메뉴 건너뛰기




Volumn 55, Issue 1, 2009, Pages 10-18

The intestinal barrier in lepidopteran larvae: Permeability of the peritrophic membrane and of the midgut epithelium to two biologically active peptides

Author keywords

Apparent permeability coefficients; Bombyx mori larvae; Intestinal barriers; Paracellular and transcellular pathways; Peptides

Indexed keywords

FLUORESCEIN ISOTHIOCYANATE; NEUROPEPTIDE; OLIGOPEPTIDE; PEPTIDE OOSTATIC HORMONE; PROCTOLIN;

EID: 57749091512     PISSN: 00221910     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinsphys.2008.09.005     Document Type: Article
Times cited : (19)

References (51)
  • 1
    • 33847393521 scopus 로고
    • Permeability of the peritrophic membrane of the Douglas fir tussock moth (Orygia pseudotsugata)
    • Adang M.J., and Spence K.A. Permeability of the peritrophic membrane of the Douglas fir tussock moth (Orygia pseudotsugata). Comparative Biochemistry and Physiology 75 (1983) 233-238
    • (1983) Comparative Biochemistry and Physiology , vol.75 , pp. 233-238
    • Adang, M.J.1    Spence, K.A.2
  • 2
    • 39149084662 scopus 로고    scopus 로고
    • Transepithelial flux of an allatostatin and analogs across the anterior midgut of Manduca sexta larvae invitro
    • Audsley N., Matthews J., Nachman R.J., and Weaver R.J. Transepithelial flux of an allatostatin and analogs across the anterior midgut of Manduca sexta larvae invitro. Peptides 29 (2008) 286-294
    • (2008) Peptides , vol.29 , pp. 286-294
    • Audsley, N.1    Matthews, J.2    Nachman, R.J.3    Weaver, R.J.4
  • 3
    • 0035379718 scopus 로고    scopus 로고
    • Roles of peritrophic membranes in protecting herbivorous insects from ingested plant allelochemicals
    • Barbehenn R.V. Roles of peritrophic membranes in protecting herbivorous insects from ingested plant allelochemicals. Archives of Insect Biochemistry and Physiology 47 (2001) 86-99
    • (2001) Archives of Insect Biochemistry and Physiology , vol.47 , pp. 86-99
    • Barbehenn, R.V.1
  • 4
    • 0002896738 scopus 로고
    • Peritrophic envelope permeability in herbivorous insects
    • Barbehenn R.V., and Martin M.M. Peritrophic envelope permeability in herbivorous insects. Journal of Insect Physiology 41 (1995) 303-311
    • (1995) Journal of Insect Physiology , vol.41 , pp. 303-311
    • Barbehenn, R.V.1    Martin, M.M.2
  • 7
    • 0242406849 scopus 로고    scopus 로고
    • Trypsin-modulating oostatic factor: a potential new larvicide for mosquito control
    • Borovsky D. Trypsin-modulating oostatic factor: a potential new larvicide for mosquito control. Journal of Experimental Biology 206 (2003) 3869-3875
    • (2003) Journal of Experimental Biology , vol.206 , pp. 3869-3875
    • Borovsky, D.1
  • 8
    • 0029012218 scopus 로고
    • Feeding the mosquito Aedes aegypti with TMOF and its analogs, effect on trypsin biosynthesis and egg development
    • Borovsky D., and Mahmood F. Feeding the mosquito Aedes aegypti with TMOF and its analogs, effect on trypsin biosynthesis and egg development. Regulatory Peptides 57 (1995) 273-281
    • (1995) Regulatory Peptides , vol.57 , pp. 273-281
    • Borovsky, D.1    Mahmood, F.2
  • 9
    • 1642618270 scopus 로고    scopus 로고
    • Biochemical and cytoimmunolgical evidence for the control of Aedes aegypti larval trypsin with Aea-TMOF
