The TRH‐related peptide pyroglutamylglutamylprolinamide is present in human semen

Cockle, Sheena M.; Aitken, Alastair; Beg, Fatima; Morrell, Jane M.; Smyth, Derek G.

doi:10.1016/0014-5793(89)80900-7

Cited by 42 publications

(22 citation statements)

References 11 publications

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“…This sequence clearly confirmed the partial sequences of penaeidin-3 obtained by the biochemical methods discussed above and allowed us to unambiguously establish the complete penaeidin-3 primary structure. Assuming that the mature peptide started with a pyroglutamic acid (cyclization of the glutamine residue) (39,40), as observed by nanoES-MS-MS experiments, the mass calculated from the deduced amino acid sequence was 56.4 Da greater than the measured mass (6617.4 Da). This observation strongly suggests that penaeidin-3 can be COOHterminally amidated by elimination of a glycine residue.…”

Section: Fig 3 Daughter Ions Observed By Nanoes-ms-ms Of the Molecumentioning

confidence: 87%

Penaeidins, a New Family of Antimicrobial Peptides Isolated from the Shrimp Penaeus vannamei (Decapoda)

Destoumieux

Bulet

Loew

et al. 1997

Journal of Biological Chemistry

372

247

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We report here the isolation of three members of a new family of antimicrobial peptides from the hemolymph of shrimps Penaeus vannamei in which immune response has not been experimentally induced. The three molecules display antimicrobial activity against fungi and bacteria with a predominant activity against Gram-positive bacteria. The complete sequences of these peptides were determined by a combination of enzymatic cleavages, Edman degradation, mass spectrometry, and cDNA cloning using a hemocyte cDNA library. The mature molecules (50 and 62 residues) are characterized by an NH 2 -terminal domain rich in proline residues and a COOH-terminal domain containing three intramolecular disulfide bridges. One of these molecules is post-translationally modified by a pyroglutamic acid at the first position. Comparison of the data obtained from the cDNA clones and mass spectrometry showed that two of these peptides are probably COOHterminally amidated by elimination of a glycine residue. These molecules with no evident homology to other hitherto described antimicrobial peptides were named penaeidins.

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Section: Fig 3 Daughter Ions Observed By Nanoes-ms-ms Of the Molecumentioning

confidence: 87%

Penaeidins, a New Family of Antimicrobial Peptides Isolated from the Shrimp Penaeus vannamei (Decapoda)

Destoumieux

Bulet

Loew

et al. 1997

Journal of Biological Chemistry

372

247

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“…The binding of labeled TRH was displaced by TRH analogues but not by TRH unrelated ligands. Pyroglutamylglutamylproline-amide, a peptide structurally related to TRH isolated from the rabbit prostate, does not bind to the rTRHR2 nor to the TRHR1 expressing cells (K i Ͼ 10,000 nM) (27). The rTRHR2 receptor evoked strong transient increases in [Ca 2ϩ ] i concentration in a dose-dependent fashion when activated by various concentrations of TRH, 3-CH 3 -TRH, and pGlu-His-Pro-Gly but not by pGlu-Glu-Proamide.…”

Section: Rtrhr2: a Novel Trh Receptor Not Expressed In The Pituitarymentioning

confidence: 99%

Cloning and Characterization of a cDNA Encoding a Novel Subtype of Rat Thyrotropin-releasing Hormone Receptor

