메뉴 건너뛰기




Volumn 123, Issue 2, 1996, Pages 113-117

At the cutting edge. Where does amidation take place?

Author keywords

Amidation; Endocrine regulation; Peptide hormones

Indexed keywords

PEPTIDE HORMONE; HORMONE;

EID: 0030607297     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(96)03903-2     Document Type: Article
Times cited : (24)

References (33)
  • 1
    • 0026436896 scopus 로고
    • Control of tumor cell biology through regulation of peptide hormone processing
    • [1] Treston, A.M., Mulshine, J.L. and Cuttitta, F. (1992) Control of tumor cell biology through regulation of peptide hormone processing. J. Natl. Cancer Inst. Monogr. 13, 169-175.
    • (1992) J. Natl. Cancer Inst. Monogr. , vol.13 , pp. 169-175
    • Treston, A.M.1    Mulshine, J.L.2    Cuttitta, F.3
  • 2
    • 0026514908 scopus 로고
    • The biosynthesis of neuropeptides; peptide α-amidation
    • [2] Eipper, B.A., Stoffers, D.S. and Mains, R.E. (1992) The biosynthesis of neuropeptides; peptide α-amidation. Annu. Rev. Neurosci. 15, 57-85
    • (1992) Annu. Rev. Neurosci. , vol.15 , pp. 57-85
    • Eipper, B.A.1    Stoffers, D.S.2    Mains, R.E.3
  • 3
    • 0025968504 scopus 로고
    • Characterization of novel mRNAs encoding enzymes involved in peptide alpha-amidation
    • [3] Stoffers, D.A., Ouafik, L. and Eipper, B.A. (1991) Characterization of novel mRNAs encoding enzymes involved in peptide alpha-amidation. J. Biol. Chem. 266, 1701-1710.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1701-1710
    • Stoffers, D.A.1    Ouafik, L.2    Eipper, B.A.3
  • 4
    • 0028972364 scopus 로고
    • Human peptidylglycine α-amidating monooxygenase transcripts derived by alternative mRNA splicing of an unreported exon
    • [4] Vos, M.D., Jones, J.E. and Treston, A.M. (1995) Human peptidylglycine α-amidating monooxygenase transcripts derived by alternative mRNA splicing of an unreported exon. Gene 163, 307-311.
    • (1995) Gene , vol.163 , pp. 307-311
    • Vos, M.D.1    Jones, J.E.2    Treston, A.M.3
  • 5
    • 0028175481 scopus 로고
    • C-terminal amidated peptides: Production by the in vitro enzymatic amidation of glycine-extended peptides and the importance of the amide to bioactivity
    • [5] Merkler, D.J. (1994) C-terminal amidated peptides: production by the in vitro enzymatic amidation of glycine-extended peptides and the importance of the amide to bioactivity. Enzyme Microbiol. Technol. 16, 450-456.
    • (1994) Enzyme Microbiol. Technol. , vol.16 , pp. 450-456
    • Merkler, D.J.1
  • 7
    • 0030008554 scopus 로고    scopus 로고
    • Fatty acid amide biosynthesis: A possible new role for peptidylglycine α-amidating enzyme and acyl-CoA:Glycine N-acyltransferase
    • [7] Merkler, D.J., Merkler, K.A., Stern, W. and Fleming, F.F. (1996) Fatty acid amide biosynthesis: a possible new role for peptidylglycine α-amidating enzyme and acyl-CoA:glycine N-acyltransferase. Arch. Biochem. Biophys. 330, 430-434.
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 430-434
    • Merkler, D.J.1    Merkler, K.A.2    Stern, W.3    Fleming, F.F.4
  • 9
    • 0011826765 scopus 로고
    • Novel tumor cell growth inhibitors acting via autocrine loops which are dependent on peptidyl α-amidating enzyme
    • [9] Iwai, N., Avis, I., Scott, F., Quinn, K., Cuttitta, F., Mulshine, J.L. and Treston, A. (1993) Novel tumor cell growth inhibitors acting via autocrine loops which are dependent on peptidyl α-amidating enzyme. Proc. Am. Assoc. Cancer Res. 34, 266.
    • (1993) Proc. Am. Assoc. Cancer Res. , vol.34 , pp. 266
    • Iwai, N.1    Avis, I.2    Scott, F.3    Quinn, K.4    Cuttitta, F.5    Mulshine, J.L.6    Treston, A.7
  • 10
    • 9444246542 scopus 로고
    • Antisense expression of peptide amidating enzyme RNA reduces growth in tumor cells
    • The Endocrine Society, Abstract P1
    • [10] Martínez, A., Vos, M. and Treston, A. (1995) Antisense expression of peptide amidating enzyme RNA reduces growth in tumor cells. Proc. 77th Annual Meeting, The Endocrine Society, Abstract P1 660.
    • (1995) Proc. 77th Annual Meeting , pp. 660
    • Martínez, A.1    Vos, M.2    Treston, A.3
  • 11
    • 0021858739 scopus 로고
    • Further characterization of the peptidyl alpha-amidating enzyme in rat anterior pituitary secretory granules
    • [11] Glembotski, C.C. (1985) Further characterization of the peptidyl alpha-amidating enzyme in rat anterior pituitary secretory granules. Arch. Biochem. Biophys. 241, 673-675.