    • Borovsky D., and Meola S. Biochemical and cytoimmunolgical evidence for the control of Aedes aegypti larval trypsin with Aea-TMOF. Insect Biochemistry and Physiology 55 (2004) 124-139
    • (2004) Insect Biochemistry and Physiology , vol.55 , pp. 124-139
    • Borovsky, D.1    Meola, S.2
  • 10
    • 57749091232 scopus 로고    scopus 로고
    • Biological and biochemical effects of organo-synthetic analogues of Trypsin Modulating Oostatic Factor (TMOF) on Aedes aegypti, Heliothis virescens and Plutella xylostella
    • Borovsky D., and Nauen R. Biological and biochemical effects of organo-synthetic analogues of Trypsin Modulating Oostatic Factor (TMOF) on Aedes aegypti, Heliothis virescens and Plutella xylostella. Pestycydy 3/4 (2007) 17-26
    • (2007) Pestycydy , vol.3-4 , pp. 17-26
    • Borovsky, D.1    Nauen, R.2
  • 11
    • 0025242490 scopus 로고
    • Mosquito oostatic factor a novel decapeptide modulating trypsin-like enzyme biosynthesis in the midgut
    • Borovsky D., Carlson D.A., Griffin P.R., Shabanowitz J., and Hunt D.F. Mosquito oostatic factor a novel decapeptide modulating trypsin-like enzyme biosynthesis in the midgut. FASEB Journal 4 (1990) 3015-3020
    • (1990) FASEB Journal , vol.4 , pp. 3015-3020
    • Borovsky, D.1    Carlson, D.A.2    Griffin, P.R.3    Shabanowitz, J.4    Hunt, D.F.5
  • 12
    • 0028278775 scopus 로고
    • Characterization and localization of mosquito-gut receptors for trypsin modulating oostatic factor using a complementary peptide and immunocytochemistry
    • Borovsky D., Powell C.A., Nayar J.K., Blalock J.E., and Hayes T.K. Characterization and localization of mosquito-gut receptors for trypsin modulating oostatic factor using a complementary peptide and immunocytochemistry. FASEB Journal 8 (1994) 350-355
    • (1994) FASEB Journal , vol.8 , pp. 350-355
    • Borovsky, D.1    Powell, C.A.2    Nayar, J.K.3    Blalock, J.E.4    Hayes, T.K.5
  • 14
    • 0032191511 scopus 로고    scopus 로고
    • Midgut carboxypeptidase from Helicoverpa armigera (Lepidoptera: Noctuidae) larvae: enzyme characterisation, cDNA cloning and expression
    • Bown D.P., Wilkinson H.S., and Gatehouse J.A. Midgut carboxypeptidase from Helicoverpa armigera (Lepidoptera: Noctuidae) larvae: enzyme characterisation, cDNA cloning and expression. Insect Biochemistry and Molecular Biology 28 (1998) 739-749
    • (1998) Insect Biochemistry and Molecular Biology , vol.28 , pp. 739-749
    • Bown, D.P.1    Wilkinson, H.S.2    Gatehouse, J.A.3
  • 17
  • 18
    • 0037718539 scopus 로고    scopus 로고
    • Size exclusion and diffusion of fluoresceinated probes within collagen fibrils
    • 021909/
    • Ekani-Nkodo A., and Kuchnir Fygenson D. Size exclusion and diffusion of fluoresceinated probes within collagen fibrils. Physical Review E 67 (2003) 1-7 021909/
    • (2003) Physical Review E , vol.67 , pp. 1-7
    • Ekani-Nkodo, A.1    Kuchnir Fygenson, D.2
  • 19
    • 0028197023 scopus 로고
    • Properties of the digestive enzymes and the permeability of the peritrophic membrane of Spodoptera frugiperda (Lepidoptera) larvae
    • Ferreira C., Capella A.N., Sitnik R., and Terra W.R. Properties of the digestive enzymes and the permeability of the peritrophic membrane of Spodoptera frugiperda (Lepidoptera) larvae. Comparative Biochemistry and Physiology 107A (1994) 630-631
    • (1994) Comparative Biochemistry and Physiology , vol.107 A , pp. 630-631
