Author Index

Total Page:16

File Type:pdf, Size:1020Kb

Author Index Author Index Page numbers in italics refer to bibliography Aarsen, P. 377, 388 Acher, R., see Chauvet, J. 165, Akutsu, H., see Ueda, E. 455, Aarsen, P. N. 253, 265 167, 168, 171, 177, 179, 180, 485 Aarsen, P. N., Caspel de Bruyn, 209 Alabaster, V.A., Bakhle, Y.S. M. van 377,388 Ackerly, J.A., Tsai, B.-S., 441,452,462,471 Aarsen, P. N., Zeegers, A. 373, Peach, M.J. 446,470,471 Aladjem, F., see Rinderknecht, 388 Ackerman, N. B., Hechmer, H. 288, 299, 308 Aarsen, P. N., see Ufkes, P.A. 361,388 Alais, C., see Jolles, P. 115,158 J. G. R. 291,299, 377, 398 Adetuyibi, A. 549, 556, 564 Albano, J., Bhoola, K.D., Aas, K., see Rapaport, S. 571, Adetuyibi, A., Mills, I.H. 401, Croker, M., Harvey, R. F., 604 421,517,518,534,535,539, Heap, P.F. 491,492,497, Abaki, K., see Yasuhara, T. 542, 549, 551, 552, 554, 556, 500,518 232,272 557,560,562,563,561 Albano, J., Bhoola, K.D., Abe, K. 610, 655 Adetuyibi, A., see Edwards, Harvey, R. F. 491,492,495, Abe, K., Seino, M., Otsuka, Y., O. M. 551, 554, 556, 557, 518 Y oshinaga, K. 534, 542 562,565 Albano, J., Bhoola, K.D., Abe, K., Watanabe, N., Adetuyibi, A., see MacFarlane, Heap, P.F., Lemon, Kumagai, N., Mouri, T., N. A. A. 526, 536, 545, 549, M.J.C. 500-503,518 Seki, T., Yoshinaga, K. 374, 552, 555, 556, 560, 561,565 Albano, J., Bhoola, K.D., 388 Adham, N., see Dyce, B.J. 67, Kingsley, G. 491,493,518 Abe, K., see Seino, J. 534,547 74 Albert, W., see Fischer, G. Abe, K., see Seino, M. 539, Anggard, E., Bohmann, S.O., 278,283 540, 547, 550, 551, 561-563, Griffin III, J.E., Larsson, C., Albertini, R. Roblero, J., 567 Maunsbach, A. B. 404, 421 Corthorn, J., Croxatto, Abe, K., see Y oshinaga, K. Aggeler, P. M., see Kaper, H. R. 541, 542 273, 285 C. K. 569, 601 Albertini, R., see Croxatto, Abell, C. W., Monahan, T. M. Aghajanian, G.K., see Guyenet, H. R. 534,535, 540, 541, 381,388 P. G. 343, 350 543,549,557,565 Abelous, J.E., Bradier, E. I, Ahnfelt-R0nne, J., see Olsen, Albertini, R. B., see Roblero, 71,489,518,549,564 U. B. 540, 547, 559, 566 J. S. 528,529,531,547,552, Abiko, T. 230, 265 Aiken, J. W., Reit, E. 334,347 567 Abiko, T., see Suzuki, K. 229, Aiken, J.W., Vane, J.R. 442, Albrecht, E., see Zelek, U. 293, 231,271 443, 462, 471 300 Abildgaard, C. F., Harrison, J. Aikin, B. S., see Cochrane, Aleksandrov, P. N., see 571,596 C. G. 14-16, 73 Barabash, R. D. 632, 646 Abildgaard, U. 69, 71 Akaike, A., see Doi, T. 313, Aleksandrov, P. N., see Abraham, J. P., see Saito, H. 349 Chernukh, A. M. 633, 646 23,56,85 Akaike, A., see Satoh, M. 321, Alekseev, O. V., see Chernukh, Abraham, J.P., see Waldmann, 354 A. M. 633, 646 R. 26,56,88 Akaike, A., see Takagi, H. Alexander, R. W., Gimbrone, Abraham, S., see Chaimoff, C. 329, 330, 355 M. A., Jr. 294, 296 376, 389 Akesson, U., see Ohlsson, K. Alexander, R. W., see Abramson, F. B., Elliott, D. F., 65,68,83 MargoJuis, H. S. 404, 423, Lindsay, D.G., Wade, R. Akimoto, S., see Moriya, H. 534, 535, 539, 540, 545, 549, 237, 266 628,656 552,554-558,560-562,565 658 Author Index Alexander, W., Gimbrone, Anderson, G.H., see Schroeder, Aoki, N., see Moroi, M. 62, M. A. 362, 388 E. T. 575, 605 70,80 Alexeenko, L. P., see Elisseeva, Anderson, M. C., Schoenfeld, Aoyagi, T., Miyata, S., Nanbo, Y. E. 441, 447, 449, 450, F.B., lams, W.B., Suwa, M., Kojima, F., Matsuzaki, 454,474,630,647 M. 586,596 M., lshizuka, M., Takeuchi, Ali, A., Guidicci, M. A., Anderson, W., Jr., see Maling, T., Umezawa, H. 203, 207 Stevenson, D. 264,266 H. M. 292, 298 Aoyagi, T., Takeuchi, T., Alimurka, K., see Ranadive, Andersson, L.