Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0043167 (pertussis)
 19,595 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

ESA152 is a highly hydrophobic 18 kDa sialoglycoprotein, which becomes expressed on ram sperm in the proximal cauda epididymis. ESA 152 is expressed on all regions of the sperm surface, most strongly on the posterior region of the head, most weakly on the anterior region of the head. In this paper, we show that induction of the acrosome reaction with Ca2+ ionophore causes ESA152 to be redistributed from the posterior to the anterior region of the head plasma membrane. Cross-linking ESA152 with bivalent antibody causes similar redistribution and induces the acrosome reaction. Induction of the acrosome reaction with ESA152 antibody requires Ca2+ but is insensitive to (10 ng/ml) pertussis toxin.
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PMID:Cross-linking a maturation-dependent ram sperm plasma membrane antigen induces the acrosome reaction. 187 27

Experimental allergic orchitis (EAO) was induced consistently in BALB/c mice by immunization with homologous testicular tissue homogenate emulsified in complete Freund's adjuvant (CFA) providing that the animals had received simultaneously at least 1 microgram of an extract of Bordetella pertussis rich in pertussigen. All animals thus treated developed orchitis and serum antibody to testicular antigens within 20 days after immunization. The lesions were located in testis (100%), rete testis (37%), cauda epididymis (21%), and vas deferens (37%). Ductus efferentes and caput epididymis were only rarely affected. Early lesions in the seminiferous tubules were characterized by peritubular and/or intratubular accumulation of eosinophils, neutrophils, lymphocytes, and macrophages. This was followed by aspermatogenesis. Late lesions included massive necrosis and extensive fibrosis of the seminiferous tubules. Disruption of blood-testis barrier on day 20 was evidenced by the detection of 1) perfused lanthanum deposits between Sertoli cells and surrounding inflammatory cells inside the seminiferous tubules, 2) deposits of endogenous mouse IgG in germinal epithelium, and 3) probable immune complexes (granular C3) surrounding seminiferous tubules. Murine EAO differed from that of the guinea pig in the lack of involvement of the ductus efferentes, the extensive necrosis, the abundant polymorphonuclear eosinophils in the lesion, and the exquisite requirement of concomitant injection of B. pertussis extract.
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PMID:Immunopathology of murine experimental allergic orchitis. 668 74

