메뉴 건너뛰기




Volumn 28, Issue 1, 2007, Pages 136-145

In vitro transport of an allatostatin across the foregut of Manduca sexta larvae and metabolism by the gut and hemolymph

Author keywords

Insect; MALDI TOF; Mass spectrometry; Metabolism; Neuropeptide; Protease inhibitor

Indexed keywords

1,10 PHENANTHROLINE; ALLATOSTATIN; AMASTATIN; BESTATIN; CYDIASTATIN; EDETIC ACID; ENZYME; UNCLASSIFIED DRUG;

EID: 33845786397     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2006.09.018     Document Type: Article
Times cited : (8)

References (59)
  • 1
    • 0003653070 scopus 로고
    • Sequencing of proteins and peptides
    • Work T.S., and Burdon R.H. (Eds), Elsevier Science Publishers, Amsterdam
    • Allen G. Sequencing of proteins and peptides. In: Work T.S., and Burdon R.H. (Eds). Laboratory Techniques in Biochemistry and Molecular Biology (1986), Elsevier Science Publishers, Amsterdam
    • (1986) Laboratory Techniques in Biochemistry and Molecular Biology
    • Allen, G.1
  • 2
    • 0036126229 scopus 로고    scopus 로고
    • Metabolism of Manduca sexta allatostatin by hemolymph of larvae of the tomato moth, Lacanobia oleracea
    • Audsley N., Weaver R.J., and Edwards J.P. Metabolism of Manduca sexta allatostatin by hemolymph of larvae of the tomato moth, Lacanobia oleracea. Peptides 23 (2002) 171-723
    • (2002) Peptides , vol.23 , pp. 171-723
    • Audsley, N.1    Weaver, R.J.2    Edwards, J.P.3
  • 3
    • 0036848395 scopus 로고    scopus 로고
    • Degradation of Manduca sexta allatostatin and allatotropin by proteases associated with the foregut Lacanobia oleracea larvae
    • Audsley N., Weaver R.J., and Edwards J.P. Degradation of Manduca sexta allatostatin and allatotropin by proteases associated with the foregut Lacanobia oleracea larvae. Peptides 23 (2002) 2015-2023
    • (2002) Peptides , vol.23 , pp. 2015-2023
    • Audsley, N.1    Weaver, R.J.2    Edwards, J.P.3
  • 4
    • 0242322706 scopus 로고    scopus 로고
    • Identification of neuropeptides from brains of larval Manduca sexta and Lacanobia oleracea using MALDI-TOF mass spectrometry and post-source decay
    • Audsley N., and Weaver R.J. Identification of neuropeptides from brains of larval Manduca sexta and Lacanobia oleracea using MALDI-TOF mass spectrometry and post-source decay. Peptides 24 (2003) 1465-1474
    • (2003) Peptides , vol.24 , pp. 1465-1474
    • Audsley, N.1    Weaver, R.J.2
  • 5
    • 0242329823 scopus 로고    scopus 로고
    • A comparison of the neuropeptides from the retrocerebral complex of adult male and female Manduca sexta using MALDI-TOF mass spectrometry
    • Audsley N., and Weaver R. A comparison of the neuropeptides from the retrocerebral complex of adult male and female Manduca sexta using MALDI-TOF mass spectrometry. Regul Pept 116 (2003) 127-137
    • (2003) Regul Pept , vol.116 , pp. 127-137
    • Audsley, N.1    Weaver, R.2
  • 6
    • 11144256340 scopus 로고    scopus 로고
    • Endopeptidase activity of larval Laconobia oleracea corpus allatum: metabolism of Manduca sexta allatostatin and allatotropin
    • Audsley N., and Weaver R. Endopeptidase activity of larval Laconobia oleracea corpus allatum: metabolism of Manduca sexta allatostatin and allatotropin. Arch Insect Biochem Physiol 57 (2004) 178-189
    • (2004) Arch Insect Biochem Physiol , vol.57 , pp. 178-189
    • Audsley, N.1    Weaver, R.2
  • 7
    • 11144274444 scopus 로고    scopus 로고
    • Neuropeptides associated with the frontal ganglion of larval Lepidoptera
    • Audsley N., Matthews J., and Weaver R.J. Neuropeptides associated with the frontal ganglion of larval Lepidoptera. Peptides 26 (2005) 11-21