-O., see Miller­ Matsuzaki, M., Kawamura, N. S. 63, 64, 83 Anderson, M. 69,80 K., Kondo, S., Hamada, M., Alkjaersig, N., see Sherry, S. Andersson, R., see Simons son, Maeda, K., Umezawa, H. 574,605 B. G. 375, 397 203,207 Allen, H., see Halushka, P. V. Andreenko, G. V., Suvorov, Aoyagi, T., Umezawa, H. 97, 540,544 A.V. 39,71 101 Alling, D. W., see Frank, Andrews, E. P., see Segrest, Aoyagi, T., see lkezawa, H. M. M. 581, 599 J. P. 151, 160 203,215 Allison, A. C., see Davies, P. Andrews, M., see Laskowski, Aoyagi, T., see Kondo, S. 203, 63,74 M., Sr. 217 217 Allison, M. E. M., see Padfield, Aoyagi, T., see Maeda, K. 203, Andrews, M.J., Jr., see Keiser, P. L. 560, 566 218 H. R. 533,534,541,545, Almeida, A. P. de, see Rocha e Aoyagi, T., see Suda, H. 203, 562, 565 Silva, M. 357,396 221 Almeida e Silva, T. c., Pelli, Andrews, P. 109, 150, 154 Aoyagi, T., see Umezawa, M. 1. R. 343, 347 Andrews, T. M., see Peart, 102 Alsever, J., see Hathaway, W.S. 419,424 Appel, W., see Marx, R. 588, W. E. 43, 77, 571, 600 Andreyenko, G. V., Suvorov, 602 Altura, B. M. 364, 388 A. V. 621,646 Appel, W., see Werle, E. 165, Amamoto, T., see Sawada, J. Andrus, V.N. 637,646 178, 185, 188,224 202,220 Araki, K., Tachibana, S., Amatnyan, A.G., see Geller, Anfinsen, C. B., see Corley, L. Uchiyama, M., Nakajima, L. 1. 638, 648 263,266 T., Yasuhara, T. 282,282 Amin, V. M., see Carretero, Angeletti, M., Sbaraglia, G., Araki, K., see Yasuhara, T. O. A. 526, 543 Campora, E. de, Frati, L. 277, 285 Amin, V. M., see Oza, N. B. 140, 141, 154, 180,201,207 Araujo, R. L., see Beraldo, B6--139, 159, 165,219,526, Angeletti, P., see Porcelli, G. W. T. 139,154 528,547 140, 141,160, 178,219 Ammons, C., see Ryan, J. W. Angeletti, P. U., see Angeletti, Araujo-Viel, M.S., see Prado, 448,449,483 R.A. 14(}"'142,154,514,518 E. S. 146, 160 Amnims, H., Gabel, D., Kasche, Angeletti, R. A., Angeletti, Arbesman, C. E., see Dolovich, V. 165,207 P. U., Calissano, P. 14(}'" J. 376,390 Amnims, H., see Kasche, V. 142, 154, 514,518 Ardelt, W., Tomczak, Z., 165,216 Angus, C. W., Lee, H.J., Ksiemy, S., Dudeh­ Amundsen, E., Nustad, K. Wilson, 1. B. 450, 459, 471 Wojciechowska, G. 64,71 584,596 Antonello, A., Baggio, B., Arens, A., Haberland, G. L. Amundsen, E., Nustad, K., Favaro, S., Zen, A., Sandei, 104, 118,154, 166, 178, 180, Waaler, B. 526, 542 F., Todesco, F., Borsatti, A. 207 Amundsen, E., Svendsen, L., 541,542 Arfors, K. E., see Svensj6, E. Venner!1ld, A. M., Laake, K. Antonello, A., see Baggio, B. 363,397 118, 154, 527,542 530,542 Arisz, L., see Donker, A.J.M. Anastasi, A., Bertaccini, G., Antonello, A., see Favaro, S. 559,565 Erspamer, V. 232, 266 541,543 Arkatov, V.A., Pekarskiy, Anastasi, A., Erspamer, V., Antonini, F. M., see Sicuteri, D. E., Surovkina, M. S., Bertaccini, G. 277,282 F. 358, 39~ 588,606 Obuchov, Y.E. 611,641, Anastasi, A., Erspamer, V., Antonio, A., see Neto, F.R. 646 Bertaccini, G., Cei, J. M. 358, 360, 394 Arkipova, S. F., Sevastyanova, 277, 282 Antonio, A., see Rocha e Silva, N. N., Lipkind, G. M., Anastasi, A., Montecucchi, P., M. 357,396, 591, 604 Popov, E. M. 261, 266 Erspamer, V., Visser, J. 278, Aoki, N., Moroi, M., Tachiya, Arman, C. G. van, Bohidar, 282 K. 71 N.R. 592,596 Author Index 659 Annstrong, D. 22, 71,244, Connane, R. H. 179, 200, Austen, K. F., see Magoon, 247,266,311,312,317,319, 