1999
DOI: 10.1002/(sici)1098-2795(199906)53:2<135::aid-mrd2>3.0.co;2-j
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Molecular cloning and localization of caprine relaxin-like factor (RLF) mRNA within the goat testis
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Cited by 26 publications
(10 citation statements)
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Abstract
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“…As revealed by in situ hybridization, INSL3 mRNA is expressed in the Leydig cells that are well known as steroid hormone-producing cells (Figure 2), which is consistent with previous study [12]. However, it is unclear whether INSL3 mRNA was translated into the protein therein.…”
Section: Source and Expression Dynamics Of Insl3
supporting
confidence: 89%
Abstract
Smart CitationsHow this paper cites the one you are viewing
“…As revealed by in situ hybridization, INSL3 mRNA is expressed in the Leydig cells that are well known as steroid hormone-producing cells (Figure 2), which is consistent with previous study [12]. However, it is unclear whether INSL3 mRNA was translated into the protein therein.…”
Section: Source and Expression Dynamics Of Insl3
supporting
confidence: 89%
Abstract
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“…P49S mutation is the only mutation that might be responsible for the phenotype of TMD. This is justified by the fact that all INSL3 peptides identified among different mammalian species, contain proline at the respective to human INSL3 protein amino acid position (49) (Bathgate et al ., ; Pusch et al .,; Roche et al ., ; Hombach‐Klonisch et al ., , ; Spiess et al ., ; Zarreh‐Hoshyari‐Khah et al ., ; Klonisch et al ., ,b). It is believed that proline at this particular site is crucial for correct orientation of the neighbouring tryptophan at position 51 (Bullesbach & Schwabe, ), which is in turn crucial for INSL3 receptor binding (Bullesbach & Schwabe, ; Rosengren et al ., ).…”
Section: Discussion
mentioning
confidence: 99%
Abstract
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“…Until now, goat INSL3 is predicted to be biosynthesized as a precursor protein (pro-INSL3) containing A-and B-domains connected by a C-domain and is assumed to be an A-B heterodimer to form an active hormone (Hombach - Klonisch et al, 1999 ). However, we succeeded in isolating and purifying biologically active INSL3 from goat testes and demonstrated for the first time that it exists as a single-chain protein, and is constitutively expressed and secreted by Leydig cells.…”
Section: Discussion
mentioning
confidence: 99%
“…Therefore, the native goat INSL3 is quite similar to insulin-like growth factors (LeRoith and Roberts , 2003 ), as well as native porcine INSL3 (Minagawa et al , 2012 ), in that the proforms are not processed into two-chain peptides and exert full bioactivity. In addition to the B-C-A single-chain structure, we determined that the B-domain of the native goat INSL3 possesses an additional six residues at the N-terminus compared with the predicted sequence from the cDNA (Hombach - Klonisch et al, 1999 ). The structures of native porcine (Minagawa et al , 2012 ), bovine ( B ü llesbach and Schwabe, 2002 ), and goat INSL3 are similar in this regard.…”
Section: Discussion
mentioning
confidence: 99%