Cao

O’Donnell

et al. 1998

Journal of Biological Chemistry

129

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The thyrotropin-releasing hormone (TRH) 1 is a tripeptide (pyroglutamic acid-histidine-proline-amide) synthesized from a precursor polypeptide whose sequence contains 5 copies of the TRH sequence (5-7).Originally isolated from the hypothalamus, TRH is present in the central nervous system (thalamus, cerebral cortex, and spinal cord,) as well as in the periphery (pancreas, gastrointestinal tracts, and placenta). In the hypothalamus, TRH is synthesized by peptidergic neurons of supraoptic and paraventricular nuclei. It is then axonally transported to be stored in the median eminence. When secreted in the bloodstream, it reaches the pituitary where it stimulates the production of thyroid stimulating hormone which in turn stimulates the production of thyroxin (T 4 ) in the thyroid gland (8).In addition to this pivotal role in controlling the synthesis and secretion of thyroid stimulating hormone and other hormones from the anterior pituitary, TRH has been implicated as a neurotransmitter (9). TRH abundantly exists in the central nervous system and exogenous administration of TRH elicits a variety of behavioral changes (see Ref. 10 for a review).The distribution of TRH containing cells, fibers, or receptors suggests a potential role of TRH in the perception of noxious stimuli. TRH is present in the periaqueductal gray, the nuclei raphe magnus and pallidus, and the dorsal horn of the spinal cord. TRH-binding sites have been described in the brain, the pituitary, in both the dorsal and ventral horns of the spinal cord as well as in peripheral tissues. When injected centrally, TRH induces a short lasting supraspinal antinociception. The analgesia induced by intracerebroventricular TRH injection is powerful since it is twice as great, on a molar basis, as that of morphine (11). This TRH-induced antinociception is detected in models of chemically and mechanically, but not thermally induced pain. On the other hand, intrathecal TRH injections do not affect basal antinociceptive thresholds (11). However, it is known that TRH enhances spinal reflexes (both in vivo and in vitro) and modulates pain transmission (4,12,13). Although the mode of action of TRH at the level of the spinal cord is unclear, there is evidence suggesting that the TRH-induced facilitation of spinal transmission involves the activation of the N-methyl-D-asparatate receptor (14).TRH actions are mediated by the stimulation of specific cell surface receptors. Studies of pituitary TRH receptors have suggested that the TRHR1 receptor triggers the phospholipase C-protein kinase C transduction pathway (3,15). A cDNA sequence encoding a G-protein-coupled TRHR was originally isolated from mouse pituitary using an expression cloning strategy (15). Subsequently, several groups have described the cloning of rat TRH receptor cDNAs expressed in a pituitary tumor cell line (GH 3 ) or in the pituitary gland (1, 3). In addition, two isoforms of the rat TRHR have been shown to be generated from a single gene by alternative splicing (2). These isoforms are 387 and 412 amin...

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“…The acidic TRH-like peptide pGlu-Glu-Pro amide was first isolated from rabbit prostate [3] and since that time it has been shown to occur in the prostate of a number of other The tripeptides in the tissue extracts were determined by TRH-RIA of aliquots of the column fractions without trypsin digestion; the N-extended forms of the tripeptides in the tissue extracts were digested with trypsin prior to chromatography and the released TRH-immunoreactive peptides together with the endogenous tripeptides were chromatographed and determined by TRH-RIA. species [14,16].…”

Section: Discussionmentioning

confidence: 99%

“…The concentrations of the peptides are given in terms of synthetic TRH; pGlu-Glu-Pro amide possesses approximately 50% of the immunoreactivity of TRH [3] and pGlu-Phe-Pro amide is equally reactive [4]. The procedure employed for RIA has been described [12] except that the separation of bound from free ligand was accomplished by using 20% (w/v) polyethylene glycol (PEG) in place of activated charcoal.…”

Section: R1a Of Trh-immunoreactive Peptidesmentioning

confidence: 99%

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The TRH‐like peptides in rabbit testis are different from the TRH‐like peptide in the prostate

Linden¹,

García

Huber³

et al. 1996

FEBS Letters

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Human seminal fluid contains a number of tripeptide amides with similar structures to thyrotropin releasing hormone (TRH), two of which have been identified as pGlu-Glu-Pro amide and pGlu-Pbe-Pro amide. To determine whether these peptides originate in the same tissues and have the same molecular origin, TRH-immunoreactive peptides were extracted from the prostate and testis of the rabbit, purified by ion exchange chromatography and HPLC, and identified by co-chromatography with 3H-labelled marker peptides. In addition, trypsin digestion was used to release TRH-iike tripeptides from N-extended forms of these peptides. The sole TRH-like peptide in the prostate was shown to be pGlu-Glu-Pro amide; it was not accompanied by a detectable amount of pGhi-Phe-Pro amide. The prostate also appeared to contain a very small amount of N-extended forms of these peptides. In contrast to the prostate, the testis contained high concentrations of N-extended forms of pGlu-Phe-Pro amide but essentially no tripeptide. The testis also contained N-extended forms of two other neutral TRH-like peptides which were less hydrophobic than pGlu-Phe-Pro amide. Neither the prostate nor the testis contained a significant amount of TRH. The results show that in the rabbit the TRH-like peptides pGlu-Glu-Pro amide and pGlu-Phe-Pro amide occur in different tissues and appear to be formed from different precursors.

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The TRH‐related peptide pyroglutamylglutamylprolinamide is present in human semen

Cited by 42 publications

References 11 publications

Penaeidins, a New Family of Antimicrobial Peptides Isolated from the Shrimp Penaeus vannamei (Decapoda)

Penaeidins, a New Family of Antimicrobial Peptides Isolated from the Shrimp Penaeus vannamei (Decapoda)

Cloning and Characterization of a cDNA Encoding a Novel Subtype of Rat Thyrotropin-releasing Hormone Receptor

The TRH‐like peptides in rabbit testis are different from the TRH‐like peptide in the prostate

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