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Biomedical subjects

M R Hanley

Publications and source records attributed to M R Hanley.

At least 19 recordsLinked to original sources

Multiple embolic events in a patient with heparin induced thrombocytopaenic thrombotic syndrome and mural thrombus.

This report describes a 55-year-old man admitted for renal colic and found to have an infarcted right kidney, for which he was treated with heparin. Heparinization for this condition was stopped on day 12 when the patient developed pain in his left foot. Heparin-induced thrombocytopaenic thrombotic syndrome was confirmed, and despite treatment with danaparoid and bilateral femoral embolectomy, a left above-knee amputation was required. Echocardiogram showed a sessile mural thrombus in the left ventricle, which was considered a likely embolic source. The preoperative development of acute renal failure delayed recovery and necessitated haemodialysis. Anticoagulation of the patient was complicated; however, warfarin was introduced slowly and with good effect.

Amputation, Surgical↗

Messenger RNA localization and further characterisation of the putative tachykinin receptor NK4 (NK3B).

We have previously shown that a cloned receptor, highly homologous to the NK3 tachykinin peptide receptor, encodes a novel functional tachykinin receptor NK4. Examining sites of receptor mRNA expression by Northern blot we show that NK4 mRNA is expressed in numerous rat tissues, in contrast to the NK3 receptor which has been shown to have a distribution principally in nervous tissues. We have localised the NK4 receptor mRNA in rat brain and spinal cord using in situ hybridisation. NK4 receptor mRNA is widely expressed in neurons in the rat central nervous system, including cerebral cortex, hippocampus, hypothalamus and dorsal horn of the spinal cord. During peripheral inflammation of the hindpaw, NK4 mRNA shows complex patterns of regulation. We have also investigated some pharmacological properties of this receptor expressed ectopically in Xenopus oocytes. We show that the functional antagonism of dynorphin at the NK4 receptor is reversed by the non-specific opioid antagonist naloxone and that tachykinin-evoked responses at the NK4 receptor are inhibited by the non-peptide NK3 receptor antagonist SR142801 in a concentration dependent manner.

Animals↗

HHV8-encoded vMIP-I selectively engages chemokine receptor CCR8. Agonist and antagonist profiles of viral chemokines.

Uncertainty regarding viral chemokine function is mirrored by an incomplete knowledge of host chemokine receptor usage by the virally encoded proteins. One such molecule is vMIP-I, a C-C type chemokine of undefined function and binding specificity, encoded by the Kaposi's sarcoma herpesvirus HHV-8. We report here that vMIP-I binds to and induces cytosolic [Ca(2+)] signals in human T cells selectively through CCR8, a CC chemokine receptor associated with Th2 lymphocytes. Furthermore, using a panel of 65 different human, viral, and rodent chemokines, we have established a comprehensive ligand binding "fingerprint" for CCR8. The receptor exhibits marked "high" affinity (K(d) < 15 nM) only for four chemokines, three of them of viral origin: vMIP-I, vMIP-II, vMCC-I, and human I-309. A previously unreported second class of lower affinity ligands includes MCP-3 and possibly two other viral chemokines. vMIP-I and I-309 appear to act as CCR8 agonists: binding to and inducing cytosolic [Ca(2+)] elevation through the receptor. By contrast, vMIP-II and vMCC-I act as potent antagonists: binding without inducing signaling, and blocking the effects of I-309 and vMIP-I. These results suggest a ligand hierarchy for CCR8, identifying vMIP-I as a selective viral chemokine agonist. CCR8 may thus engage a specific subset of chemokines with the potential to regulate each other during viral infection and immune regulation.

Animals↗

Calcium influx factor (CIF) as a diffusible messenger for the activation of capacitative calcium entry in Xenopus oocytes.

Acid extracts of thapsigargin-treated Xenopus oocytes revealed Ca2(+)-dependent Cl- currents by microinjection into Xenopus oocytes. These currents were detected in highly purified fractions by carrying out a sequence of purification steps including gel filtration chromatography and high performance thin layer chromatography. The nature of the membrane currents evoked by the highly purified fractions were carried by chloride ions as blockade by the selective chloride channel blocker 1 mM niflumic acid. Injection of the Ca2+ chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid (BAPTA) eradicated the current activities, indicating that the current responses are completely Ca2(+)-dependent. Moreover, the currents were sensitive to the removal of extracellular calcium, indicating the dependence on calcium entry through plasma membrane calcium entry channels. These results elucidate that the highly purified fractions aquired by thapsigargin-stimulated oocytes is an authentic calcium influx factor (CIF). Thus, the detection of increased CIF production from thapsigargin treatment in Xenopus oocytes would give strong support for the existence of CIF as a diffusible messenger for the activation of capacitative calcium entry pathways in Xenopus oocytes.