    • Ferreira, C.1    Capella, A.N.2    Sitnik, R.3    Terra, W.R.4
  • 20
    • 33745629348 scopus 로고    scopus 로고
    • The paracellular pathway in the lepidopteran larval midgut and its modulation by intracellular mediators
    • Fiandra L., Casartelli M., and Giordana B. The paracellular pathway in the lepidopteran larval midgut and its modulation by intracellular mediators. Comparative Biochemistry and Physiology 144A (2006) 464-473
    • (2006) Comparative Biochemistry and Physiology , vol.144 A , pp. 464-473
    • Fiandra, L.1    Casartelli, M.2    Giordana, B.3
  • 22
    • 0017706186 scopus 로고
    • Extracellular space values and intracellular ionic concentrations in the isolated midgut of Philosamia cynthia and Bombyx mori
    • Giordana B., and Sacchi V.F. Extracellular space values and intracellular ionic concentrations in the isolated midgut of Philosamia cynthia and Bombyx mori. Experientia 33 (1977) 1065-1066
    • (1977) Experientia , vol.33 , pp. 1065-1066
    • Giordana, B.1    Sacchi, V.F.2
  • 23
    • 32544442655 scopus 로고    scopus 로고
    • Critical role of tight junctions in drug delivery across epithelial and endothelial cell layers
    • Gonzalez-Mariscal L., Nava P., and Hernandez S. Critical role of tight junctions in drug delivery across epithelial and endothelial cell layers. The Journal of Membrane Biology 207 (2005) 55-68
    • (2005) The Journal of Membrane Biology , vol.207 , pp. 55-68
    • Gonzalez-Mariscal, L.1    Nava, P.2    Hernandez, S.3
  • 25
    • 0036149377 scopus 로고    scopus 로고
    • Fluorescein uptake by a monocarboxylic acid transporter in human intestinal Caco-2 cells
    • Kuwayama K., Miyauchi S., Tateoka R., Abe H., and Kamo N. Fluorescein uptake by a monocarboxylic acid transporter in human intestinal Caco-2 cells. Biochemical Pharmacology 63 (2002) 81-88
    • (2002) Biochemical Pharmacology , vol.63 , pp. 81-88
    • Kuwayama, K.1    Miyauchi, S.2    Tateoka, R.3    Abe, H.4    Kamo, N.5
  • 26
    • 0030891189 scopus 로고    scopus 로고
    • Peritrophic matrix structure and function
    • Lehane M.L. Peritrophic matrix structure and function. Annual Review of Entomology 42 (1997) 525-550
    • (1997) Annual Review of Entomology , vol.42 , pp. 525-550
    • Lehane, M.L.1
  • 27
    • 0003018251 scopus 로고
    • A flash photolysis study of fluoresceins
    • Lindquist L. A flash photolysis study of fluoresceins. Arkiv för kemi 16 (1960) 79-138
    • (1960) Arkiv för kemi , vol.16 , pp. 79-138
    • Lindquist, L.1
  • 28
    • 0035433880 scopus 로고    scopus 로고
    • TMOF like factor controls the biosynthesis of serine proteases in the larval gut of Heliothis virescens
    • Nauen R., Sorge D., Sterner A., and Borovsky D. TMOF like factor controls the biosynthesis of serine proteases in the larval gut of Heliothis virescens. Archives of Insect Biochemistry and Physiology 47 (2001) 169-180
    • (2001) Archives of Insect Biochemistry and Physiology , vol.47 , pp. 169-180
    • Nauen, R.1    Sorge, D.2    Sterner, A.3    Borovsky, D.4
  • 29
    • 0036189323 scopus 로고    scopus 로고
    • Midgut exopeptidase activities in Aedes aegypti are induced by blood feeding
    • Noriega F.G., Edgar K.A., Bechet R., and Wells M.A. Midgut exopeptidase activities in Aedes aegypti are induced by blood feeding. Journal of Insect Physiology 48 (2002) 205-212
