scholarly journals A Concerted Response of the Enzymes of Urea Biosynthesis during Thyroxine-induced Metamorphosis of Rana catesbeiana

1972 ◽  
Vol 247 (11) ◽  
pp. 3684-3692
Author(s):  
Robert L. Wixom ◽  
M. Kumudavalli Reddy ◽  
Philip P. Cohen
Keyword(s):  
Rana Catesbeiana

Vesicular system associated with spermiogenesis of bullfrog

1987 ◽  
Vol 45 ◽  
pp. 818-819
Author(s):  
K. C. Liu ◽  
S. F. Tsay
Keyword(s):  
Electron Microscopy ◽  
Microscopic Study ◽  
Electron Microscopic Study ◽  
Reproductive System ◽  
Seminiferous Tubule ◽  
Rana Catesbeiana ◽  
Routine Procedure ◽  
Electron Microscopic ◽  
Twisted Tubules ◽  
Electron Lucent

In the histologic and electron microscopic study of the male reproductive system of bullfrog, Rana catesbeiana, a vesicular system associated with spermiogenesis was observed. It appeared in the lumenal space of the seminiferous tubule (Fig. 1), in the heads of spermatids (Fig. 2), associated with the chromatins of the spermatid (Fig. 4). As deduced from sections, this vesicular system consisted of vesicles of various size or a large group of waving and twisted tubules (Fig. 3), After routine procedure of treatment for electron microscopy, the lumens of both of the vesicles and tubules were electron lucent.In human, vesicles and vesicular system associated with reproductive cell and tissue were reported. In abnormal spermiogenesis, flower-like body, actually vesicles, and giant vesicle associated with the head of spermatid were observed. In both cases the number of vesicle was limited from a single one to a few.

Synergistic Cytotoxicity of Rana catesbeiana Ribonuclease and IFN-γ on Hepatoma Cells

2001 ◽  
Vol 280 (5) ◽  
pp. 1229-1236 ◽  
Author(s):  
Chih-Chi Andrew Hu ◽  
Yu-Hsiu Lee ◽  
Chih-Hang Anthony Tang ◽  
Jiin-Tsuey Cheng ◽  
Jaang-Jiun Wang
Keyword(s):  
Rana Catesbeiana ◽  
Hepatoma Cells ◽  
Synergistic Cytotoxicity ◽  
Ifn Γ

scholarly journals Phosphorylation of an inhibitory subunit of cGMP phosphodiesterase in Rana catesbeiana rod photoreceptors. I. Characterization of the phosphorylation.

1994 ◽  
Vol 269 (21) ◽  
pp. 15024-15029
Author(s):  
S. Tsuboi ◽  
H. Matsumoto ◽  
K.W. Jackson ◽  
K. Tsujimoto ◽  
T. Williams ◽  
...  
Keyword(s):  
Rana Catesbeiana ◽  
Rod Photoreceptors ◽  
Cgmp Phosphodiesterase

scholarly journals Identification and characterization of amphibian SLC26A5 using RNA-Seq

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Zhongying Wang ◽  
Qixuan Wang ◽  
Hao Wu ◽  
Zhiwu Huang
Keyword(s):  
Amino Acid ◽  
Inner Ear ◽  
Hair Cells ◽  
Rana Catesbeiana ◽  
Site Directed Mutagenesis ◽  
Amino Acid Residues ◽  
Rna Seq ◽  
American Bullfrog ◽  
Frog Species

Abstract Background Prestin (SLC26A5) is responsible for acute sensitivity and frequency selectivity in the vertebrate auditory system. Limited knowledge of prestin is from experiments using site-directed mutagenesis or domain-swapping techniques after the amino acid residues were identified by comparing the sequence of prestin to those of its paralogs and orthologs. Frog prestin is the only representative in amphibian lineage and the studies of it were quite rare with only one species identified. Results Here we report a new coding sequence of SLC26A5 for a frog species, Rana catesbeiana (the American bullfrog). In our study, the SLC26A5 gene of Rana has been mapped, sequenced and cloned successively using RNA-Seq. We measured the nonlinear capacitance (NLC) of prestin both in the hair cells of Rana’s inner ear and HEK293T cells transfected with this new coding gene. HEK293T cells expressing Rana prestin showed electrophysiological features similar to that of hair cells from its inner ear. Comparative studies of zebrafish, chick, Rana and an ancient frog species showed that chick and zebrafish prestin lacked NLC. Ancient frog’s prestin was functionally different from Rana. Conclusions We mapped and sequenced the SLC26A5 of the Rana catesbeiana from its inner ear cDNA using RNA-Seq. The Rana SLC26A5 cDNA was 2292 bp long, encoding a polypeptide of 763 amino acid residues, with 40% identity to mammals. This new coding gene could encode a functionally active protein conferring NLC to both frog HCs and the mammalian cell line. While comparing to its orthologs, the amphibian prestin has been evolutionarily changing its function and becomes more advanced than avian and teleost prestin.

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