206,208 E.H. 61,80 322, 323, 324, 347 Ashutosh, K., Keighley, Austen, K. F., see Olemoiyoi, Annstrong, D., Jepson, J. P., J.F.H. 434,458,471 O. 131, 133, 159, 526,547 Keele, C.A., Stewart, J. W. Assali, N. S. 411 Austen, K. P., see Orange, 3,4, 5, 71 Assali, N. S., Johnson, G. H., R. P. 376, 395 Annstrong, D., Mills, G. L., Brinkmann, C. R., Austen, K.F., see Pisano, J.J. Stewart, J. W. 22,71 Huntsman, D.J. 364,388 301,308 Annstrong, D., see Keele, Assan, C. J., see Krieger, E. M. Austen, K. F., see Ruddy, S. C. A. 316, 323, 340, 352, 460, 462, 478 586,605 591,601 Asselin, J., see Boucher, R. Austen, K. P., see Schreiber, Annstrong, D.A.J., Stewart, 442, 458, 472 A. D. 30, 62, 85 J. W. 3, 45, 71 Astapova, M. V., see Popkova, Austen, K.F., see Soter, N.A. Annstrong, S., Stewart, J. W. G. A. 229,270,618, 619, 581,606 303,307 620,653 Austen, K. F., see Talamo, Arndts, D., Raker, K.-O., Astraken, M., see Henriques, R. C. 301-304, 306, 307, Torok, P., Habennann, E. O.B. 52,77 309, 526, 548, 549, 567, 583, 166, 181,207 Astrup, T., see Moskowitz, 592, 606 Arnhold, M., see Fritz, H. 180, R.W. 22,80 Austen, K. F., see Wintroub, 185, 193,200,201,212 Atendio, W., see Nugent, B. U. 369, 375, 399 Arnhold, M., see Schiessler, H.
Recommended publications
  • Chronic Social Isolation Reduces 5-HT Neuronal Activity Via Upregulated SK3 Calcium-Activated Potassium Channels Derya Sargin1, David K Oliver1, Evelyn K Lambe1,2,3*
    SHORT REPORT Chronic social isolation reduces 5-HT neuronal activity via upregulated SK3 calcium-activated potassium channels Derya Sargin1, David K Oliver1, Evelyn K Lambe1,2,3* 1Department of Physiology, University of Toronto, Toronto, Canada; 2Department of Obstetrics and Gynaecology, University of Toronto, Toronto, Canada; 3Department of Psychiatry, University of Toronto, Toronto, Canada Abstract The activity of serotonin (5-HT) neurons is critical for mood regulation. In a mouse model of chronic social isolation, a known risk factor for depressive illness, we show that 5-HT neurons in the dorsal raphe nucleus are less responsive to stimulation. Probing the responsible cellular mechanisms pinpoints a disturbance in the expression and function of small-conductance Ca2+-activated K+ (SK) channels and reveals an important role for both SK2 and SK3 channels in normal regulation of 5-HT neuronal excitability. Chronic social isolation renders 5-HT neurons insensitive to SK2 blockade, however inhibition of the upregulated SK3 channels restores normal excitability. In vivo, we demonstrate that inhibiting SK channels normalizes chronic social isolation- induced anxiety/depressive-like behaviors. Our experiments reveal a causal link for the first time between SK channel dysregulation and 5-HT neuron activity in a lifelong stress paradigm, suggesting these channels as targets for the development of novel therapies for mood disorders. DOI: 10.7554/eLife.21416.001 Introduction *For correspondence: evelyn. Major depression is a prevalent and debilitating disease for which standard treatments remain inef- [email protected] fective. Social isolation has long been implicated as a risk factor for depression in humans Competing interests: The (Cacioppo et al., 2002,2006; Holt-Lunstad et al., 2010) and induces anxiety- and depressive-like authors declare that no behaviors in rodents (Koike et al., 2009; Wallace et al., 2009; Dang et al., 2015; Shimizu et al., competing interests exist.
