Molecular cloning in the marmoset shows that semenogelin is not the precursor of the TRH-like peptide pGlu-Glu-Pro amide

Huber, Ariana; Fraser, Hamish M.; Rio-García, Jesús del; Kreil, Günther; Smyth, Derek G.

doi:10.1016/s0167-4838(98)00116-2

Cited by 8 publications

(8 citation statements)

References 27 publications

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“…Pyroglutamine is a key amino acid residue for thyrotrophin-releasing hormone (TRH) and TRH-like peptides (Huber et al , 1998) that promote fertilisation by enhancing sperm capacitation (Cockle et al , 1994; Huber et al , 1998), act as paracrine factors influencing prostate cell growth and differentiation (Bilek et al , 1992), and stimulate thyroid hormone secretion (Bilek et al , 1991; Bilek, 2000; Maran et al , 2001). Gamma-glutamylphenylalanine and gamma-glutamylglycine peptides were also inversely associated with aggressive prostate cancer, similar to the gamma-glutamylhistidine finding in the ATBC Study (Mondul et al , 2015).…”

Section: Discussionmentioning

confidence: 99%

Serum metabolomic profiling of prostate cancer risk in the prostate, lung, colorectal, and ovarian cancer screening trial

et al. 2016

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Background:Two recent metabolomic analyses found serum lipid, energy, and other metabolites related to aggressive prostate cancer risk up to 20 years prior to diagnosis.Methods:We conducted a serum metabolomic investigation of prostate cancer risk in the Prostate, Lung, Colorectal, and Ovarian Cancer Screening Trial that included annual serum total prostate-specific antigen measurement and digital rectal examination. This nested study included 380 cases diagnosed post-screening and 380 controls individually matched to cases on age, race, study centre, and blood-collection date (median time to diagnosis, 10 years (range 4.4–17 years)). Sera were analysed on a high-resolution accurate mass platform of ultrahigh-performance liquid and gas chromatography/mass spectroscopy that identified 695 known metabolites. Logistic regression conditioned on the matching factors estimated odds ratios (OR) and 95% confidence intervals of risk associated with an 80th percentile increase in the log-metabolite signal.Results:Twenty-seven metabolites were associated with prostate cancer at P<0.05. Pyroglutamine, gamma-glutamylphenylalanine, phenylpyruvate, N-acetylcitrulline, and stearoylcarnitine showed the strongest metabolite-risk signals (ORs=0.53, 0.51, 0.46, 0.58, and 1.74, respectively; 0.001⩽P⩽0.006). Findings were similar for aggressive disease (peptide chemical class, P=0.03). None of the P-values were below the threshold of Bonferroni correction, however.Conclusions:A unique metabolomic profile associated with post-screening prostate cancer is identified that differs from that in a previously studied, unscreened population.

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Section: Discussionmentioning

confidence: 99%

Serum metabolomic profiling of prostate cancer risk in the prostate, lung, colorectal, and ovarian cancer screening trial

et al. 2016

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“…The authors of this study noted that the peptides likely possess biological activity, since they observed the presence of an amide bond at the C-terminal, a feature believed to be essential for activity [72]. In addition, one such peptide was recently shown to increase the level of sperm capacitation [85]. However, the presence of a tryptophan residue adjacent to the C-terminal end of the peptides in Sg I instead of the usual glycine residue raises the possibility that they are generated from a precursor that strategy is based on harnessing the high specificity and affinity of peptides derived from the Sg sequence for PSA.…”

Section: Applications and Benefits Derived From Sg Imentioning

confidence: 89%

“…As elaborated above, the main functions of Sg I appear to be related to the coagulation and liquefaction of semen and the concomitant early immobilization and subsequent progressive release of motile spermatozoa in [87,88] is closely related to but different from Sg I [72,85]. Obviously, the exact physiological role of such bioactive peptides as inhibin-like peptides and TRH-like peptides in human semen remains to be established.…”

Section: Review Articlementioning

confidence: 97%

Semenogelin I: a coagulum forming, multifunctional seminal vesicle protein

Robert¹,

Gagnon²

1999

CMLS, Cell. Mol. Life Sci.