    • (2005) Peptides , vol.26 , pp. 11-21
    • Audsley, N.1    Matthews, J.2    Weaver, R.J.3
  • 8
    • 0010277167 scopus 로고
    • Intestinal absorption of proctolin in Helicoverpa armigera (Lepidoptera noctuidae) larvae
    • Bavoso A., Falabella P., Giacometti R., Halane A.J., Ostuni A., Pennacchio F., et al. Intestinal absorption of proctolin in Helicoverpa armigera (Lepidoptera noctuidae) larvae. Redia 78 (1995) 173-185
    • (1995) Redia , vol.78 , pp. 173-185
    • Bavoso, A.1    Falabella, P.2    Giacometti, R.3    Halane, A.J.4    Ostuni, A.5    Pennacchio, F.6
  • 9
    • 0242406849 scopus 로고    scopus 로고
    • Typsin-modulating oostatic factor: a potential new larvicide for mosquito control
    • Borovsky D. Typsin-modulating oostatic factor: a potential new larvicide for mosquito control. J Exp Biol 206 (2003) 3869-3875
    • (2003) J Exp Biol , vol.206 , pp. 3869-3875
    • Borovsky, D.1
  • 10
    • 0029012218 scopus 로고
    • Feeding the mosquito Aedes aegypti with TMOF and its analogues: effect on trypsin biosynthesis and egg development
    • Borovsky D., and Mahmood F. Feeding the mosquito Aedes aegypti with TMOF and its analogues: effect on trypsin biosynthesis and egg development. Regul Pept 57 (1995) 273-281
    • (1995) Regul Pept , vol.57 , pp. 273-281
    • Borovsky, D.1    Mahmood, F.2
  • 11
    • 0001721683 scopus 로고
    • The role of the frontal ganglion and corpora cardiaca corpora allata complex in post-feeding weight loss in adult Heliothis zea
    • Bushman D.W., and Nelson J.O. The role of the frontal ganglion and corpora cardiaca corpora allata complex in post-feeding weight loss in adult Heliothis zea. Physiol Entomol 15 (1990) 269-274
    • (1990) Physiol Entomol , vol.15 , pp. 269-274
    • Bushman, D.W.1    Nelson, J.O.2
  • 13
    • 0001256294 scopus 로고
    • Metabolic stimulation of transepithelial potential difference across the midgut of the tobacco hornworm (Manduca sexta)
    • Chamberlin M.E. Metabolic stimulation of transepithelial potential difference across the midgut of the tobacco hornworm (Manduca sexta). J Exp Biol 141 (1989) 295-311
    • (1989) J Exp Biol , vol.141 , pp. 295-311
    • Chamberlin, M.E.1
  • 14
    • 0001701325 scopus 로고
    • Midgut protease activities in 12 phytophagous lepidopteran larvae-dietary and protease inhibitor interactions
    • Christeller J.T., Laing W.A., Markwick N.P., and Burgess E.P.J. Midgut protease activities in 12 phytophagous lepidopteran larvae-dietary and protease inhibitor interactions. Insect Biochem Mol Biol 22 (1992) 735-746
    • (1992) Insect Biochem Mol Biol , vol.22 , pp. 735-746
    • Christeller, J.T.1    Laing, W.A.2    Markwick, N.P.3    Burgess, E.P.J.4
  • 15
    • 77956750113 scopus 로고
    • Insect Midgut Function
    • Dow J.A.T. Insect Midgut Function. Adv Insect Physiol 19 (1986) 87-328
    • (1986) Adv Insect Physiol , vol.19 , pp. 87-328
    • Dow, J.A.T.1
  • 16
    • 0030955849 scopus 로고    scopus 로고
    • Identification, tissue localisation and physiological effect in vitro of a neuroendocrine peptide identical to a dipteran Leu-callatostatin in the codling moth Cydia pomonella (Tortricidae: Lepidoptera)
    • Duve H., Johnsen A.H., Maestro J.L., Scott A.G., Crook N., Winstanley D., et al. Identification, tissue localisation and physiological effect in vitro of a neuroendocrine peptide identical to a dipteran Leu-callatostatin in the codling moth Cydia pomonella (Tortricidae: Lepidoptera). Cell Tissue Res 289 (1997) 73-83
