Thyrotrophin-releasing hormone in human ejaculate

Rui, Hong-Bing; Welinder, Benny S.; Purvis, K.; Dolva, O

doi:10.1677/joe.0.1140329

Cited by 10 publications

(2 citation statements)

References 11 publications

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“…The 'TRH-like' peptides have been shown to occur in the male reproductive system and in certain regions of the brain (del Rio Garcia & Smyth, 1990). In addition, however, there have been a number of reports that the hypothalamic peptide pGlu-His-Pro amide (TRH) is present in rat prostate and testis (Pekary, Sharpe, Briggs et al 1983;Pekary, Reeve & Smith, 1986;Pekary et al 1987) and human semen (Pekary, Hershman & Friedman, 1983;Rui, Welinder, Purvis & Dolva, 1987).…”

Section: Introductionmentioning

confidence: 99%

The thyrotrophin-releasing hormone (TRH)-like peptides in rat prostate are not formed by expression of the TRH gene but are suppressed by thyroid hormone

Bílek¹,

Gkonos²,

Tavianini³

et al. 1992

Journal of Endocrinology

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Thyrotrophin-releasing hormone (TRH)-immunoreactive peptides were extracted from rat prostate and divided into two groups by mini-column cation exchange chromatography. The amounts of the peptides in each group were determined by radioimmunoassay with a TRH antiserum. The unretained peptides which lacked a basic group and the retained peptides which possessed a basic group were further purified by high-performance liquid chromatography. The unretained fraction was found to contain a series of TRH-immunoreactive peptides, one of which corresponded chromatographically to synthetic pGlu-Glu-Pro amide and another to pGlu-Phe-Pro amide. None of the TRH-immunoreactive peptides in either fraction exhibited the chromatographic behaviour of TRH. Additional evidence for the absence of TRH gene expression in the prostate was obtained by Northern blot analysis and by application of polymerase chain reaction amplification, which failed to reveal TRH mRNA. Furthermore the preproTRH-derived peptide, preproTRH(53-74), could not be detected by radioimmunoassay. The influence of thyroid status was investigated on the levels of the TRH-like peptides in the prostate. Adult rats were treated chronically with thyroxine (T4) or propylthiouracil (PTU) and the concentrations of the TRH-immunoreactive peptides were determined by chromatography and radioimmunoassay. Treatment with T4 caused the levels of the neutral and acidic TRH-like peptides to fall to approximately one-third of the levels in the controls. No significant difference from the controls was seen in the concentrations of the peptides in the prostates of rats rendered hypothyroid by administration of PTU. The results demonstrate that rat prostate contains TRH-immunoreactive peptides which are not derived from the TRH gene.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Introductionmentioning

confidence: 99%

The thyrotrophin-releasing hormone (TRH)-like peptides in rat prostate are not formed by expression of the TRH gene but are suppressed by thyroid hormone

Bílek¹,

Gkonos²,

Tavianini³

et al. 1992

Journal of Endocrinology

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“…Other reports, however, have provided Chromatographie evidence that the TRH immunoreactivity is due at least in part to peptides that differ structurally from TRH. For example, it appears that authentic TRH is present in rat prostate (Pekary, Sharp, Briggs et al 1983/3), pancreas (Martino, Lernkark, Seo et al 1978;Engler, Scanion & Jackson, 1981), testis (Pekary, Meyer, Vaillant & Hershman, 1980) and in human semen (Pekary, Hershman & Friedman, 1983a; Rui, Welinder, Purvis & Dolva, 1987) while peptides that differ from TRH but react with TRH antibodies appear to be present in rat pancreas (Youngblood, Humm & Kizer, 1979), prostate and testis (Pekary et al 1980), eye and placenta (Youngblood et al 1979) and human semen (Pekary et al 1983 ). Furthermore, analysis of rat portal blood by high-performance liquid chromatography has clearly demonstrated the presence of three cbromatographically distinct substances that react with TRH antisera, of which only one corres¬ MATERIALS AND METHODS Extraction of TRH and TRH-like peptides Tissues were dissected from male and female SpragueDawley rats (average weight 250-300 g) which were killed by stunning and decapitation.…”

Section: Introductionmentioning

confidence: 99%

Distribution of pyroglutamylpeptide amides related to thyrotrophin-releasing hormone in the central nervous system and periphery of the rat

Rio-García

Smyth²

1990

Journal of Endocrinology

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A rapid and sensitive chromatographic method is presented for determining TRH and TRH-like peptides in small quantities of tissues and fluids. The procedure was applied to screen a comprehensive range of tissues from the central nervous system (CNS) and periphery of the rat. When hydrochloric acid (100 mmol/l) was used for extraction, the TRH immunoreactivity obtained was identified solely with the known tripeptide hormone. In contrast, when weakly acidic conditions were used for extraction, neutral or acidic TRH-like peptides which lacked the histidine residue at position 2 of the hormone, but reacted with TRH antibodies, were shown to be present in addition to TRH. The TRH-like peptides in the brain were located principally in the hippocampus, brain stem and dorsal colliculi. In the periphery, TRH-like peptides were shown to be present in the male reproductive system and certain endocrine tissues. In addition, the presence of TRH-like peptides was confirmed in portal blood. The results indicate that peptides with a neutral or acidic TRH-like sequence at their C-terminus are widely distributed in the CNS and periphery of the rat. These peptides appear to occur mainly or exclusively in precursor forms from which TRH immunoreactivity can be released during extraction under weakly acidic conditions.

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The TRH‐related peptide pyroglutamylglutamylprolinamide is present in human semen

Cockle¹,

Aitken²,

Beg³

et al. 1989

FEBS Letters

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We have recently identified a novel peptide in the rabbit prostate complex which cross-reacts with an antibody to thyrotrophin-releasing hormone (TRH) and has the structure pGlu-Glu-ProNH,. In the present study, high concentrations of a TRH-related tripeptide and also a polypeptide (l&l2 kDa) containing a TRH-immunoreactive peptide at its C-terminus were detected in human semen. The low molecular mass TRH-like peptide and the immunoreactive fragment from the polypeptide were isolated from human Semen and shown to have identical structum. Amino acid analysis suggested compositions Gl%, Pro,, and after mild acid hydrolysis, the same sequence, Glu-Glu-Pro, was established for the two peptides. Fast atom bombardment (FAB) mass spectrometry yielded a pseudomolecular ion (M + H)+ of 355.38 which was identical to that of the synthetic peptide pGlu-Glu-ProN&. The data demonstrate that human semen contains the TRH-like peptide pyroglutamylglutamylprolinamide and also a polypeptide terminating in the sequence Gln-GluProNH,.

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Thyrotrophin-releasing hormone in human ejaculate

Cited by 10 publications

References 11 publications

The thyrotrophin-releasing hormone (TRH)-like peptides in rat prostate are not formed by expression of the TRH gene but are suppressed by thyroid hormone

The thyrotrophin-releasing hormone (TRH)-like peptides in rat prostate are not formed by expression of the TRH gene but are suppressed by thyroid hormone

Distribution of pyroglutamylpeptide amides related to thyrotrophin-releasing hormone in the central nervous system and periphery of the rat

The TRH‐related peptide pyroglutamylglutamylprolinamide is present in human semen

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