonin Receptor to Different G Proteins

Chakraborty, Munmun; Chatterjee, Diptendu; Kellokumpu, Sakari; Rasmussen, Howard; Baron, Roland

doi:10.1126/science.1847755

Cited by 131 publications

(53 citation statements)

References 47 publications

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“…8B). protein, and a subsequent switch from the adenylyl cyclase to the Ca 2ϩ /protein kinase C signal pathway was reported for the calcitonin receptor in a pig kidney cell line (35). For the parathyroid hormone receptor, an additional coupling to G i proteins and a subsequent increase in Ca 2ϩ influx depending on cell cycle was shown in osteogenic sarcoma cells (36).…”

Section: Resultsmentioning

confidence: 90%

Cell Cycle-dependent Coupling of the Vasopressin V1a Receptor to Different G Proteins

Abel¹,

Wittau²,

Wieland³

et al. 2000

Journal of Biological Chemistry

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The biological effects of the neuropeptide hormone arginine vasopressin (AVP) 1 are induced by binding of AVP to specific membrane receptors that are members of the GTP-binding protein (G protein)-coupled receptor (GPCR) superfamily. To date, three AVP receptor subtypes (V 1a , V 1b , and V 2 ) have been cloned and characterized according to their tissue distribution and functional properties. The V 2 receptor subtype is predominantly expressed in the kidney, mediating the antidiuretic effects of AVP. The activated V 2 receptor couples to the heterotrimeric G protein G s and activates adenylyl cyclases (1, 2). Two V 1 -receptor subtypes have been cloned (3) and can be pharmacologically differentiated by their binding affinities to various AVP agonists and antagonists (4, 5). While the expression of the V 1b receptor subtype is restricted mainly to the central nervous system (6), the V 1a receptor is expressed in different neuronal and nonneuronal tissues. In nonneuronal tissues, the V 1a receptor induces a wide range of physiological effects such as contraction of vascular smooth muscles, stimulation of hepatic glycogenolysis and cell proliferation (for a review, see Refs.

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Section: Resultsmentioning

confidence: 90%

Cell Cycle-dependent Coupling of the Vasopressin V1a Receptor to Different G Proteins

Abel¹,

Wittau²,

Wieland³

et al. 2000

Journal of Biological Chemistry

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“…The CTR, like other members of this family, is known to couple to multiple trimeric G proteins that activate several signaling molecules, thereby producing diverse biological responses in different cell types. For example, we and others have shown that some aspects of the osteoclast (OC) response to CT are mediated by the cAMP pathway, while others are mediated by protein kinase C (5,6), and studies in our laboratory, using synchronized LLC-PK1 kidney proximal tubule cells, have shown that the mode of receptor coupling and the biological effects of CT vary with the stage of the cell cycle (7,8). The coupling of a recombinant CTR to both the adenylyl cyclase and phospholipase C signaling pathways has been demonstrated (9,10).…”

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confidence: 99%

The Deletion of 14 Amino Acids in the Seventh Transmembrane Domain of a Naturally Occurring Calcitonin Receptor Isoform Alters Ligand Binding and Selectively Abolishes Coupling to Phospholipase C

Shyu¹,

Inoue

Baron

et al. 1996

Journal of Biological Chemistry

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The cDNA that encodes the rabbit calcitonin receptor was cloned by screening a rabbit osteoclast library. Reverse transcription-polymerase chain reaction amplification of calcitonin receptor sequences from rabbit osteoclast RNA yielded cDNAs that encode two isoforms of the calcitonin receptor. One isoform is homologous to the C1a isoform previously identified in multiple cell types and species, while the second, designated CTR⌬e13, is a previously unidentified isoform that is apparently generated by alternative splicing during mRNA processing that deletes exon 13, resulting in the absence of 14 amino acids in the predicted seventh transmembrane domain. Expression of mRNA transcripts encoding the two isoforms varies in a tissuespecific manner, with CTR⌬e13 accounting for less than 15% of the total calcitonin receptor mRNA in osteoclasts, kidney, and brain, but comprising at least 50% of the transcripts in skeletal muscle and lung. The two isoforms were expressed, and the ligand binding and signal transduction properties were characterized. Deletion of the residues in the seventh transmembrane domain in CTR⌬e13 reduced the binding affinity for salmon and human calcitonin by more than 10-fold and approximately 2-fold, respectively, resulting in a receptor that failed to discriminate between the two forms of calcitonin. Both isoforms activated adenylyl cyclase, with EC 50 values consistent with the difference in ligand affinities. In contrast, only the C1a isoform, but not the CTR⌬e13 isoform, activated phospholipase C. Thus, while the CTR⌬e13 remains active despite the deletion of a significant portion of its seventh transmembrane domain, it has significantly altered ligand recognition and signal transduction properties. Calcitonin (CT)1 is a 32-amino acid peptide hormone that acts to reduce serum calcium levels by inhibiting bone resorption and promoting renal calcium excretion. Besides this hypocalcemic effect, CT modulates the renal transport of water and several ions other than calcium, and acts on the central nervous system to induce analgesia, anorexia, and gastric secretion (1). The CT receptor (CTR) belongs to a family of G protein-coupled peptide receptors that includes receptors for parathyroid hormone/parathyroid hormone-related peptide, secretin, vasoactive intestinal peptide, growth hormone-releasing hormone, glucagon, glucagon-like peptide, pituitary adenylyl cyclase-activating peptide, corticotropin-releasing factor, and calcitonin gene-related peptide (2-4).