    • (1997) Cell Tissue Res , vol.289 , pp. 73-83
    • Duve, H.1    Johnsen, A.H.2    Maestro, J.L.3    Scott, A.G.4    Crook, N.5    Winstanley, D.6
  • 18
    • 0033604315 scopus 로고    scopus 로고
    • Regulation of lepidopteran foregut movement by allatostatins and allatotropin from the frontal ganglion
    • Duve H., East P.D., and Thorpe A. Regulation of lepidopteran foregut movement by allatostatins and allatotropin from the frontal ganglion. J Comp Neurol 413 (1999) 405-416
    • (1999) J Comp Neurol , vol.413 , pp. 405-416
    • Duve, H.1    East, P.D.2    Thorpe, A.3
  • 19
    • 0034088347 scopus 로고    scopus 로고
    • Triple co-localisation of two types of allatostatin and an allatotropin in the frontal ganglion of the lepidopteran Lacanobia oleracea (Noctuidae): innervation and action on the foregut
    • Duve H., Audsley N., Weaver R.J., and Thorpe A. Triple co-localisation of two types of allatostatin and an allatotropin in the frontal ganglion of the lepidopteran Lacanobia oleracea (Noctuidae): innervation and action on the foregut. Cell Tissue Res 300 (2000) 153-163
    • (2000) Cell Tissue Res , vol.300 , pp. 153-163
    • Duve, H.1    Audsley, N.2    Weaver, R.J.3    Thorpe, A.4
  • 20
    • 0141993551 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme (ACE) activity of the tomato moth, Lacanobia oleracea: changes in levels of activity during development and after copulation suggest roles during metamorphosis and reproduction
    • Ekbote U.V., Weaver R.J., and Isaac R.E. Angiotensin I-converting enzyme (ACE) activity of the tomato moth, Lacanobia oleracea: changes in levels of activity during development and after copulation suggest roles during metamorphosis and reproduction. Insect Biochem Mol Biol 33 (2003) 989-998
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 989-998
    • Ekbote, U.V.1    Weaver, R.J.2    Isaac, R.E.3
  • 21
    • 0035013453 scopus 로고    scopus 로고
    • In vitro and in vivo binding of snowdrop (Galanthus nivalis agglutinin; GNA) and jackbean (Canavalia ensiformis; Con A) lectins within tomato moth (Lacanobia oleracea) larvae: mechanisms of insecticidal action
    • Fitches E., Woodhouse S., Edwards J.P., and Gatehouse J.A. In vitro and in vivo binding of snowdrop (Galanthus nivalis agglutinin; GNA) and jackbean (Canavalia ensiformis; Con A) lectins within tomato moth (Lacanobia oleracea) larvae: mechanisms of insecticidal action. J. Insect Physiol 47 (2001) 777-787
    • (2001) J. Insect Physiol , vol.47 , pp. 777-787
    • Fitches, E.1    Woodhouse, S.2    Edwards, J.P.3    Gatehouse, J.A.4
  • 22
    • 0036891358 scopus 로고    scopus 로고
    • Fusion proteins containing neuropeptides as novel insect control agents: snowdrop lectin delivers fused allatostatin to insect hemolymph following oral ingestion
    • Fitches E., Audsley N., Gatehouse J.A., and Edwards J.P. Fusion proteins containing neuropeptides as novel insect control agents: snowdrop lectin delivers fused allatostatin to insect hemolymph following oral ingestion. Insect Biochem Mol Biol 32 (2002) 1653-1661
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 1653-1661
    • Fitches, E.1    Audsley, N.2    Gatehouse, J.A.3    Edwards, J.P.4
  • 23
    • 0030727771 scopus 로고    scopus 로고
    • Hormonal regulation in insects: facts, gaps, and future directions
    • Gäde G., Hoffmann K.-H., and Spring J.H. Hormonal regulation in insects: facts, gaps, and future directions. Physiol Rev 77 (1997) 963-1032
    • (1997) Physiol Rev , vol.77 , pp. 963-1032