Animals↗

Calcium influx factor is synthesized by yeast and mammalian cells depleted of organellar calcium stores.

Depletion of endoplasmic reticulum Ca2+ stores leads to the entry of extracellular Ca2+ into the cytoplasm, a process termed capacitative or store-operated Ca2+ entry. Partially purified extracts were prepared from the human Jurkat T lymphocyte cell line and yeast in which Ca2+ stores were depleted by chemical and genetic means, respectively. After microinjection into Xenopus laevis oocytes, the extracts elicited a wave of increased cytoplasmic free Ca2+ ([Ca2+]i) that spread from the point of injection across the oocyte. Extracts from cells with replete organellar Ca2+ stores were inactive. The increases depended on extracellular Ca2+, were unaffected by the inositol 1,4,5-trisphosphate (IP3) inhibitor heparin or an anti-IP3 receptor antibody and were unchanged when the endoplasmic reticulum was segregated to the hemisphere opposite the injection site by centrifugation. Confocal microscopy revealed that [Ca2+]i increases were most pronounced at the periphery of the oocyte. The patterns of [Ca2+]i increases were replicated by computer simulations based on a diffusible messenger of about 700 Da that directly activates Ca2+ influx. In addition, ICRAC, a Ca2+ release-activated Ca2+ current monitored in Jurkat cells by whole-cell patch clamp recordings, was more rapidly activated when active extracts were included in the patch pipette than by the inclusion of a Ca2+ chelator or IP3. These data support the existence in yeast and mammalian cells depleted of Ca2+ stores of a functionally conserved diffusible calcium influx factor that directly activates Ca2+ influx.

Animals↗

Double-stranded-RNA-activated protein kinase (PKR) regulates Ca2+ stores in Xenopus oocytes.

Expression of the double-stranded-RNA-dependent protein kinase (PKR) in Xenopus oocytes attenuated Ca2+ entry-dependent membrane currents activated by depletion of Ca2+ stores, whereas expression of a dominant-negative PKR mutant had the opposite effect. These results appeared to be due to perturbation of releasable Ca2+ stores, and not actions of PKR on protein synthesis. PKR may thus have novel protein substrates and cellular functions in Ca2+ storage and signalling.

Animals↗

17beta-estradiol stimulates substance P receptor gene expression.

The actions of substance P (SP), a widely distributed tachykinin neuropeptide, are mediated by the NK1 receptor, a seven trans-membrane spanning domain cell surface receptor coupled to heterotrimeric G-proteins. SP regulates cellular processes in the CNS, placenta and vasculature including permeability, inflammation, mitogenesis and transformation. Examples of sexual dimorphism in tissue distribution and expression of SP and the SP receptor (SPR) in various organ systems (breast, uterus, brain) suggest the SPR may be under hormonal control. Using Northern blot analysis of SPR mRNA levels, we studied the effects of 17beta-estradiol (E2) on SPR gene expression in AR42J (rat pancreatic acinar) cells which constitutively express high levels of SPR. E2 (100 nM) led to a 2.5-fold increase in SPR mRNA levels (4.7 kb band) which was time- and concentration-dependent. The increase was inhibited by the RNA polymerase inhibitor actinomycin D (5 microg/ml) but not by the translational inhibitor cycloheximide (10 microg/ml). In addition, the antiestrogen tamoxifen (1 microM) blocked the stimulatory effect of E2 on SPR mRNA. Increased SPR mRNA levels in response to E2 were linearly related to increased [3H]SP binding to the SPR. This study has implications for understanding molecular mechanisms of hormonal control of receptor gene expression.

Animals↗

Inducible receptors.

While regulation of receptor function is known to occur at many levels (e.g. transcriptional, post-translational), it is generally perceived that a tissue either expresses or does not express a particular receptor in an all-or-none fashion. Many pathological (e.g. tissue injury) and physiological (e.g. angiogenesis) processes have, however, been shown to be associated with the transcriptional induction of specific receptors. Induced receptors are not confined to any particular class, but range from G protein-coupled receptors to receptor tyrosine kinases. The potential implications of de novo receptor expression are profound with respect to potential novel therapeutic targets in specific disease states. Further, this observation may explain unexpected side-effects in the pharmacotherapy of existing disease states. In this article Lucy Donaldson, Michael Hanley and Amparo Villablanca discuss circumstances under which de novo receptor induction has been described, potential mechanisms of induction and the implications for pharmacology.

