A G Protein-coupled Receptor from Zebrafish Is Activated by Human Parathyroid Hormone and Not by Human or Teleost Parathyroid Hormone-related Peptide

Rubin, David A.; Hellman, Per; Zon, Leonard I.; Lobb, Craig J.; Bergwitz, Clemens; Jüppner, Harald

doi:10.1074/jbc.274.33.23035

Cited by 66 publications

(52 citation statements)

References 46 publications

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“…A radioimmunoassay also has been developed and validated for the peptide transcribed from this sequence, and immunoreactivity was localized to the gills, as well as the pituitary, esophagus, kidney, and intestine (650). Two relevant receptors have now been cloned from the zebrafish, one more sensitive to fugu PTHrP than human PTH (654) and another sensitive to human PTH and not human PTHrP (653). Expression of these receptors in relevant fish tissues has not been published.…”

Section: Parathyroid Hormone-related Proteinmentioning

confidence: 99%

The Multifunctional Fish Gill: Dominant Site of Gas Exchange, Osmoregulation, Acid-Base Regulation, and Excretion of Nitrogenous Waste

Evans¹,

Piermarini²,

Choe³

2005

Physiological Reviews

2,218

1,751

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The fish gill is a multipurpose organ that, in addition to providing for aquatic gas exchange, plays dominant roles in osmotic and ionic regulation, acid-base regulation, and excretion of nitrogenous wastes. Thus, despite the fact that all fish groups have functional kidneys, the gill epithelium is the site of many processes that are mediated by renal epithelia in terrestrial vertebrates. Indeed, many of the pathways that mediate these processes in mammalian renal epithelial are expressed in the gill, and many of the extrinsic and intrinsic modulators of these processes are also found in fish endocrine tissues and the gill itself. The basic patterns of gill physiology were outlined over a half century ago, but modern immunological and molecular techniques are bringing new insights into this complicated system. Nevertheless, substantial questions about the evolution of these mechanisms and control remain.

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Section: Parathyroid Hormone-related Proteinmentioning

confidence: 99%

The Multifunctional Fish Gill: Dominant Site of Gas Exchange, Osmoregulation, Acid-Base Regulation, and Excretion of Nitrogenous Waste

Evans¹,

Piermarini²,

Choe³

2005

Physiological Reviews

2,218

1,751

View full text Add to dashboard Cite

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“…(18) Immunoblots Eight rabbit polyclonal antisera specific for N-terminal hPTHrP and one rabbit polyclonal antiserum specific for N terminus hPTH were used to test the cross-reactivity with fPTH(1-34). Seven antisera (R88, R1904, R1942, R87, R1348, R196, R212) were raised against hPTHrP (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14), and one antiserum (R190) was raised against hPTHrP(1-141). The anti-PTH polyclonal was raised against hPTH(1-34) (BioGenex, San Ramon, CA, USA).…”

Section: Biological Activitymentioning

confidence: 99%

“…(11) Zebrafish PTH2R was activated by hPTH but not by hPTHrP or fPTHrP, thus suggesting that PTH might occur in fish. (12) Recent studies indicate that 39 amino acids of tuberoinfundibular peptide (TIP39) may be an endogenous ligand for the PTH2 receptor (13) and that TIP 39 could be a distant relative of PTH and PTHrP. (14) Dr Martin serves as a consultant.…”

Section: Introductionmentioning

confidence: 99%

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Identification of a Parathyroid Hormone in the Fish Fugu rubripes

Danks

Notini

et al. 2003

Journal of Bone and Mineral Research

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A PTH gene has been isolated from the fish Fugu rubripes. The encoded protein of 80 amino acid has the lowest homology with any of the PTH family members. Fugu PTH(1-34) had 5-fold lower potency than human PTH(1-34) in a mammalian cell system. Introduction: Parathyroid hormone (PTH) is the major hypercalcemic hormone in higher vertebrates. Fish lack parathyroid glands, but there have numerous attempts to identify and isolate PTH from fish. Materials and Methods: Polymerase chain reaction (PCR) was performed with primers based on preliminary data from the Joint Genome Institute database. PCR amplification was performed on genomic DNA isolated from Fugu rubripes. PCR products were purified and DNA was sequenced. All sequence was confirmed from more than one independently amplified PCR product. Multiple sequence alignments were carried out, and the percentage of identities and similarities were calculated. An unrooted phylogenetic tree, using all the known PTH and PTH-related protein (PTHrP) amino acid sequences, was determined. Synthetic peptides were tested in a biological assay that measured cyclic adenosine 3Ј,5Ј-monophosphate formation in UMR106.1 cells. Rabbit polyclonal antisera specific for N-terminal human PTHrP and one rabbit polyclonal antiserum specific for N terminus hPTH were used to test the cross-reactivity with fPTH(1-34) in immunoblots.

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“…(39) PTHR1 binds both PTH and PTHrP, (40) whereas the ligand for the PTHR2 is TIP39. (28) In ray-fin fishes, there are three receptors, Pthr1(41), Pthr2 (42), and Pthr3 (41), and Pthr3 prefers Pthrp as its ligand. (41) The receptors for the Pth gene family are yet to be identified in elephant shark.…”

Section: Discussionmentioning

confidence: 99%

Parathyroid hormone gene family in a cartilaginous fish, the elephant shark (Callorhinchus milii)

Liu¹,

Ibrahim²,

Tay³

et al. 2010

Journal of Bone and Mineral Research

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The development of bone was a major step in the evolution of vertebrates. A bony skeleton provided structural support and a calcium reservoir essential for the movement from an aquatic to a terrestrial environment. Cartilaginous fishes are the oldest living group of jawed vertebrates. In this study we have identified three members of the parathyroid hormone (Pth) gene family in a cartilaginous fish, the elephant shark (Callorhinchus milii). The three genes include two Pth genes, designated as Pth1 and Pth2, and a Pthrp gene. Phylogenetic analysis suggested that elephant shark Pth2 is an ancient gene whose orthologue is lost in bony vertebrates. The Pth1 and Pth2 genes have the same structure as the Pth gene in bony vertebrates, whereas the structure of the Pthrp gene is more complex in tetrapods compared with elephant shark. The three elephant shark genes showed distinct patterns of expression, with Pth2 being expressed only in the brain and spleen. This contrasts with localization of the corresponding proteins, which showed considerable overlap in their distribution. There were conserved sites of localization for Pthrp between elephant shark and mammals, including tissues such as kidney, skin, skeletal and cardiac muscle, pancreas, and cartilage. The elephant shark Pth1(1-34) and Pthrp(1-34) peptides were able to stimulate cAMP accumulation in mammalian UMR106.01 cells. However, Pth2(1-34) peptide did not show such PTH-like biologic activity. The presence of Pth and Pthrp genes in the elephant shark indicates that these genes played fundamental roles before their recruitment to bone development in bony jawed vertebrates. ß

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A G Protein-coupled Receptor from Zebrafish Is Activated by Human Parathyroid Hormone and Not by Human or Teleost Parathyroid Hormone-related Peptide

Cited by 66 publications

References 46 publications

The Multifunctional Fish Gill: Dominant Site of Gas Exchange, Osmoregulation, Acid-Base Regulation, and Excretion of Nitrogenous Waste

The Multifunctional Fish Gill: Dominant Site of Gas Exchange, Osmoregulation, Acid-Base Regulation, and Excretion of Nitrogenous Waste

Identification of a Parathyroid Hormone in the Fish Fugu rubripes

Parathyroid hormone gene family in a cartilaginous fish, the elephant shark (Callorhinchus milii)

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