    • Gäde, G.1    Hoffmann, K.-H.2    Spring, J.H.3
  • 24
    • 19244383044 scopus 로고    scopus 로고
    • Insect peptide hormones: a selective review of their physiology and potential application for pest control
    • Gäde G., and Goldsworthy G.J. Insect peptide hormones: a selective review of their physiology and potential application for pest control. Pest Manage Sci 59 (2003) 1063-1075
    • (2003) Pest Manage Sci , vol.59 , pp. 1063-1075
    • Gäde, G.1    Goldsworthy, G.J.2
  • 25
    • 0030889622 scopus 로고    scopus 로고
    • Degradation of Dip-allatostatins by hemolymph from the cockroach Diploptera punctata
    • Garside C.S., Hayes T.K., and Tobe S.S. Degradation of Dip-allatostatins by hemolymph from the cockroach Diploptera punctata. Peptides 18 (1997) 17-25
    • (1997) Peptides , vol.18 , pp. 17-25
    • Garside, C.S.1    Hayes, T.K.2    Tobe, S.S.3
  • 26
    • 0030859720 scopus 로고    scopus 로고
    • Inactivation of Dip-allatostatin 5 by membrane preparations from the cockroach, Diploptera punctata
    • Garside C.S., Hayes T.K., and Tobe S.S. Inactivation of Dip-allatostatin 5 by membrane preparations from the cockroach, Diploptera punctata. Gen Comp Endocrin 108 (1997) 258-270
    • (1997) Gen Comp Endocrin , vol.108 , pp. 258-270
    • Garside, C.S.1    Hayes, T.K.2    Tobe, S.S.3
  • 27
    • 0033875827 scopus 로고    scopus 로고
    • Injection of Dip-allatostatin or Dip-allatostatin pseudopeptides into mated female Diploptera punctata inhibits endogenous rates of JH biosynthesis and basal oocyte growth
    • Garside C.S., Nachman R.J., and Tobe S.S. Injection of Dip-allatostatin or Dip-allatostatin pseudopeptides into mated female Diploptera punctata inhibits endogenous rates of JH biosynthesis and basal oocyte growth. Insect Biochem Mol Biol 30 (2000) 703-710
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 703-710
    • Garside, C.S.1    Nachman, R.J.2    Tobe, S.S.3
  • 28
    • 0036596291 scopus 로고    scopus 로고
    • Uptake, flow, and digestion of casein and green fluorescent protein in the digestive system of Lygus hesperus Knight
    • Habibi J., Brandt S.L., Coudron T.A., Wagner R.M., Wright M.K., Backus E.A., et al. Uptake, flow, and digestion of casein and green fluorescent protein in the digestive system of Lygus hesperus Knight. Arch Insect Biochem Physiol 50 (2002) 62-74
    • (2002) Arch Insect Biochem Physiol , vol.50 , pp. 62-74
    • Habibi, J.1    Brandt, S.L.2    Coudron, T.A.3    Wagner, R.M.4    Wright, M.K.5    Backus, E.A.6
  • 29
    • 0032445750 scopus 로고    scopus 로고
    • Recent advances in hormones in insect pest control
    • Hoffmann K.H., and Lorenz M.W. Recent advances in hormones in insect pest control. Phytoparasitica 26 (1998) 323-330
    • (1998) Phytoparasitica , vol.26 , pp. 323-330
    • Hoffmann, K.H.1    Lorenz, M.W.2
  • 30
    • 0000319218 scopus 로고    scopus 로고
    • Insect angiotensin-converting enzyme: comparative biochemistry and evolution
    • Coast G.M., and Webster S.G. (Eds), Cambridge University Press, Cambridge
    • Isaac R.E., Coates D., Williams T.A., and Schoofs L. Insect angiotensin-converting enzyme: comparative biochemistry and evolution. In: Coast G.M., and Webster S.G. (Eds). Recent Advances in Arthropod Endocrinology (1998), Cambridge University Press, Cambridge 357-378
    • (1998) Recent Advances in Arthropod Endocrinology , pp. 357-378
    • Isaac, R.E.1    Coates, D.2    Williams, T.A.3    Schoofs, L.4
  • 31
    • 0033387605 scopus 로고    scopus 로고
    • A processing enzyme with broad substrate specificity and a role in reproduction