153

134

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Human seminal plasma spontaneously coagulates after ejaculation. The major component of this coagulum is semenogelin 1, a 52-kDa protein expressed exclusively in the seminal vesicles. Recently, a sperm motility inhibitor has been found to be identical to semenogelin I, suggesting that it may also be a physiological sperm motility inhibitor. The protein is rapidly cleaved after ejaculation by the chymotrypsin-like prostatic protease prostate-specific antigen, resulting in liquefaction of the semen coagulum and the progressive release of motile spermatozoa. Some of the cleavage products of Sg I may also have various biological functions. While the semenogelin I protein is unique to human and higher primates, it has recently been shown to belong to a gene family having a similar gene structure but encoding widely differing proteins. The recently elucidated characteristics of the semenogelin I gene as well as the biochemical and functional properties of the encoded protein are reviewed, and an attempt is made to integrate the various findings into a model for semen coagulation, sperm immobilization and potential other functions.

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“…The sequence of the SEMG1 transcript presented here was compared to that of a previously reported marmoset SEMG1 clone (GenBank accession number AJ005842) [17]. The latter is presumably derived from an unspliced primary transcript or genomic DNA, as it carries the second exon flanked by a few hundred base pairs of intron sequence.…”

Section: Semenogelin Imentioning

confidence: 99%

“…In contrast, investigation of the closely related common marmoset by Southern blot hybridization has shown that this species probably has two semenogelin genes [10]. The partial sequence also has been reported of a presumably unspliced transcript of marmoset SEMG1 [17].…”

Section: Introductionmentioning

confidence: 97%

The Common Marmoset (Callithrix jacchus) Has Two Very Similar Semenogelin Genes as the Result of Gene Conversion1

Valtonen‐André

Olsson

Kullberg

et al. 2007

Biology of Reproduction

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The semen coagulum proteins have undergone substantial structural changes during evolution. In primates, these seminal vesicle-secreted proteins are known as semenogelin I (SEMG1) and semenogelin II (SEMG2). Previous studies on the common marmoset (Callithrix jacchus) showed that ejaculated semen from this New World monkey contains semenogelin, but it remained unclear whether it carries both genes or only SEMG1 and no SEMG2, like the closely related cotton-top tamarin (Saguinus oedipus). In this study we show that there are two genes, both expressed in the seminal vesicles. Surprisingly, the genes show an almost perfect sequence identity in a region of 1.25 kb, encompassing nearly half of the genes and containing exon 1, intron 1, and the first 0.9 kb of exon 2. The underlying molecular mechanism is most likely gene conversion, and a phylogenetic analysis suggests that SEMG1 is the most probable donor gene. The marmoset SEMG1 in this report differs from a previously reported cDNA by a lack of nucleotides encoding one repeat of 60 amino acids, suggesting that marmoset SEMG1 displays allelic size variation. This is similar to what was recently demonstrated in humans, but in marmosets the polymorphism was generated by a repeat duplication, whereas in humans it was a deletion. Together, these studies shed new light on the evolution of semenogelins and the mechanisms that have generated the structural diversity of semen coagulum proteins.

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Molecular cloning in the marmoset shows that semenogelin is not the precursor of the TRH-like peptide pGlu-Glu-Pro amide

Cited by 8 publications

References 27 publications

Serum metabolomic profiling of prostate cancer risk in the prostate, lung, colorectal, and ovarian cancer screening trial

Serum metabolomic profiling of prostate cancer risk in the prostate, lung, colorectal, and ovarian cancer screening trial

Semenogelin I: a coagulum forming, multifunctional seminal vesicle protein

The Common Marmoset (Callithrix jacchus) Has Two Very Similar Semenogelin Genes as the Result of Gene Conversion1

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