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Volumn 15, Issue 9, 1998, Pages 1480-1484

Enzymatic degradation of luteinizing hormone releasing hormone (LHRH)/[D-Ala6]-LHRH in lung pneumocytes

Author keywords

Degradation; Epithelial cells; LHRH; Lung; Macrophages; Peptides

Indexed keywords

GONADORELIN;

EID: 0031723472     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1011926310666     Document Type: Article
Times cited : (16)

References (21)
  • 1
    • 0026572056 scopus 로고
    • Routes of delivery: Case study. Pulmonary delivery of peptides and proteins for systemic action
    • J. S. Patton and R. M. Platz. Routes of delivery: Case study. Pulmonary delivery of peptides and proteins for systemic action. Adv. Drug Deliv. Rev. 8:179-196 (1992).
    • (1992) Adv. Drug Deliv. Rev. , vol.8 , pp. 179-196
    • Patton, J.S.1    Platz, R.M.2
  • 2
    • 0026813472 scopus 로고
    • Allometic relationships of cell numbers and size in the mammalian lung
    • K. C. Stone, R. R. Mercer, P. Gehi, and J. D. Crapo. Allometic relationships of cell numbers and size in the mammalian lung. Am. Respir. Cell Mol. Biol. 6:235-243 (1992).
    • (1992) Am. Respir. Cell Mol. Biol. , vol.6 , pp. 235-243
    • Stone, K.C.1    Mercer, R.R.2    Gehi, P.3    Crapo, J.D.4
  • 3
    • 0019862564 scopus 로고
    • Dose response of the pulmonary macrophagic system to various particles and its relationship to transepithelial passage of free panicles
    • I. Y. Adamson and D. H. Bowden. Dose response of the pulmonary macrophagic system to various particles and its relationship to transepithelial passage of free panicles. Exp. Lung Res. 2:165-175 (1981).
    • (1981) Exp. Lung Res. , vol.2 , pp. 165-175
    • Adamson, I.Y.1    Bowden, D.H.2
  • 4
    • 0015992802 scopus 로고
    • The type II cell as progenitor of alveolar epithelial regeneration: A cytodynamic study in mice after exposure to oxygen
    • I. Y. Adamson and D. H. Bowden. The type II cell as progenitor of alveolar epithelial regeneration: A cytodynamic study in mice after exposure to oxygen. Lab. Invest. 30:35-42 (1974).
    • (1974) Lab. Invest. , vol.30 , pp. 35-42
    • Adamson, I.Y.1    Bowden, D.H.2
  • 5
    • 0027489007 scopus 로고
    • Transport and hydrolysis of enkephalins in cultured alveolar epithellial monolayers
    • L. Y. Wang, D. Toledo, D. B. Schwegler, J. K. H. Ma, and Y. Rojanasakul. Transport and hydrolysis of enkephalins in cultured alveolar epithellial monolayers. Pharm. Res. 10:1662-1667 (1993).
    • (1993) Pharm. Res. , vol.10 , pp. 1662-1667
    • Wang, L.Y.1    Toledo, D.2    Schwegler, D.B.3    Ma, J.K.H.4    Rojanasakul, Y.5
  • 6
    • 0024467703 scopus 로고
    • Type I cell-like morphology in tight alveolar epithelial monolyers
    • J. M. Cheek, M. J. Evans, and E. D. Crandall. Type I cell-like morphology in tight alveolar epithelial monolyers. Exp. Cell Res. 184: 375-387 (1989).
    • (1989) Exp. Cell Res. , vol.184 , pp. 375-387
    • Cheek, J.M.1    Evans, M.J.2    Crandall, E.D.3
  • 7
    • 0026826191 scopus 로고
    • Reactivity of alveolar epithelial cells in primary culture with type I cell monoclonal antibodies
    • S. I. Danto, S. M. Zabski, and E. D. Crandall. Reactivity of alveolar epithelial cells in primary culture with type I cell monoclonal antibodies. Am. J. Respir. Cell Mol. Biol. 6:296-306 (1992).
    • (1992) Am. J. Respir. Cell Mol. Biol. , vol.6 , pp. 296-306
    • Danto, S.I.1    Zabski, S.M.2    Crandall, E.D.3
  • 8
    • 0031008595 scopus 로고    scopus 로고
    • Involvement of an NAD(P)H oxidase-like enzyme in Superoxide anion and hydrogen peroxide generation by rat type II cells
    • R. J. van Klaveren, C. Roelant, M. Boogaerts, M. Demedts, and B. Nemery. Involvement of an NAD(P)H oxidase-like enzyme in Superoxide anion and hydrogen peroxide generation by rat type II cells. Thorax 52:465-471 (1997).
    • (1997) Thorax , vol.52 , pp. 465-471
    • Van Klaveren, R.J.1    Roelant, C.2    Boogaerts, M.3    Demedts, M.4    Nemery, B.5
  • 9
    • 0017577408 scopus 로고
    • Luteinizing-hormone-releasing-hormone
    • S. M. MacCann. Luteinizing-hormone-releasing-hormone. Physiol. Med. 296:797-802 (1977).