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“…Manse-DPII is shorter (30 residues) than other known DH and has lower sequence similarity with other DH than does Manse-DH. However, in 1998, we identified a second DH from Tenebrio molitor, termed Tenmo-DH 47 (12) to distinguish this peptide from the known Tenmo-DH 37 (11). More recently we identified two DH from Hyles lineata (a sphingid moth closely related to M. sexta), Hylli-DH 30 and Hylli-DH 41 , which each differ at only one residue from their M. sexta counterparts.…”

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confidence: 99%

“…However, they are most likely paralogous sequences (arising from a gene duplication event), as is the case for fish CRF and urotensin I. The lower potency of Tenmo-DH 47 vs. Tenmo-DH 37 (12) suggests for it a somewhat different role, just as urocortin, an orthologue of urotensin I (15), has effects that differ in vivo from those of CRF (16,17).…”

mentioning

confidence: 99%

Cockroach diuretic hormones: Characterization of a calcitonin-like peptide in insects

Furuya

Milchak

Schegg

et al. 2000

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

131

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Insect diuretic hormones are crucial for control of water balance. We isolated from the cockroach Diploptera punctata two diuretic hormones (DH), Dippu-DH31 and Dippu-DH46, which increase cAMP production and fluid secretion in Malpighian tubules of several insect species. Dippu-DH 31 and -DH46 contain 31 and 46 amino acids, respectively. Dippu-DH46 belongs to the corticotropin-releasing factor (CRF)-like insect DH family, whereas Dippu-DH 31 has little sequence similarity to the CRF-like DH, but is similar to the calcitonin family. Dippu-DH46 and -DH31 have synergistic effects in D. punctata but have only additive effects in Locusta migratoria. Dippu-DH31 represents a distinct type of insect DH with actions that differ from those of previously identified insect peptides with diuretic activity.Malpighian tubules ͉ corticotropin-releasing factor ͉ Diploptera punctata ͉ Locusta migratoria ͉ Manduca sexta I n insects, urine production by the Malpighian tubules (Mt) is driven by hormonally controlled active transport processes, rather than by ultrafiltration, as in vertebrates. There are several families of insect diuretic peptides, including myokinins, which increase urine production by elevating intracellular Ca 2ϩ (1, 2), and the ''corticotropin-releasing factor (CRF)-like'' diuretic hormones (DH), which act via cAMP (3). CRF-like DH have been identified from eight species in five insect orders (4-14); they are similar to the sauvagine͞CRF͞urotensin I͞urocortin family of vertebrate peptides.For some years, only Manduca sexta was known to possess two CRF-like DH, Manse-DH (4) and Manse-DPII (9). Manse-DPII is shorter (30 residues) than other known DH and has lower sequence similarity with other DH than does Manse-DH. However, in 1998, we identified a second DH from Tenebrio molitor, termed Tenmo-DH 47 (12) to distinguish this peptide from the known Tenmo-DH 37 (11). More recently we identified two DH from Hyles lineata (a sphingid moth closely related to M. sexta), Hylli-DH 30 and Hylli-DH 41 , which each differ at only one residue from their M. sexta counterparts. Thus, in at least three insect species, two DH exist. The extent of sequence similarity between these ''long'' and ''short'' DH indicates that they belong to the same peptide family. However, they are most likely paralogous sequences (arising from a gene duplication event), as is the case for fish CRF and urotensin I. The lower potency of Tenmo-DH 47 vs. Tenmo-DH 37 (12) suggests for it a somewhat different role, just as urocortin, an orthologue of urotensin I (15), has effects that differ in vivo from those of CRF (16,17).We now report the identification of two DH from brain and corpora cardiaca (CC) of the Pacific beetle cockroach (Diploptera punctata), one of which (Dippu-DH 31 ) is a peptide with biological properties that differ from those of the CRF-like DH. Materials and MethodsInsects. D. punctata were maintained as described previously (18). Brains and CC were dissected from adult males 2-10 days old. For bioassays, newly emerged adult males wer...

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Cell Cycle-dependent Coupling of the Calcitonin Receptor to Different G Proteins

Cited by 131 publications

References 47 publications

Cell Cycle-dependent Coupling of the Vasopressin V1a Receptor to Different G Proteins

Cell Cycle-dependent Coupling of the Vasopressin V1a Receptor to Different G Proteins

The Deletion of 14 Amino Acids in the Seventh Transmembrane Domain of a Naturally Occurring Calcitonin Receptor Isoform Alters Ligand Binding and Selectively Abolishes Coupling to Phospholipase C

Cockroach diuretic hormones: Characterization of a calcitonin-like peptide in insects

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