Animals↗

Functional characterization by heterologous expression of a novel cloned tachykinin peptide receptor.

An orphan receptor resembling the neurokinin 3 tachykinin receptor (NK3), initially claimed to be an atypical opioid receptor, is shown herein to respond potently to the physiological NK3 receptor ligand, neurokinin B. This 'NK4' receptor did not give functional responses in Xenopus oocytes to opioid agonists. However, NK4 receptor activation was inhibited by nanomolar concentrations of dynorphin. The NK4 receptor is therefore a tachykinin receptor which is functionally antagonized by an endogenous opioid peptide.

3T3 Cells↗

Regulation of inositol trisphosphate-induced membrane currents in Xenopus oocytes by a Jurkat cell calcium influx factor.

The functional interactions of a Jurkat cell-derived calcium influx factor (CIF) with Ins(1,4,5)P3 were examined by microinjection and voltage-clamp recording of current responses in Xenopus oocytes. CIF, which stimulates Ca2+ entry directly on microinjection, was active at dilutions at which it had no direct effect by augmenting both initial rapid Ins(1,4,5)P3-mediated Ca2+ discharge-activated currents and later sustained Ca2+ entry-activated currents. Augmented initial membrane currents were 3-5-fold greater in peak amplitude than currents evoked by injection of the same dose of Ins(1,4,5)P3 alone. The augmented initial response was not decreased by removal of extracellular Ca2+, suggesting that there is potentiation of Ins(1,4,5)P3-mediated discharge from intracellular Ca2+ stores. However, the augmentation of Ins(1,4,5)P3-mediated discharge cannot be due to an enhanced production of endogenous Ins(1,4,5)P3 because maximal Ins(1,4,5)P3-activated currents saturate (approx. 500 nA) with supramaximal levels of Ins(1,4,5)P3 (10-50 microM). Depletion of Ca2+ stores, by pretreatment with thapsigargin or by prior injection with the Ins(1,4,5)P3 receptor antagonist heparin, abolished membrane currents elicited by Ins(1,4,5)P3/CIF co-injection, further suggesting that the Ins(1,4,5)P3 receptor was the target for the initial-current potentiating actions of CIF. In this regard, CIF also induced augmented initial currents with co-injection of either Ins(2,4,5)P3 or Ins(1,3,4,5)P4. The augmentation of Ins(1,4,5)P3-mediated currents by CIF was bell-shaped with regard to Ins(1,4,5)P3 concentration, reminiscent of the regulatory influence of Ca2+ on Ins(1,4,5)P3 responses. Co-injection of Ins(1,4,5)P3 and CIF also augmented (2-3-fold) later current responses arising from sustained Ca2+ entry. The augmented late-current responses were not due to enhanced Ca2+ store depletion because supramaximal levels of Ins(1,4,5)P3 (50 microM) or injection of the poorly metabolized Ins(1,4,5)P3 analogue, Ins(2,4,5)P3, cannot activate the same magnitude of Ca(2+)-entry-dependent currents. These results suggest that CIF at low levels interacts with Ins(1,4,5)P3 to sensitize two pathways of Ca2+ signalling: initial discharge and later Ca2+ entry. Thus under physiological conditions CIF might be more potent as a co-messenger than as a direct Ca2+ entry signal and might provide a novel type of direct feedback regulation between the stores-activated influx pathway and the Ins(1,4,5)P3 receptor. Moreover these results suggest that CIF modulation of the receptor for Ins(1,4,5)P3 may underlie control of both augmentation of discharge and Ca2+ entry, as has been predicted from the conformational coupling model of Ca2+ entry.

Animals↗

Stimulation of Ca(2+)-dependent membrane currents in Xenopus oocytes by microinjection of pyrimidine nucleotide-glucose conjugates.