    [Show full text]
  • Apamin As a Selective Blocker of the Calcium-Dependent Potassium
    Proc. NatL Acad. Sci. USA Vol. 79, pp. 1308-1312, February 1982 Neurobiology Apamin as a selective blocker of the calcium-dependent potassium channel in neuroblastoma cells: Voltage-clamp and biochemical characterization of the toxin receptor (receptor binding/neuroblastoma cell differentiation) M. HUGUES, G. ROMEY, D. DUVAL, J. P. VINCENT, AND M. LAZDUNSKI Centre de Biochimie du Centre National de la Recherche Scientifique, Facult, des Sciences, Parc Valrose, 06034 Nice Cedex, France Communicated by Jean-Marie P. Lehn, October 13, 1981 ABSTRACT This paper describes the interaction of apamin, MATERIALS AND METHODS a bee venom neurotoxin, with the mouse neuroblastoma cell mem- brane. Voltage-clamp analyses have shown thatapamin atlowcon- Cultures of Neuroblastoma Cells. Neuroblastoma cells centrations specifically blocks the Ca2"-dependent K+ channel in (clone N1E 115) were grown as described (12); they were in- differentiated neuroblastoma cells. Binding experiments with duced to differentiate in the presence of1% fetal calfserum and highly radiolabeled toxin indicate that the dissociation constant of 1.5% dimethyl sulfoxide. the apamin-receptor complex in differentiated neuroblastoma lodination ofApamin. Apamin was purified as described (13). cells is 15-22 pM and the maximal binding capacity is 12 fmol/ There is no tyrosine residue in the sequence, but there is his- mg ofprotein. The receptor is destroyed by proteases, suggesting tidine residue that is not essential for activity (4) and that can that it is a protein.The binding capacity ofneuroblastoma cells for be iodinated. It has been found that the previously radiolabeled apamin dramatically increases during the transition described to prepare "2I-labeled apamin ('p9rocedureI-apamin) (14) could from the nondifferentiated to the differentiated state.
    [Show full text]
  • Antimicrobial Activity of Apitoxin, Melittin and Phospholipase A2 of Honey Bee (Apis Mellifera) Venom Against Oral Pathogens
    Anais da Academia Brasileira de Ciências (2015) 87(1): 147-155 (Annals of the Brazilian Academy of Sciences) Printed version ISSN 0001-3765 / Online version ISSN 1678-2690 http://dx.doi.org/10.1590/0001-3765201520130511 www.scielo.br/aabc Antimicrobial activity of apitoxin, melittin and phospholipase A2 of honey bee (Apis mellifera) venom against oral pathogens LUÍS F. LEANDRO, CARLOS A. MENDES, LUCIANA A. CASEMIRO, ADRIANA H.C. VINHOLIS, WILSON R. CUNHA, ROSANA DE ALMEIDA and CARLOS H.G. MARTINS Laboratório de Pesquisas em Microbiologia Aplicada (LaPeMA), Universidade de Franca, Av. Dr. Armando Salles Oliveira, 201, Bairro Parque Universitário, 14404-600 Franca, SP, Brasil Manuscript received on November 19, 2013; accepted for publication on June 30, 2014 ABSTRACT In this work, we used the Minimum Inhibitory Concentration (MIC) technique to evaluate the antibacterial potential of the apitoxin produced by Apis mellifera bees against the causative agents of tooth decay. Apitoxin was assayed in natura and in the commercially available form. The antibacterial actions of the main components of this apitoxin, phospholipase A2, and melittin were also assessed, alone and in combination. The following bacteria were tested: Streptococcus salivarius, S. sobrinus, S. mutans, S. mitis, S. sanguinis, Lactobacillus casei, and Enterococcus faecalis. The MIC results obtained for the commercially available apitoxin and for the apitoxin in natura were close and lay between 20 and 40µg / mL, which indicated good antibacterial activity. Melittin was the most active component in apitoxin; it displayed very promising MIC values, from 4 to 40µg / mL. Phospholipase A2 presented MIC values higher than 400µg / mL. Association of mellitin with phospholipase A2 yielded MIC values ranging between 6 and 80µg / mL.