    • (1977) Physiol. Med. , vol.296 , pp. 797-802
    • MacCann, S.M.1
  • 10
    • 0020824984 scopus 로고
    • A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides
    • M. Orlowski, C. Michaud, and T. G. Chu. A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides. Eur. J. Biochem. 135:81-88 (1983).
    • (1983) Eur. J. Biochem. , vol.135 , pp. 81-88
    • Orlowski, M.1    Michaud, C.2    Chu, T.G.3
  • 12
    • 0021175531 scopus 로고
    • Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase
    • R. A. Skidgel and E. G. Erdos. Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase. Peptides 5:769-776 (1984).
    • (1984) Peptides , vol.5 , pp. 769-776
    • Skidgel, R.A.1    Erdos, E.G.2
  • 13
    • 0023721848 scopus 로고
    • Endopeptidase 24.15 is the primary enzyme that degrades luteinizing hormone releasing hormone both in vitro and in vivo
    • C. J. Molineaux, A. L. Lasdun, and M. Orlowski. Endopeptidase 24.15 is the primary enzyme that degrades luteinizing hormone releasing hormone both in vitro and in vivo. J. Neurochem. 51:624-633 (1988).
    • (1988) J. Neurochem. , vol.51 , pp. 624-633
    • Molineaux, C.J.1    Lasdun, A.L.2    Orlowski, M.3
  • 14
    • 0342645890 scopus 로고
    • Multiple functions of human converting enzyme and enkephalinase in peptide metabolism
    • E. G. Erdos. Multiple functions of human converting enzyme and enkephalinase in peptide metabolism. Jp. J. Hypertension 6:71-80 (1984).
    • (1984) Jp. J. Hypertension , vol.6 , pp. 71-80
    • Erdos, E.G.1
  • 15
    • 0023696879 scopus 로고
    • Alkaline phosphatase: A marker of alveolar type II cell differentiation
    • J. R. Edelson, J. M. Shannon, and R. J. Mason. Alkaline phosphatase: a marker of alveolar type II cell differentiation. Am. Rev. Respir. Ois. 138:1268-1275 (1988).
    • (1988) Am. Rev. Respir. Ois. , vol.138 , pp. 1268-1275
    • Edelson, J.R.1    Shannon, J.M.2    Mason, R.J.3
  • 16
    • 0022460440 scopus 로고
    • Enkephalin hydrolysis in homogenates of various absorptive mucosae of the albino rabbit: Similarities in rates and involvement of aminopeptidases
    • S. D. Kashi and V. H. L. Lee. Enkephalin hydrolysis in homogenates of various absorptive mucosae of the albino rabbit: Similarities in rates and involvement of aminopeptidases. Life Sci. 38:2019-2028 (1986).
    • (1986) Life Sci. , vol.38 , pp. 2019-2028
    • Kashi, S.D.1    Lee, V.H.L.2
  • 17
    • 0025100418 scopus 로고
    • Pulmonary delivery of peptide drugs: Effect of particle size on bioavailability of leuprolide acetate in healthy male volunteers
    • A. Adjei and J. Garren. Pulmonary delivery of peptide drugs: Effect of particle size on bioavailability of leuprolide acetate in healthy male volunteers. Pharm. Res. 7:565-569 (1990).
    • (1990) Pharm. Res. , vol.7 , pp. 565-569
    • Adjei, A.1    Garren, J.2
  • 18
    • 0021857736 scopus 로고
    • Are there neuropeptide-specific peptidases?
    • A. J. Turner, R. Matsas, and A. J. Kenny. Are there neuropeptide-specific peptidases? Biochem. Pharmacol. 34:1347-1356 (1985).
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 1347-1356
    • Turner, A.J.1    Matsas, R.2    Kenny, A.J.3
  • 20
    • 0023224317 scopus 로고
    • Effect of D-amino acid substituents on degradation of LHRH analogues by proximal tubule
    • G. Flouret, T. Majewski, D. R. Peterson, and A. J. Kenny. Effect of D-amino acid substituents on degradation of LHRH analogues by proximal tubule. Am. Physiol. E320-D326 (1987).
    • (1987) Am. Physiol.
    • Flouret, G.1    Majewski, T.2    Peterson, D.R.3    Kenny, A.J.4
  • 21
    • 0026094773 scopus 로고
    • Comparison of in vivo biological activities of luteinizing hormone-releasing hormone (LHRH) analogues in 60-day old cockerels
    • T. Nakamura, T. Nagata, Y. Tanabe, N. Yanaihara, and Y. Hasegawa. Comparison of in vivo biological activities of luteinizing hormone-releasing hormone (LHRH) analogues in 60-day old cockerels. Gen. Comp. Endocrinol. 83:290-296 (1991).
    • (1991) Gen. Comp. Endocrinol. , vol.83 , pp. 290-296
    • Nakamura, T.1    Nagata, T.2    Tanabe, Y.3    Yanaihara, N.4    Hasegawa, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.