ArticleThe Journal of biological chemistry2010
Rhesus glycoprotein p2 (Rhp2) is a novel member of the Rh family of ammonia transporters highly expressed in shark kidney.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 31 citations in OpenAlex.
- Investigating nitrogen movement in North Pacific spiny dogfish (Squalus acanthias suckleyi), with focus on UT, Rhp2, and Rhbg mRNA abundance.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2023Article
- Highly sensitive and specific responses of shrimp gill cells to high pH stress based on single cell RNA-seq analysis.Frontiers in cell and developmental biology · 2022Article
- Molecular characterization of two Rhesus glycoproteins from the euryhaline freshwater white-rimmed stingray, Himantura signifer, and changes in their transcript levels and protein abundance in the gills, kidney, and liver during brackish water acclimation.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2017Article
- Article
- Nitrogen metabolism, acid-base regulation, and molecular responses to ammonia and acid infusions in the spiny dogfish shark (Squalus acanthias).Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2015Article
- Ammonia excretion in Caenorhabditis elegans: mechanism and evidence of ammonia transport of the Rhesus protein CeRhr-1.The Journal of experimental biology · 2015Article
- Expression of a novel isoform of Na(+)/H(+) exchanger 3 in the kidney and intestine of banded houndshark, Triakis scyllium.American journal of physiology. Regulatory, integrative and comparative physiology · 2013Article
- Marine, freshwater and aerially acclimated mangrove rivulus (Kryptolebias marmoratus) use different strategies for cutaneous ammonia excretion.American journal of physiology. Regulatory, integrative and comparative physiology · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rhesus (Rh) glycoproteins are a family of membrane proteins capable of transporting ammonia. We isolated the full-length cDNA of a novel Rh glycoprotein, Rhp2, from a kidney cDNA library from the banded hound shark, Triakis scyllium. Molecular cloning and characterization indicated that Rhp2 consists of 476 amino acid residues and has 12 putative transmembrane spans, consistent with the structure of other family members. The shark Rhp2 gene was found to consist of only one coding exon. Northern blotting and in situ hybridization revealed that Rhp2 mRNA is exclusively expressed in the renal tubules of the sinus zone but not in the bundle zone and renal corpuscles. Immunohistochemical staining with a specific antiserum showed that Rhp2 is localized in the basolateral membranes of renal tubule cells. Double fluorescence labeling with phalloidin or labeling of the Na(+)/K(+)-ATPase further narrowed the location to the second and fourth loops in the sinus zone. Vacuolar type H(+)-ATPase was localized in apical membranes of the Rhp2-expressing tubule cells. Quantitative real-time PCR analysis and Western blotting showed that expression of Rhp2 was increased in response to elevation of environmental salinity. Functional analysis using the Xenopus oocyte expression system showed that Rhp2 has transport activity for methylammonium, an analog of ammonia. This transport activity was inhibited by NH(4)Cl but not trimethylamine-N-oxide and urea. These results suggested that Rhp2 is involved in ammonia reabsorption in the kidney of the elasmobranch group of cartilaginous fish comprising the sharks and rays.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.