    • Isaac R.E., Ekbote U., Coates D., and Shirras A.D. A processing enzyme with broad substrate specificity and a role in reproduction. Ann NY Acad Sci 897 (1999) 342-347
    • (1999) Ann NY Acad Sci , vol.897 , pp. 342-347
    • Isaac, R.E.1    Ekbote, U.2    Coates, D.3    Shirras, A.D.4
  • 32
    • 0029138570 scopus 로고
    • Protease activities in the larval midgut of Heliothis virescens: evidence for trypsin and chymotrypsin-like enzymes
    • Johnston K.A., Lee M., Brough C., Hilder V.A., Gatehouse A.M.R., and Gatehouse J.A. Protease activities in the larval midgut of Heliothis virescens: evidence for trypsin and chymotrypsin-like enzymes. Insect Biochem Mol Biol 25 (1995) 375-383
    • (1995) Insect Biochem Mol Biol , vol.25 , pp. 375-383
    • Johnston, K.A.1    Lee, M.2    Brough, C.3    Hilder, V.A.4    Gatehouse, A.M.R.5    Gatehouse, J.A.6
  • 33
    • 38249036101 scopus 로고
    • Speculations on biotechnology applications for insect neuroendocrine research
    • Keeley L.L., and Hayes T.K. Speculations on biotechnology applications for insect neuroendocrine research. Insect Biochem 17 (1987) 639-651
    • (1987) Insect Biochem , vol.17 , pp. 639-651
    • Keeley, L.L.1    Hayes, T.K.2
  • 34
    • 0027685748 scopus 로고
    • Metabolism of insect neuropeptides: properties of a membrane-bound endopeptidase from heads of Musca domestica
    • Lamango N.S., and Isaac R.E. Metabolism of insect neuropeptides: properties of a membrane-bound endopeptidase from heads of Musca domestica. Insect Biochem Mol Biol 23 (1993) 801-808
    • (1993) Insect Biochem Mol Biol , vol.23 , pp. 801-808
    • Lamango, N.S.1    Isaac, R.E.2
  • 35
    • 0026298119 scopus 로고
    • Digestive proteinases of larvae of the corn earworm, Heliothis zea: characterisation, distribution, and dietary relationships
    • Lenz C.J., Kang J., Rice W.C., McIntosh A.H., Chippendale G.M., and Schubert K.R. Digestive proteinases of larvae of the corn earworm, Heliothis zea: characterisation, distribution, and dietary relationships. Arch Insect Biochem Physiol 16 (1991) 201-212
    • (1991) Arch Insect Biochem Physiol , vol.16 , pp. 201-212
    • Lenz, C.J.1    Kang, J.2    Rice, W.C.3    McIntosh, A.H.4    Chippendale, G.M.5    Schubert, K.R.6
  • 36
    • 0031441709 scopus 로고    scopus 로고
    • Metabolism of an insect diuretic hormone by Malpighian tubules studied by liquid chromatography coupled with electrospray ionisation mass spectrometry
    • Li H., Wang H., Schegg K.M., and Schooley D.A. Metabolism of an insect diuretic hormone by Malpighian tubules studied by liquid chromatography coupled with electrospray ionisation mass spectrometry. Proc Natl Acad Sci USA 94 (1997) 13463-13468
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13463-13468
    • Li, H.1    Wang, H.2    Schegg, K.M.3    Schooley, D.A.4
  • 37
    • 0001168035 scopus 로고
    • The permeability of the cuticular lining of the insect alimentary canal
    • Maddrell S.H.P., and Gardiner B.O.C. The permeability of the cuticular lining of the insect alimentary canal. J Exp Biol 85 (1980) 227-237
    • (1980) J Exp Biol , vol.85 , pp. 227-237
    • Maddrell, S.H.P.1    Gardiner, B.O.C.2
  • 38
    • 0027350489 scopus 로고
    • Insect neuropeptides: discovery and application in insect management
    • Masler E.P., Kelly J.T., and Menn J.J. Insect neuropeptides: discovery and application in insect management. Arch Insect Biochem Physiol 22 (1993) 87-111
    • (1993) Arch Insect Biochem Physiol , vol.22 , pp. 87-111
    • Masler, E.P.1    Kelly, J.T.2    Menn, J.J.3