    • (2002) Journal of Insect Physiology , vol.48 , pp. 205-212
    • Noriega, F.G.1    Edgar, K.A.2    Bechet, R.3    Wells, M.A.4
  • 30
    • 0030792730 scopus 로고    scopus 로고
    • Estimation of the relative contribution of the transcellular and paracellular pathway to the transport of passively absorbed drugs in the Caco-2 cell culture Model
    • Pade V., and Stavchansky S. Estimation of the relative contribution of the transcellular and paracellular pathway to the transport of passively absorbed drugs in the Caco-2 cell culture Model. Pharmaceutical Research 14 (1997) 1210-1215
    • (1997) Pharmaceutical Research , vol.14 , pp. 1210-1215
    • Pade, V.1    Stavchansky, S.2
  • 31
    • 0023521841 scopus 로고
    • Contribution of solvent drag through intercellular junctions to absorption of nutrients by small intestine of the rat
    • Pappenheimer J.R., and Reiss K.Z. Contribution of solvent drag through intercellular junctions to absorption of nutrients by small intestine of the rat. Journal of Membrane Biology 100 (1987) 123-136
    • (1987) Journal of Membrane Biology , vol.100 , pp. 123-136
    • Pappenheimer, J.R.1    Reiss, K.Z.2
  • 34
    • 0030903756 scopus 로고    scopus 로고
    • Effect of size and charge on the passive diffusion of peptides across Caco-2 cell monolayers via the paracellular pathway
    • Pauletti G.M., Okumu F.W., and Borchardt R.T. Effect of size and charge on the passive diffusion of peptides across Caco-2 cell monolayers via the paracellular pathway. Pharmaceutical Research 14 (1997) 164-168
    • (1997) Pharmaceutical Research , vol.14 , pp. 164-168
    • Pauletti, G.M.1    Okumu, F.W.2    Borchardt, R.T.3
  • 35
    • 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 G.G. Degradation of the neuropeptide proctolin by membrane bound proteases of the hindgut and ovary of Locusta migratoria and the effects of different inhibitors. Archives of Insect Biochemistry and Physiology 19 (1992) 193-202
    • (1992) Archives of Insect Biochemistry and Physiology , vol.19 , pp. 193-202
    • Puiroux, J.1    Loughton, G.G.2
  • 37
    • 0026485122 scopus 로고
    • Peritrophic membrane structure and formation in the larva of a moth, Heliothis
    • Ryerse J.S., Purcell J.P., Sammons R.D., and Lavrik P.B. Peritrophic membrane structure and formation in the larva of a moth, Heliothis. Tissue and Cell 24 (1992) 751-771
    • (1992) Tissue and Cell , vol.24 , pp. 751-771
    • Ryerse, J.S.1    Purcell, J.P.2    Sammons, R.D.3    Lavrik, P.B.4
  • 39
    • 0000170190 scopus 로고
    • Distribution and characterisation of oligomeric digestive enzymes from Erinnys ello larvae and inferences concernine secretory mechanisms and the permeability of the peritrophic membrane
    • Santos C.D., and Terra W. Distribution and characterisation of oligomeric digestive enzymes from Erinnys ello larvae and inferences concernine secretory mechanisms and the permeability of the peritrophic membrane. Insect Biochemistry 16 (1986) 691-700
    • (1986) Insect Biochemistry , vol.16 , pp. 691-700
    • Santos, C.D.1    Terra, W.2
  • 40
    • 0023414365 scopus 로고
    • The permeability properties of septate junction in Malpighian tubules of Rhodnius
    • Skaer H., Le B., Maddrell S.H.P., and Harrison J.B. The permeability properties of septate junction in Malpighian tubules of Rhodnius. Journal of Cell Science 88 (1987) 251-267