Microinjection, but not extracellular application, of cytidine-5'-diphosphate-D-glucose (CDPG) has been shown to elicit Ca(2+)-dependent currents in Xenopus laevis oocytes. These responses were comparable to those of inositol-1,4,5-trisphosphate (InsP3) in being both rapid and dose dependent. For example, maximal amplitudes of CDPG-induced current were similar (approximately 365 +/- 75 nA at 1 microM CDPG) to those of InsP3. The CDPG currents were insensitive to removal of extracellular Ca2+, indicating the dependence on Ca2+ release from intracellular Ca2+ stores but not on Ca2+ entry through plasma membrane. CDPG-induced currents were reduced or abolished by pretreatment with thapsigargin, by injection of the Ca2+ chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid, or by extracellular perfusion of the Cl- channel blocker niflumic acid but were insensitive to injection of the InsP3 antagonist heparin. These results suggest that CDPG induces Ca2+ discharge from intracellular Ca2+ stores via a mechanism distinct from that of InsP3 in Xenopus oocytes. Another pyrimidine nucleotide-glucose derivative, uridine-5'-diphosphate-alpha-D-glucose, also induced Ca(2+)-dependent currents, but the activity was lower than that of CDPG (maximal amplitude, 272 +/- 62 nA). Other nucleotide-glucose compounds (adenosine-5'-diphosphate-D-glucose, guanosine-5'-diphosphate-D-glucose, and thymidine-5'-diphosphate-D-glucose) had no current responses when injected into oocytes. After injection of CDPG, CDPG-induced Ca2+ release appeared to couple to a Ca2+ entry pathway similar to that coupled to InsP3. These results indicate that pyrimidine nucleotide-glucose conjugates may provide novel pharmacological tools for the study of Ca2+ signaling in oocytes.

Adenosine Diphosphate Glucose↗

Diverse molecular provocation of programmed cell death.

The experimental study and manipulation of programmed cell death has been greatly assisted by the identification of genetic and pharmacological tools that can either induce or block cell lethality. This review discusses new insights into the molecular sensing of perturbations induced by such tools, as well as the possible consequences of this detection in determining cell survival.

Amyloid↗

Chromatographic resolution of an intracellular calcium influx factor from thapsigargin-activated Jurkat cells. Evidence for multiple activities influencing calcium elevation in Xenopus oocytes.

Acid extracts of thapsigargin-stimulated Jurkat cells revealed both intracellular and extracellular activities stimulating Ca(2+)-dependent Cl- currents on Xenopus laevis oocytes. Chromatographic fractionation of these extracts on gel filtration separated two active fractions of M(r) approximately 600 and 400. Moreover, the M(r) 600 fraction exhibited both intracellular and extracellular activities. However, the intracellular activity was absent from extracts of unstimulated Jurkat cells, suggesting its production was stimulated by thapsigargin. The further purification of this fraction by high performance thin layer chromatography resolved a single fraction which was active only on microinjection and which required calcium entry for activation of current responses. These results suggest that a single authentic calcium influx factor can be resolved by purification from confounding activities detected in crude acid extracts.

Animals↗

Evaluation of calcium influx factors from stimulated Jurkat T-lymphocytes by microinjection into Xenopus oocytes.

Acid extracts of thapsigargin-activated Jurkat cells have been shown to have intracellular activity in inducing a dose-dependent rapid chloride current upon microinjection in Xenopus laevis oocytes. The extracts act by elevation of calcium through calcium entry. The factor(s) responsible for this activity have been termed calcium influx factor (CIF) and have been found to be small, relatively polar molecules (< 1000 daltons) whose activity is abolished by alkaline phosphatase treatment and potentiated by co-injection of okadaic acid (a protein phosphatase inhibitor). CIF is produced in a time-dependent manner following thapsigargin treatment of Jurkat cells, being first elevated above basal levels by 2 min. Intracellular CIF activity is completely absent from NG115-401L neuronal cells, which lack capacitative entry. On this basis, it appears that Jurkat cells, activated by stimuli that deplete internal calcium stores, produce one or more CIF activities acting intracellularly, and Xenopus oocytes may be a powerful tool to purify and characterize CIFs.

Animals↗

Attenuation of agonist-induced desensitization of the rat substance P receptor by progressive truncation of the C-terminus.

We have investigated the C-terminal tail of the rat substance P receptor (SPR) as a domain essential for agonist-induced desensitization. Four progressively shorter mutants, using premature termination in the C-terminus, were constructed and compared with the unaltered SPR using ectopic expression of wild-type and mutant receptors in Xenopus oocytes. These mutants were designated D16, D47, D70 and D96 with 16, 47, 70 and 96 amino acids residues deleted from the tail, respectively. Wild type SPR, D16 and D47 exhibited normal current responses when challenged with substance P, but D70 and D96 had reduced maximal current responses (70% and 5% of wild type SPR, respectively). D70, however, exhibited substantial resistance to substance P-induced desensitization in that 55%, versus 8% for wild type SPR, of the peak current of the first response was preserved on second challenge with substance P. Therefore, a domain from residues 338 to 360 of the rat SPR, though not necessary for the functional activity of the receptor, plays an essential role in agonist-induced desensitization.

Amino Acid Sequence↗