  • 39
    • 0022588434 scopus 로고
    • Transport of peroxidase through the midgut epithelium of Glossinia m. morsitans (Diptera, Glossiinidae)
    • Modespacher U.P., Rudin W., Jenni L., and Hecker H. Transport of peroxidase through the midgut epithelium of Glossinia m. morsitans (Diptera, Glossiinidae). Tissue Cell 18 (1986) 429-436
    • (1986) Tissue Cell , vol.18 , pp. 429-436
    • Modespacher, U.P.1    Rudin, W.2    Jenni, L.3    Hecker, H.4
  • 40
    • 0001836781 scopus 로고    scopus 로고
    • Mimetic analogues of the myotropic/duiretic insect kinin neuropeptide family
    • Coast G.M., and Webster S.G. (Eds), Cambridge University Press, Cambridge
    • Nachman R.J., Holman M.G., and Coast G.M. Mimetic analogues of the myotropic/duiretic insect kinin neuropeptide family. In: Coast G.M., and Webster S.G. (Eds). Recent Advances in Arthropod Endocrinology (1998), Cambridge University Press, Cambridge 379-391
    • (1998) Recent Advances in Arthropod Endocrinology , pp. 379-391
    • Nachman, R.J.1    Holman, M.G.2    Coast, G.M.3
  • 41
    • 0032954543 scopus 로고    scopus 로고
    • Hemolymph and tissue-bound peptidase-resistant analogues of the insect allatostatins
    • Nachman R.J., Garside C.S., and Tobe S.S. Hemolymph and tissue-bound peptidase-resistant analogues of the insect allatostatins. Peptides 20 (1999) 23-29
    • (1999) Peptides , vol.20 , pp. 23-29
    • Nachman, R.J.1    Garside, C.S.2    Tobe, S.S.3
  • 42
    • 0035136873 scopus 로고    scopus 로고
    • Comparative topical pheromonotropic activity of insect pyrokinin/PBAN amphiphilic analogs incorporating different fatty and/or cholic acid components
    • Nachman R.J., Teal P.E.A., and Ujvary I. Comparative topical pheromonotropic activity of insect pyrokinin/PBAN amphiphilic analogs incorporating different fatty and/or cholic acid components. Peptides 22 (2001) 279-285
    • (2001) Peptides , vol.22 , pp. 279-285
    • Nachman, R.J.1    Teal, P.E.A.2    Ujvary, I.3
  • 43
    • 0036848483 scopus 로고    scopus 로고
    • Enhanced oral availability/pheromonotropic activity of peptidase-resistant topical amphiphilic analogs of pyrokinin/PBAN insect neuropeptides
    • Nachman R.J., Teal P.E.A., and Strey A. Enhanced oral availability/pheromonotropic activity of peptidase-resistant topical amphiphilic analogs of pyrokinin/PBAN insect neuropeptides. Peptides 23 (2002) 2035-2043
    • (2002) Peptides , vol.23 , pp. 2035-2043
    • Nachman, R.J.1    Teal, P.E.A.2    Strey, A.3
  • 44
    • 0036126195 scopus 로고    scopus 로고
    • Enhanced in vivo activity of peptidase-resistant analogs of the insect kinin neuropeptide family
    • Nachman R.J., Strey A., Isaac E., Pryor N., Lopez J.D., Deng J.G., et al. Enhanced in vivo activity of peptidase-resistant analogs of the insect kinin neuropeptide family. Peptides 23 (2002) 735-745
    • (2002) Peptides , vol.23 , pp. 735-745
    • Nachman, R.J.1    Strey, A.2    Isaac, E.3    Pryor, N.4    Lopez, J.D.5    Deng, J.G.6
  • 45
    • 0002478606 scopus 로고    scopus 로고
    • A microdialysis study of allatostatin degradation in Blattella germanica (L.) (Dictyoptera, Blattellidae
    • Peralta E., Vilaplana L., Pascual N., Carreno C., Piulachs M.-D., Andrea D., et al. A microdialysis study of allatostatin degradation in Blattella germanica (L.) (Dictyoptera, Blattellidae. Physiol Entomol 25 (2000) 254-259
    • (2000) Physiol Entomol , vol.25 , pp. 254-259
    • Peralta, E.1    Vilaplana, L.2    Pascual, N.3    Carreno, C.4    Piulachs, M.-D.5    Andrea, D.6
  • 46
    • 0014295331 scopus 로고