    [Show full text]
  • Top-Down Sequencing of Apis Dorsata Apamin by MALDI-TOF MS and Evidence of Its Inactivity Against Microorganisms
    Toxicon 71 (2013) 105–112 Contents lists available at SciVerse ScienceDirect Toxicon journal homepage: www.elsevier.com/locate/toxicon Top-down sequencing of Apis dorsata apamin by MALDI-TOF MS and evidence of its inactivity against microorganisms D. Baracchi a,*, G. Mazza a, E. Michelucci b, G. Pieraccini b, S. Turillazzi a,b, G. Moneti b a Department of Biologia Evoluzionistica “Leo Pardi”, University of Firenze, Via Romana 17, 50125 Firenze, Italy b Mass Spectrometry Centre, University of Firenze, Viale G. Pieraccini 6, 50139 Firenze, Italy article info abstract Article history: Apis mellifera venom is one of the best characterized venoms among Hymenoptera, yet Received 13 March 2013 relatively little is known about venom belonging to other species in the genus Apis. Received in revised form 18 May 2013 Melittin, one of the most important bioactive peptides, has been isolated and characterized Accepted 22 May 2013 in A. mellifera, Apis cerana, Apis dorsata and Apis florea, while apamin has been only Available online 7 June 2013 characterized in A. mellifera and A. cerana. At present, no information is available about the sequence of A. dorsata apamin. Moreover, while the antiseptic properties of melittin and Keywords: MCD peptides are well documented, the antimicrobial activity of apamin has never been MALDI-TOF Venom tested. In the present study, we isolated and characterized apamin from the venom of the Honeybee giant honeybee A. dorsata. We tested the activity of apamin against bacteria and yeasts in a Antimicrobial peptides microbiological assay to gain a more complete understanding of the antimicrobial Peptide sequencing competence of the medium molecular weight venom fraction.
    [Show full text]
  • Synthesis and Structure-Activity Studies of Novel Potassium K+ Ion
    P^ge Urn Replace with 30 8 ...its responce being... ...and its response is... 31 1 Dispite... Despite... 32 10 These channels were... This channel was... 33 5 ...and can be envisaged... ...and it can be envisaged... 38 13 ...with rise... ...with a rise... 42 11 etal etal. 42 13 ...of Lys^... ...or Lys^... 43 15 etal etal. 44 16 etal etal. 45 7 etal etal. 48 13 Concequently... Consequently... 49 1 etal etal. 52 14 etal etal. 52 25 ...suggeted... ...suggested... 60 2 etal etal. 77 14 ...quatermaiy... ...quaternary... 79 3 ...whch... ...which... 82 9 ...appart... ...apart... 99 6 ...excert... ...exert... 104 entry 14 26.0 + 14 26 ±14 109 9 ...propeiies... ...properties... 122 7 ...accosiated... ...associated... 123 4 —Elumo consists... -E lumo provides... 123 5 ...ralationships... ...relationships... 124 12 etal etal. 131 4 ...section 2.3... ...section 2.4... 133 12 ...IC-jS... ...Ki values... 133 13 ...500 times... ...50 times... 135 Table Kcal/raol kcal/mol 135 11 Kcal/mol kcal/mol 136 6 Kcal/mol kcal/mol 136 23 Kcal/mol kcal/mol 136 26 Kcal/mol kcal/mol 136 27 Kcal/mol kcal/mol 137 13 Kcal/mol kcal/mol 137 14 Kcal/mol kcal/mol 137 15 Kcal/mol kcal/mol 137 16 Kcal/mol kcal/mol 138 6 Kcal/mol kcal/mol 138 Table KcalAnol kcal/mol 139 9 Kcal/mol kcal/mol 139 Table Kcal/mol kcal/mol 140 Table Kcal/mol kcal/mol 141 10 Kcal/mol kcal/mol 141 12 Kcal/mol kcal/mol 143 6 ...space i.e.... ...space, i.e...