1. The subtypes of alpha-adrenoceptor mediating the contractile responses of the cauda epididymis of the guinea-pig were investigated. The alpha 1-adrenoceptor agonist phenylephrine, but not the alpha 2-adrenoceptor agonist, xylazine (up to 10 microM), elicited concentration-dependent contractions from preparations of cauda epididymis (EC50 3.4 microM). The L-type Ca2+ channel antagonist, nifedipine (10 microM), reduced the maximal response to phenylephrine (by 77%). Preincubation of tissues with the alpha 1B-adrenoceptor-alkylating agent, chloroethylclonidine (50 microM, 30 min), shifted phenylephrine concentration-response curves to the right (4 fold) only when the alpha 2-adrenoceptor antagonist idazoxan (100 nM) was included during the pre-incubation with chloroethylclonidine. 2. Xylazine (1 microM) significantly shifted phenylephrine concentration-response curves to the left (3 fold); this effect was attenuated by idazoxan (100 nM). Both the incubation of preparations with nifedipine (10 microM) and the pre-incubation of preparations with chloroethylclonidine (50 microM, 30 min) attenuated the potentiating effects of xylazine (1 microM). Protection of alpha 2-adrenoceptors with idazoxan (100 nM) during the chloroethylclonidine (50 microM, 30 min) incubation restored the xylazine-mediated enhancement of phenylephrine concentration-response curves. Pertussis toxin (200 ng ml-1, 24 h) attenuated the xylazine (1 microM)-mediated potentiation of phenylephrine concentration-response curves. 3. Following the pre-incubation of preparations with chloroethylclonidine (50 microM, 30 min) 5-methylurapidil (10 nM to 3 microM) shifted phenylephrine concentration-response curves, in parallel, to the right with mean pKB values in the range of 8.27 (at 10 nM 5-methylurapidil) to 7.76 (at 3 microM 5-methylurapidil), the addition of idazoxan (100 nM) to the incubation medium did not significantly affect the 5-methylurapidil (10 to 300 nM) pKB values (8.41 to 7.64, respectively). In the presence of both idazoxan (100 nM) and nifedipine (10 microM), and following the pre-incubation with chloroethylclonidine (50 microM, 30 min), 5-methylurapidil (30 to 300 nM) still shifted phenylephrine concentration-response curves to the right (pKB values 7.77 to 7.36, respectively). 4. Phenylephrine (1 microM to 1 mM) increased the accumulation of [3H]-inositol phosphates (10 fold) in preparations of cauda epididymis (EC50 12 microM). This effect was sensitive to chloroethylclonidine pretreatment (50 microM, 30 min), antagonized with low affinity by 5-methylurapidil (- log pKi 7.8), but not potentiated by xylazine (1 microM). Xylazine (10 nM - 100 microM) reversed the forskolin (10 or 30 microM) stimulated accumulation of [3H]-adenosine 3':5'-cylic monophosphate (cyclic AMP) in preparations of cauda epididymis (by approximately 45%). Incubation of tissues with both pertussis toxin (200 ng ml-1, 24 h) and pertussis toxin vehicle increased the basal activity of adenylate cyclase (3 fold) but did not increase the capacity of forskolin (30 microM) to stimulate the accumulation of [3H]-cyclic AMP in these tissues. Xylazine did not significantly inhibit the forskolin-stimulated accumulation of [3H]-cyclic AMP in either vehicle or pertussis toxin treated tissues. 5. These studies indicate that the epididymis of the guinea-pig contains alpha 1- and alpha 2-adrenoceptors. On the basis of the actions of chloroethylclonidine and 5-methylurapidil the alpha 1-adrenoceptors of this tissue may be of the alpha 1A- and alpha 1B-subtypes and are linked to both the influx of extracellular Ca2+ and to phospholipase C. The alpha 2-adrenoceptors of this tissue are negatively coupled to adenylate cyclase, sensitive to pertussis toxin, but do not amplify phenylephrine-stimulated [3H]-inositol phosphate accumulation. Stimulation of the alpha 2-adrenoceptors of this tissue may selectively potentiate the influx of extracellular Ca2+.
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PMID:Alpha-adrenoceptor mediated responses of the cauda epididymis of the guinea-pig. 893 24

1. The effects of adenosine receptor agonists upon phenylephrine-stimulated contractility and [3H]-cyclic adenosine monophosphate ([3H]-cyclic AMP) accumulation in the cauda epididymis of the guinea-pig were investigated. The alpha1-adrenoceptor agonist, phenylephrine elicited concentration dependent contractile responses from preparations of epididymis. In the absence or presence of the L-type Ca2+ channel blocker, nifedipine (10 microM) the non-selective adenosine receptor agonist, 5'-N-ethylcarboxamidoadenosine (NECA, 1 microM) shifted phenylephrine concentration-response curves to the left (4 and 5 fold respectively). Following the incubation of preparations with pertussis toxin (200 ng ml(-1) 24 h) NECA shifted phenylephrine concentration-response curves to the right (5.7+/-0.9 fold). 2. In the presence of phenylephrine (1 microM), NECA and the A1 adenosine receptor selective agonists, N6-cyclopentyladenosine (CPA) and (2S)-N6-[2-endo-norbornyl]adenosine ((S)-ENBA) elicited concentration-responses dependent contractions from preparations of epididymis (pEC50 values 8.18+/-0.19, 7.79+/-0.29 and 8.15+/-0.43 respectively). The A3 adenosine receptor agonists N6-iodobenzyl-5'-N-methylcarboxamido adenosine (IBMECA) and N6-2-(4-aminophenyl) ethyladenosine (APNEA) mimicked this effect (but only at concentrations greater than 10 microM). In the presence of 8-cyclopentyl-1,3-dipropylxanthine (DPCPX, 30 nM) CPA concentration-response curves were shifted, in parallel to the right (apparent pKB 8.75+/-0.88) and the maximal response to NECA was reduced. 3. In the presence of DPCPX (100 nM) the adenosine agonist NECA and the A2A adenosine receptor selective agonist, CGS 21680 (2-p-(2-carboxyethyl)-phenethylamino-N-ethylcarboxamido adenosine), but not CPA, inhibited phenylephrine (20 microM) stimulated contractions (pIC50 7.15+/-0.48). This effect of NECA was blocked by xanthine amine congener (XAC, 1 microM) and the A2A adenosine receptor-selective antagonist 4-(2-[7-amino-2-(2-furyl)[1,2,4]triazolo[2,3-a][1,3,5]triazin-5-++ +ylamino]ethyl)phenol (ZM 241385; 30 nM). 4. (S)-ENBA (in the absence and presence of ZM 241385, 100 nM), but not NECA or CPA inhibited the forskolin (30 microM)-stimulated accumulation of [3H]-cyclic AMP in preparations of the epididymis of the guinea-pig (by 17+6% of control). In the presence of DPCPX (100 nM) NECA and CGS 21680, but not (S)-ENBA, increased the accumulation of [3H]-cyclic AMP in preparations of epididymis (pEC50 values 5.35+/-0.35 and 6.42+/-0.40 respectively), the NECA-induced elevation of [3H]-cyclic AMP was antagonised by XAC (apparent pKB 6.88+/-0.88) and also by the A2A adenosine receptor antagonist, ZM 241385 (apparent pKB 8.60+/-0.76). 5. These studies are consistent with the action of stable adenosine analogues at post-junctional A1 and A2 adenosine receptors in the epididymis of the guinea-pig. A1 Adenosine receptors potentiate alpha1-adrenoceptor contractility, an effect blocked by pertussis toxin, but which may not be dependent upon an inhibition of adenylyl cyclase. The epididymis of the guinea-pig also contains A2 adenosine receptors, possibly of the A2A subtype, which both inhibit contractility and also stimulate adenylyl cyclase.
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PMID:A1 and A2 adenosine receptor modulation of contractility in the cauda epididymis of the guinea-pig. 980 42