    • Molecular sieving of hydrophilic molecules by the rectal intima of the desert locust (Schistocerca gregaria)
    • Phillips J.E., and Dockrill A.A. Molecular sieving of hydrophilic molecules by the rectal intima of the desert locust (Schistocerca gregaria). J Exp Biol 48 (1968) 521-532
    • (1968) J Exp Biol , vol.48 , pp. 521-532
    • Phillips, J.E.1    Dockrill, A.A.2
  • 47
    • 0032127598 scopus 로고    scopus 로고
    • Immunohistochemical and developmental studies to elucidate the mechanism of action of the snowdrop lectin on the rice brown planthopper, Nilaparvata lugens (Stal)
    • Powell K.S., Spence J., Bharathi M., Gatehouse J.A., and Gatehouse A.M.R. Immunohistochemical and developmental studies to elucidate the mechanism of action of the snowdrop lectin on the rice brown planthopper, Nilaparvata lugens (Stal). J Insect Physiol 44 (1998) 529-539
    • (1998) J Insect Physiol , vol.44 , pp. 529-539
    • Powell, K.S.1    Spence, J.2    Bharathi, M.3    Gatehouse, J.A.4    Gatehouse, A.M.R.5
  • 48
    • 84990437067 scopus 로고
    • Degradation of the neuropeptide proctolin by membrane bound proteases of the hindgut and ovary of Locusta migratoria and the effects of different inhibitors
    • Puiroux J., and Loughton B.G. Degradation of the neuropeptide proctolin by membrane bound proteases of the hindgut and ovary of Locusta migratoria and the effects of different inhibitors. Arch Insect Biochem Physiol 19 (1992) 193-202
    • (1992) Arch Insect Biochem Physiol , vol.19 , pp. 193-202
    • Puiroux, J.1    Loughton, B.G.2
  • 49
    • 0028087210 scopus 로고
    • Pheromonotropic activity of orally administered PBAN and its analogues in Helicoverpa zea
    • Raina A.K., Rafeali A., and Kingan T.G. Pheromonotropic activity of orally administered PBAN and its analogues in Helicoverpa zea. J Insect Physiol 40 (1994) 393-397
    • (1994) J Insect Physiol , vol.40 , pp. 393-397
    • Raina, A.K.1    Rafeali, A.2    Kingan, T.G.3
  • 50
    • 0001665580 scopus 로고
    • In vitro inactivation of the insect neuropeptide proctolin Periplaneta americana
    • Steele R.W., and Starratt A.N. In vitro inactivation of the insect neuropeptide proctolin Periplaneta americana. Insect Biochem 5 (1985) 511-519
    • (1985) Insect Biochem , vol.5 , pp. 511-519
    • Steele, R.W.1    Starratt, A.N.2
  • 51
    • 0033392275 scopus 로고    scopus 로고
    • Development of amphiphylic mimics of insect neuropeptides for pest control
    • Teal P.E.A., Meredith J.A., and Nachman R.J. Development of amphiphylic mimics of insect neuropeptides for pest control. Ann NY Acad Sci 897 (1999) 348-360
    • (1999) Ann NY Acad Sci , vol.897 , pp. 348-360
    • Teal, P.E.A.1    Meredith, J.A.2    Nachman, R.J.3
  • 52
    • 0027037395 scopus 로고
    • Physiological mechanisms underlying the control of meal size in Manduca sexta larvae
    • Timmins W.A., and Reynolds S.E. Physiological mechanisms underlying the control of meal size in Manduca sexta larvae. Physiol Entomol 17 (1992) 81-89
    • (1992) Physiol Entomol , vol.17 , pp. 81-89
    • Timmins, W.A.1    Reynolds, S.E.2
  • 53
    • 0002427362 scopus 로고    scopus 로고
    • Structures, functions and occurrence of insect allatostatic peptides
    • Coast G.M., and Webster S.G. (Eds), Cambridge University Press, Cambridge
    • Weaver R.J., Edwards J.P., Bendena W.G., and Tobe S.S. Structures, functions and occurrence of insect allatostatic peptides. In: Coast G.M., and Webster S.G. (Eds). Recent Advances in Arthropod Endocrinology (1998), Cambridge University Press, Cambridge 3-32