    [Show full text]
  • Crucial Role of a Shared Extracellular Loop in Apamin Sensitivity and Maintenance of Pore Shape of Small- Conductance Calcium-Activated Potassium (SK) Channels
    Crucial role of a shared extracellular loop in apamin sensitivity and maintenance of pore shape of small- conductance calcium-activated potassium (SK) channels Kate L. Weatheralla, Vincent Seutinb, Jean-François Liégeoisc, and Neil V. Marriona,1 aSchool of Physiology and Pharmacology, University of Bristol, Bristol BS8 1TD, United Kingdom; and Laboratories of bPharmacology and Groupe Interdisciplinaire de Génoprotéomique Appliquée-Neuroscience and cCentre Interfacultaire de Recherche du Médicament, University of Liège, B-4000 Liège, Belgium Edited by Michael D. Cahalan, University of California, Irvine, CA, and approved September 29, 2011 (received for review July 3, 2011) Activation of small-conductance calcium (Ca2+)-dependent potas- apamin does not behave as a classical pore blocker, but blocks sium (KCa2) channels (herein called “SK”) produces membrane hy- using an allosteric mechanism (7). Apamin also interacts with perpolarization to regulate membrane excitability. Three subtypes a serine residue in the S3–S4 extracellular loop to impart a high- (SK1–3) have been cloned and are distributed throughout the ner- sensitivity block of SK2, with mutation of the corresponding vous system, smooth muscle, and heart. It is difficult to discern the threonine in hSK1 to a serine increasing sensitivity of block of physiological role of individual channel subtypes as most blockers hSK1 by the toxin (8). Block of SK channel current by apamin is or enhancers do not discriminate between subtypes. The archetyp- clearly more complicated than these data suggest, as despite ical blocker apamin displays some selectivity between SK channel containing an identical outer pore sequence to the apamin-sen- – subtypes, with SK2 being the most sensitive, followed by SK3 and sitive hSK1 and a serine in this position in the S3 S4 loop, rSK1 – then SK1.
    [Show full text]
  • Chemical Characterization, Antioxidant, Anti-Inflammatory and Cytotoxic
    Chemical characterization, antioxidant, anti-inflammatory and cytotoxic properties of bee venom collected in Northeast Portugal Filipa Sobrala, Andreia Sampaioa, Soraia Falcãoa, Maria João R.P. Queirozb, Ricardo C. Calhelhaa,b, Miguel Vilas-Boasa,*, Isabel C.F.R. Ferreiraa,* aCentro de Investigação de Montanha (CIMO), ESA, Instituto Politécnico de Bragança, Campus de Santa Apolónia, 5300-253 Bragança, Portugal. bCentro de Química da Universidade do Minho, Campus de Gualtar, 4710-057 Braga, Portugal. * Authors to whom correspondence should be addressed (e-mail: [email protected] telephone +351-273-303219; fax +351-273-325405; e-mail: [email protected] telephone +351-273-303237; fax +351-273-325405). 1 Abstract Bee venom (BV) or apitoxin is a complex mixture of substances with reported biological activity. In the present work, five bee venom samples obtained from Apis mellifera iberiensis from the Northeast Portugal (two different apiaries) were chemically characterized and evaluated for their antioxidant, anti-inflammatory and cytotoxic properties. The LC/DAD/ESI-MSn analysis of the samples showed that melittin was the most abundant compound, followed by phospholipase A2 and apamin. All the samples revealed antioxidant and anti-inflammatory activity but without a direct relation with any of the individual chemical components identified. The results highlight that there are specific concentrations (present in BV5) in which these compounds are more active. The BV samples showed similar cytotoxicity for all the tested tumour cell lines (MCF-7, NCI-H460, HeLa and HepG2), being MCF-7 and HeLa the most susceptible ones. Nevertheless, the studied samples seem to be suitable to treat breast, hepatocellular and cervical carcinoma because at the active concentrations, the samples were not toxic for non-tumour cells (PLP2).