By using 2-[125I]iodomelatonin receptor binding studies, we have previously demonstrated high affinity melatonin receptors, the binding activities of which are regulated by testosterone, in the corpus epididymis of rats. In this report, some of the basic molecular and cellular characteristics of these high affinity melatonin receptors in rat corpus epididymis were analyzed. MEL1A and MEL1B receptor mRNAs were expressed by rat corpus epididymal epithelial cells as revealed by in situ hybridization. Functionally, these high affinity melatonin receptors are negatively coupled to adenylyl cyclase via pertussis toxin (PTX) sensitive Gi protein and the inhibitory effects of melatonin on forskolin-stimulated cAMP accumulation were enhanced by 5alpha-dihydrotestosterone (5alpha-DHT). Interestingly, opposing interactions between melatonin and beta-adrenergic receptor signaling in rat epididymal epithelial cells were observed with melatonin inhibiting norepinephrine- and isoproterenol-stimulated cAMP accumulation. In conclusion, our data support a modulatory action of melatonin, mediated via pertussis toxin-sensitive Gi-coupled MEL1A and MEL1B receptors, in androgenic and adrenergic regulation of rat corpus epididymal epithelial cell functions.
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PMID:Molecular and cellular analyses of melatonin receptor-mediated cAMP signaling in rat corpus epididymis. 988 91

The mammalian epididymis plays an important role in sperm maturation, an important process of male reproduction. Specific high-affinity 2-[(125)I]iodomelatonin binding sites, satisfying the pharmacokinetic properties of specific receptors, have been found in the rat corpus epididymis, suggesting a direct melatonin action on epididymal physiology. Subsequent molecular and cell biology studies have identified these 2-[(125)I]iodomelatonin binding sites to be mt(1) (MEL(1A)) and MT(2) (MEL(1B)) melatonin receptor subtypes. Changes in the binding characteristics of these receptors in the rat corpus epididymis in response to castration and steroid hormones like testosterone and hydrocortisone indicated that these membrane melatonin receptors are biologically functional receptors, whose activities are differentially regulated by testosterone and hydrocortisone. These melatonin receptors are coupled to pertussis toxin (PTX)-sensitive G(i) protein and probably participate in androgenic and adrenergic regulation of rat corpus epididymal epithelial cell functions. Furthermore, rat corpus epididymal epithelial cell proliferation was stimulated by melatonin, whose action was dependent on the concentration and duration of exposure to the hormone. Interestingly, an MT(2) receptor ligand (4-phenyl-2-propionamidotetraline, 4-P-PDOT) induced a stimulatory effect on epididymal epithelial cell proliferation similar to that produced by melatonin. In contrast, a nuclear melatonin receptor agonist (1-[3-allyl-4-oxo-thiazolidine-2-ylidene]-4-methyl-thiosemi-car bazone , CGP52608) and 8-bromo-cAMP inhibited epididymal epithelial cell proliferation. Taken together, our data lead us to postulate that one of the possible physiological functions of melatonin on the rat epididymis is the stimulation of mt(1) and MT(2) melatonin receptors resulting in the inhibition of cAMP signaling and an increase in epithelial cell proliferation.
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PMID:Biological basis and possible physiological implications of melatonin receptor-mediated signaling in the rat epididymis. 1089 2