    • (1998) Recent Advances in Arthropod Endocrinology , pp. 3-32
    • Weaver, R.J.1    Edwards, J.P.2    Bendena, W.G.3    Tobe, S.S.4
  • 54
    • 0028817816 scopus 로고
    • Degradation of pheromone biosynthesis-activating peptide (PBAN) by hemolymph enzymes of the tobacco hormone, Manduca sexta, and the corn earworm, Helicoverpa zea
    • Weirich G.F., Kochansky J.P., Masler E.P., Lusby W.R., Feldlaufer M.F., Raina A.K., et al. Degradation of pheromone biosynthesis-activating peptide (PBAN) by hemolymph enzymes of the tobacco hormone, Manduca sexta, and the corn earworm, Helicoverpa zea. Experientia 51 (1995) 961-966
    • (1995) Experientia , vol.51 , pp. 961-966
    • Weirich, G.F.1    Kochansky, J.P.2    Masler, E.P.3    Lusby, W.R.4    Feldlaufer, M.F.5    Raina, A.K.6
  • 55
    • 0000516346 scopus 로고
    • Mass rearing of the tobacco hornworm. II. Larval rearing and pupation
    • Yamamoto R. Mass rearing of the tobacco hornworm. II. Larval rearing and pupation. J Econ Entomol 62 (1969) 1427-1431
    • (1969) J Econ Entomol , vol.62 , pp. 1427-1431
    • Yamamoto, R.1
  • 56
    • 0028811185 scopus 로고
    • + in asymmetric paracellular transport of 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu-Gly-L-Pro-D-Arg across rabbit colonic segments and Caco-2 cell monolayers
    • + in asymmetric paracellular transport of 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu-Gly-L-Pro-D-Arg across rabbit colonic segments and Caco-2 cell monolayers. J Pharm Exp Therap 275 (1995) 114-119
    • (1995) J Pharm Exp Therap , vol.275 , pp. 114-119
    • Yen, W.-C.1    Lee, V.H.2
  • 57
    • 0001720015 scopus 로고
    • Allatostatin content of brain, corpora allata and hemolymph at different developmental stages of the cockroach, Diploptera punctata: quantitation by ELISA and bioassay
    • Yu C.G., Stay B., Joshi S., and Tobe S.S. Allatostatin content of brain, corpora allata and hemolymph at different developmental stages of the cockroach, Diploptera punctata: quantitation by ELISA and bioassay. J Insect Physiol 39 (1993) 111-122
    • (1993) J Insect Physiol , vol.39 , pp. 111-122
    • Yu, C.G.1    Stay, B.2    Joshi, S.3    Tobe, S.S.4
  • 58
    • 0035186967 scopus 로고    scopus 로고
    • In vitro degradation of the Neb-trypsin modulating oostatic Factor (Neb-TMOF) in gut luminal content and hemolymph of the grey fleshfly, Neobellieria bullata
    • Zhu W., Vandingenen A., Huybrechts R., Baggerman G., De Loof A., Poulos C.P., et al. In vitro degradation of the Neb-trypsin modulating oostatic Factor (Neb-TMOF) in gut luminal content and hemolymph of the grey fleshfly, Neobellieria bullata. Insect Biochem Mol Biol 31 (2001) 87-95
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 87-95
    • Zhu, W.1    Vandingenen, A.2    Huybrechts, R.3    Baggerman, G.4    De Loof, A.5    Poulos, C.P.6
  • 59
    • 0034761848 scopus 로고    scopus 로고
    • Proteolytic breakdown of the Neb-trypsin modulating oostatic factor (Neb-TMOF) in the hemolymph of different insects and its gut epithelial transport
    • Zhu W., Vandingenen A., Huybrechts R., Vercammen T., Baggerman G., De Loof A., et al. Proteolytic breakdown of the Neb-trypsin modulating oostatic factor (Neb-TMOF) in the hemolymph of different insects and its gut epithelial transport. J Insect Physiol 47 (2001) 1235-1242
    • (2001) J Insect Physiol , vol.47 , pp. 1235-1242
    • Zhu, W.1    Vandingenen, A.2    Huybrechts, R.3    Vercammen, T.4    Baggerman, G.5    De Loof, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.