    [Show full text]
  • Bee Venom Phospholipase A2 Alleviates Collagen-Induced
    www.nature.com/scientificreports OPEN Bee venom phospholipase A2 alleviates collagen‑induced polyarthritis by inducing Foxp3 + regulatory T cell polarization in mice Gwang‑Muk Choi1,6, Bombi Lee2,6, Riwon Hong3, Seon‑Young Park3, Da‑Eun Cho1, Mijung Yeom2, Hi‑Joon Park2,3, Hyunsu Bae3* & Dae‑Hyun Hahm1,4,5* The mechanism underlying bee venom (BV) therapy is still controversial, with opinions ranging from constituent‑based pharmacological action to homeopathic‑like activity. The purpose of this study was to examine whether BV phospholipase A2 (bvPLA2), an enzymatic component of BV, is a novel anti‑infammatory and anti‑arthritic mediator capable of stimulating CD25+ Foxp3+ regulatory T cell (Treg) polarization in a mouse model of human rheumatoid arthritis (RA). An experimental model of RA was established in male DBA/1 mouse by 2‑week‑interval injections of 100 μg type II collagen emulsifed in complete (frst injection) or incomplete Freund’s adjuvant (second injection) at the base of the tail. During arthritis development, bvPLA2 (0.1, 0.5, 1.0 mg/kg) and/or Treg inhibitors such as anti‑CD25 antibodies and peptide 60 (P60) were injected intraperitoneally for 5 weeks. Arthritic symptoms and the expansion of Tregs were then assessed by behavioral assessments, histological and micro‑CT imaging, and fow cytometry. bvPLA2 injections signifcantly alleviated arthritic behaviors such as squeaking and joint swelling, consistent with changes seen on both histological and micro‑CT images. The anti‑arthritic efects of bvPLA2 were blocked by intraperitoneal injections of 0.25 mg/ kg anti‑CD25 antibody and 10 μg/kg P60, as determined by behavioral assessments.
    [Show full text]
  • The Effect of Bee Venom Peptides Melittin, Tertiapin, and Apamin On
    H OH metabolites OH Article The Effect of Bee Venom Peptides Melittin, Tertiapin, and Apamin on the Human Erythrocytes Ghosts: A Preliminary Study 1, 2, 1 3 Agata Swiatły-Błaszkiewicz´ y, Lucyna Mrówczy ´nska y, Eliza Matuszewska , Jan Lubawy , Arkadiusz Urba ´nski 3 , Zenon J. Kokot 1, Grzegorz Rosi ´nski 3 and Jan Matysiak 1,* 1 Department of Inorganic and Analytical Chemistry, Poznan University of Medical Sciences, 60-780 Poznan, Poland; [email protected] (A.S.-B.);´ [email protected] (E.M.); [email protected] (Z.J.K.) 2 Department of Cell Biology, Faculty of Biology, Adam Mickiewicz University in Poznan, 61-614 Poznan, Poland; [email protected] 3 Department of Animal Physiology and Development, Faculty of Biology, Adam Mickiewicz University in Poznan, 61-614 Poznan, Poland; [email protected] (J.L.); [email protected] (A.U.); [email protected] (G.R.) * Correspondence: [email protected] These two authors contributed equally to this work. y Received: 11 April 2020; Accepted: 11 May 2020; Published: 13 May 2020 Abstract: Red blood cells (RBCs) are the most abundant cells in the human blood that have been extensively studied under morphology, ultrastructure, biochemical and molecular functions. Therefore, RBCs are excellent cell models in the study of biologically active compounds like drugs and toxins on the structure and function of the cell membrane. The aim of the present study was to explore erythrocyte ghost’s proteome to identify changes occurring under the influence of three bee venom peptides-melittin, tertiapin, and apamin. We conducted preliminary experiments on the erythrocyte ghosts incubated with these peptides at their non-hemolytic concentrations.
    [Show full text]
  • (12) United States Patent (10) Patent No.: US 9,097,707 B2 Isacoffet Al
    US009097707B2 (12) United States Patent (10) Patent No.: US 9,097,707 B2 Isacoffet al. (45) Date of Patent: Aug. 4, 2015 (54) PHOTOREACTIVE REGULATOR OF 2003. O181531 A1 9, 2003 Sherris et al. PROTEIN FUNCTION AND METHODS OF 2005/0272677 A1 12/2005 Friesen et al. 2006/0252677 A1* 11/2006 Ohara et al. .................... 514/12 USE THEREOF 2007,0191411 A1 8, 2007 Smith (71) Applicant: The Regents of the University of 2009/0170901 A1* 7/2009 Borza et al. ................... 514,330 California, Oakland, CA (US) FOREIGN PATENT DOCUMENTS (72) Inventors: Ehud Y. Isacoff, Berkeley, CA (US); WO WO O2/O61415 8, 2002 Richard H. Kramer, Oakland, CA WO WO 2007/024290 3, 2007 (US); Dirk Trauner, Munich (DE): OTHER PUBLICATIONS Matthew R. Banghart, Oakland, CA (US); Matthew Volgraf, Oakland, CA Ichinose et al. (2003) Ca2+-independent, but voltage- and activity (US); Pablo Ignacio Gorostiza Langa, dependent regulation of the NMDA receptor outward K+ current in Barcelona (ES); Katharine Borges, mouse cortical neurons, vol. 551, pp. 403-417.* Centerport, NY (US) Colledge etal. (2003) Ubiquitination Regulates PSD-95 Degradation and AMPA Receptor Surface Expression, Neuron, vol. 40, No. 3, pp. (73) Assignee: The Regents of the University of 595-6O7.* California, Oakland, CA (US) Allen, C. "A Molecular Light Switch Turns Off Neural Activity”. - 2004, Nat. Neurosci., 2004, vol. 7, No. 12, p. 1291. (*) Notice: Subject to any disclaimer the term of this Banghartet al., “Light Activated Ion Channels for Remote Control of patent is extended or adjusted under 35 Neuronal Firing”, 2004, Nature Neuroscience, vol. 7, No. 12, pp.