    • (1987) Journal of Cell Science , vol.88 , pp. 251-267
    • Skaer, H.1    Le, B.2    Maddrell, S.H.P.3    Harrison, J.B.4
  • 42
    • 0035378362 scopus 로고    scopus 로고
    • The origin and functions of the insect peritrohic membrane and peritrophic gel
    • Terra W.R. The origin and functions of the insect peritrohic membrane and peritrophic gel. Archives of Insect Biochemistry and Physiology 47 (2001) 47-51
    • (2001) Archives of Insect Biochemistry and Physiology , vol.47 , pp. 47-51
    • Terra, W.R.1
  • 43
    • 85069944088 scopus 로고    scopus 로고
    • Biochemistry of digestion
    • Gilbert L.I., Iatrou K., and Gill S.S. (Eds), Pergamon Press, Oxford
    • Terra W.R., and Ferreira C. Biochemistry of digestion. In: Gilbert L.I., Iatrou K., and Gill S.S. (Eds). Comprehensive Molecular Insect Science vol. 4 (2005), Pergamon Press, Oxford 171-224
    • (2005) Comprehensive Molecular Insect Science , vol.4 , pp. 171-224
    • Terra, W.R.1    Ferreira, C.2
  • 44
    • 3242736673 scopus 로고    scopus 로고
    • An insect peptide engineered into the tomato prosystemin gene is released in transgenic tabacco plants and exerts biological activity
    • Tortiglione C., Fogliano V., Ferracane R., Fanti P., Pennacchio F., Maria Monti L., and Rao R. An insect peptide engineered into the tomato prosystemin gene is released in transgenic tabacco plants and exerts biological activity. Plant Molecular Biology 53 (2002) 891-902
    • (2002) Plant Molecular Biology , vol.53 , pp. 891-902
    • Tortiglione, C.1    Fogliano, V.2    Ferracane, R.3    Fanti, P.4    Pennacchio, F.5    Maria Monti, L.6    Rao, R.7
  • 45
    • 0035377371 scopus 로고    scopus 로고
    • Molecular structure of the peritrophic membrane (PM): identification of potential PM target sites for insect control
    • Wang P., and Granados R. Molecular structure of the peritrophic membrane (PM): identification of potential PM target sites for insect control. Archives of Insect Biochemistry and Physiology 47 (2001) 110-118
    • (2001) Archives of Insect Biochemistry and Physiology , vol.47 , pp. 110-118
    • Wang, P.1    Granados, R.2
  • 46
    • 33847614299 scopus 로고    scopus 로고
    • Delivery methods for peptide and protein toxins in insect control
    • Whetstone P.A., and Hammock B.D. Delivery methods for peptide and protein toxins in insect control. Toxicon 49 (2007) 576-596
    • (2007) Toxicon , vol.49 , pp. 576-596
    • Whetstone, P.A.1    Hammock, B.D.2
  • 48
    • 0013538319 scopus 로고
    • Permeability of the peritrophic membrane of tobacco hornworm larval midgut
    • Wolfersberger M.G., Spaeth D.D., and Dow J.A.T. Permeability of the peritrophic membrane of tobacco hornworm larval midgut. American Zoologist 26 (1986) 74A
    • (1986) American Zoologist , vol.26
    • Wolfersberger, M.G.1    Spaeth, D.D.2    Dow, J.A.T.3
  • 49
    • 0028811185 scopus 로고
    • + in the 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 the asymmetric paracellular transport of 4-phenylazobenzyloxycarbonyl-l-Pro-l-Leu-Gly-l-Pro-d-Arg across rabbit colonic segments and Caco-2 cell monolayers. The Journal of Pharmacology and Experimental Therapeutics 275 (1995) 114-119
    • (1995) The Journal of Pharmacology and Experimental Therapeutics , vol.275 , pp. 114-119
    • Yen, W.C.1    Lee, V.H.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.