Mammalian fertilization is initiated by the species-specific binding of sperm to the zona pellucida, or egg coat. Earlier studies suggested that sperm-egg adhesion in mouse is mediated by the binding of beta1,4-galactosyltransferase-I (GalT) on the sperm surface to specific glycoside ligands on the egg coat glycoprotein, ZP3. Binding of multiple ZP3 oligosaccharides induces GalT aggregation, triggering a pertussis toxin-sensitive G-protein cascade leading to induction of the acrosome reaction. Consistent with this, sperm bearing targeted deletions in GalT are unable to bind ZP3 nor undergo ZP3-dependent acrosomal exocytosis; however, GalT-null sperm are still able to bind to the egg coat. This indicates that sperm-egg binding requires at least two independent binding mechanisms: a GalT-ZP3-independent event that mediates initial adhesion, followed by a GalT-ZP3 interaction that facilitates acrosomal exocytosis. During the past few years, novel GalT-ZP3-independent gamete receptors have been identified that appear to participate in initial gamete adhesion. On such receptor is SED1, an EGF repeat and discoidin domain protein that coats sperm as they traverse through the epididymis, and which is required for sperm to bind the egg coat. Similarly, a novel egg coat ligand is present on ovulated oocytes, but not on ovarian eggs, and which also appears to function in initial sperm binding. The identification of novel gamete receptors that are required for sperm-egg binding opens up new avenues for the development of specific contraceptive strategies.
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PMID:Identification of novel gamete receptors that mediate sperm adhesion to the egg coat. 1641 65

Mammalian fertilization is initiated by species-specific binding of the sperm to the zona pellucida, or egg coat. Previous studies suggested that sperm adhesion to the egg coat is facilitated, at least in part, through the binding of sperm surface beta1 ,4-galactosyltransferase I (GaIT) to glycoside chains on the egg coat glycoprotein, ZP3. Binding of multiple ZP3 oligosaccharides induces aggregation of GaIT within the sperm membrane, triggering, directly or indirectly, a pertussis toxin sensitive G-protein cascade leading to induction of the acrosome reaction. Consistent with this, spermatozoa bearing targeted deletions in GaIT are unable to bind ZP3 or undergo ZP3-dependent acrosomal exocytosis; however, unexpectedly, GaIT-null sperm are still able to bind to the egg coat. This indicates that sperm-egg binding requires at least two independent binding mechanisms; a GaIT-ZP3-independent event that mediates initial adhesion, followed by a GaIT-ZP3 interaction that facilitates acrosomal exocytosis. Our recent efforts have focused on the identification and characterization of these novel gamete receptors. One recently identified sperm protein that is required for sperm adhesion to the egg coat is SED1. SED1 is a bimotif protein composed of two Notch-like EGF repeats and two discoidin/complement F5/8 domains. SED1 is secreted by the epididymal epithelium and coats spermatozoa as they progress through the epididymis. Spermatozoa null for SED1 fail to bind the egg coat, illustrating its requirement for gamete adhesion. Interestingly, SED1 is also expressed by a variety of other epithelial tissues, where it appears to be required for epithelial morphogenesis and/or maintenance. A second novel gamete receptor has recently been identified on the coat of ovulated oocytes. This ZP3-independent, egg coat component is a high molecular weight, wheat germ agglutinin (WGA)-reactive glycoprotein that is derived from oviduct secretions and appears to participate in initial sperm adhesion. The amino acid sequence of this oviduct-derived ligand is currently being determined for the generation of peptide-specific antibodies and for the creation of knock out mice. The identification of novel gamete receptors that are required for sperm-egg binding opens up new avenues for the development of specific contraceptive strategies.
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PMID:Novel gamete receptors that facilitate sperm adhesion to the egg coat. 1756 85