    [Show full text]
  • Apis Mellifera) Venom
    Int. J. Electrochem. Sci., 10 (2015) 1249 - 1260 International Journal of ELECTROCHEMICAL SCIENCE www.electrochemsci.org The Electrochemical and Statistical Evaluation of Isolation of Mellitin and Apamin from Honey Bee (Apis Mellifera) Venom Hoai Viet Nguyen1,2, Zbynek Heger1,2, Marketa Kominkova1,2,Petr Michalek1,2, Jaromir Gumulec2,4, Roman Guran1,2, Antonin Pridal3, Carlos Fernandez5, David Hynek1,2, Vojtech Adam1,2, Rene Kizek1,2* 1 Department of Chemistry and Biochemistry, Laboratory metallomics and nanotechnology, Mendel University in Brno, Zemedelska 1, CZ-613 00 Brno, Czech Republic - European Union 2 Central European Institute of Technology, Brno University of Technology, Technicka 3058/10, CZ- 616 00 Brno, Czech Republic - European Union 3 Department of Zoology, Fisheries, Hydrobiology and Apiculture, Faculty of Agronomy, Mendel University in Brno, Zemedelska 1, CZ-613 00 Brno, Czech Republic - European Union 4Department of Pathological Physiology, Faculty of Medicine, Masaryk University, Kamenice 5, CZ- 625 00 Brno, Czech Republic - European Union 5School of Pharmacy and Life Sciences, Robert Gordon University, Garthdee Road, Aberdeen AB10 7GJ, United Kingdom - European Union *E-mail: [email protected] Received: 21 October 2014 / Accepted: 4 December 2014 / Published: 16 December 2014 We present in this manuscript for the first time the electrochemical and statistical evaluation of FPLC isolation of mellitin and apamin from honey bee (Apis mellifera) venom. Venoms are extremely complex blends of diverse substances that target a myriad of receptors or ion channels. Therefore, toxins, isolated from venomous organisms can be a valuable tool with diverse biological applications. In this study we decided to optimize the purification of honey bee venom by using fast protein liquid chromatography, to obtain biologically active peptide - melittin (2846.46 Da).
    [Show full text]
  • Bee Venom and Its Sub-Components: Characterization, Pharmacology, and Therapeutics
    toxins Editorial Bee Venom and Its Sub-Components: Characterization, Pharmacology, and Therapeutics Woojin Kim Department of Physiology, College of Korean Medicine, Kyung Hee University, Seoul 02453, Korea; [email protected] Bee venom, which is a complex substance produced by Apis mellifera, is widely used to treat various diseases, such as pain [1], inflammation [2], and cancer [3]. In addition, along with bee venom, a variety of sub-components are being used as therapeutic agents. How- ever, their safety is still an important concern [4], and their pharmaceutical characterization and mechanism of action are not clearly understood. Therefore, further investigation is re- quired. Bee venom contains various types of peptides (i.e., melittin, apamin), enzymes (i.e., phospholipase A2 (PLA2), hyaluronidase), biologically active amines (i.e., histamine and epinephrine), and non-peptides (i.e., amino acids). Among them, melittin is a major com- pound, as it consists of 40–50% of the dry weight of bee venom. PLA2 and apamin are other major components, accounting for 10–12% and 2–3% of dry bee venom, respectively [5]. Thus, this Special Issue has focused on the pharmaceutical characterization and therapeutic effects of bee venom and its sub-components. A total of 11 studies were published. Three reviews provided a good overview of the therapeutic effect of bee venom [6–8], and eight original research articles focused on bee venom, melittin, PLA2, and apamin [9–16]. Among these eight papers, four dealt with melittin. First, using an ultra-performance liquid chromatography-quadrupole time-of-flight mass spectrometry (UPLC-QqTOF-MS) Citation: Kim, W.
    [Show full text]