    • (1985) Arch. Biochem. Biophys. , vol.241 , pp. 673-675
    • Glembotski, C.C.1
  • 12
    • 0027523133 scopus 로고
    • Immunocytochemical localization of peptidylglycine alpha-amidating monooxygenase enzymes (PAM) in human endocrine pancreas
    • [12] Martínez, A., Montuenga, L.M., Springall, D.R., Treston, A., Cuttitta, F. and Polak, J.M. (1993) Immunocytochemical localization of peptidylglycine alpha-amidating monooxygenase enzymes (PAM) in human endocrine pancreas. J. Histochem. Cytochem. 41, 375-380.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 375-380
    • Martínez, A.1    Montuenga, L.M.2    Springall, D.R.3    Treston, A.4    Cuttitta, F.5    Polak, J.M.6
  • 14
  • 15
    • 0030038259 scopus 로고    scopus 로고
    • Expression of peptidyl-glycine α-amidating monooxygenase (PAM) enzymes in morphological abnormalities adjacent to pulmonary tumors
    • [15] Martínez, A., Treston, A., Saldise, L., Montuenga, L.M. and Linnoila, R.I. (1996) Expression of peptidyl-glycine α-amidating monooxygenase (PAM) enzymes in morphological abnormalities adjacent to pulmonary tumors. Am. J. Pathol. 149, 707-716.
    • (1996) Am. J. Pathol. , vol.149 , pp. 707-716
    • Martínez, A.1    Treston, A.2    Saldise, L.3    Montuenga, L.M.4    Linnoila, R.I.5
  • 16
    • 0011827674 scopus 로고
    • Biology of preneoplastic lesions
    • (Roth, J.A., Cox, J.D. and Hong, W.K., ed.), Blackwell Scientific, Boston
    • [16] Lee, J.S. and Hong, W.K. (1993) Biology of preneoplastic lesions. In: Lung Cancer (Roth, J.A., Cox, J.D. and Hong, W.K., ed.), pp. 34-56. Blackwell Scientific, Boston.
    • (1993) Lung Cancer , pp. 34-56
    • Lee, J.S.1    Hong, W.K.2
  • 18
    • 0028179173 scopus 로고
    • Distribution of immunoreactivity for peptidylglycine alpha-amidating monooxygenase in the human pituitary and in 40 pituitary tumours
    • [18] Steel, J.H., Martínez, A., Springall, D.R., Treston, A., Cuttitta, F. and Polak, J.M. (1994) Distribution of immunoreactivity for peptidylglycine alpha-amidating monooxygenase in the human pituitary and in 40 pituitary tumours. Cell Tissue Res. 276, 197-207.
    • (1994) Cell Tissue Res. , vol.276 , pp. 197-207
    • Steel, J.H.1    Martínez, A.2    Springall, D.R.3    Treston, A.4    Cuttitta, F.5    Polak, J.M.6
  • 20
    • 0026591319 scopus 로고
    • Expression of peptidylglycine α-amidating monooxygenase (EC 1.14,17.3) in the rat central nervous system
    • [20] Schafer, M.K., Stoffers, D.A., Eipper, B.A. and Watson, S.J. (1992) Expression of peptidylglycine α-amidating monooxygenase (EC 1.14,17.3) in the rat central nervous system. J. Neurosci. 12, 222-234.
    • (1992) J. Neurosci. , vol.12 , pp. 222-234
    • Schafer, M.K.1    Stoffers, D.A.2    Eipper, B.A.3    Watson, S.J.4
  • 22
    • 0027690439 scopus 로고
    • Biochemical characterization of peptide α-amidation enzyme activities of human neuroendocrine lung cancer cell lines
    • [22] Treston, A.M., Scott, F.M., Vos, M., Iwai, N., Mains, R.E., Eipper, B.A., Cuttitta, F. and Mulshine, J.L. (1993) Biochemical characterization of peptide α-amidation enzyme activities of human neuroendocrine lung cancer cell lines. Cell Growth Differ. 4, 911-920.
    • (1993) Cell Growth Differ. , vol.4 , pp. 911-920
    • Treston, A.M.1    Scott, F.M.2    Vos, M.3    Iwai, N.4    Mains, R.E.5    Eipper, B.A.6    Cuttitta, F.7    Mulshine, J.L.8
  • 23
    • 0025874817 scopus 로고
    • Neuroepithelial bodies stimulate proliferation of airway epithelium in fetal hamster lung
    • [23] Hoyt, R.F., McNelly, N.A., McDowell, E.M. and Sorokin, S.P. (1991) Neuroepithelial bodies stimulate proliferation of airway epithelium in fetal hamster lung. Am. J. Physiol. 260, L234-L240.
    • (1991) Am. J. Physiol. , vol.260
    • Hoyt, R.F.1    McNelly, N.A.2    McDowell, E.M.3    Sorokin, S.P.4
  • 24
    • 0027195465 scopus 로고
    • Neuroendocrine cells and nerves of the lung
    • [24] Adriaensen, D. and Scheuermann, D.W. (1993) Neuroendocrine cells and nerves of the lung. Anat. Rec. 236, 70-85.
    • (1993) Anat. Rec. , vol.236 , pp. 70-85
    • Adriaensen, D.1    Scheuermann, D.W.2
  • 25
    • 0025483582 scopus 로고
    • Bombesin increases fetal lung growth and maturation in utero and in organ culture
    • [25] Sunday, M.E., Hua, J., Dai, H.B., Nusrat, A. and Torday, J.S. (1990) Bombesin increases fetal lung growth and maturation in utero and in organ culture. Am. J. Respir. Cell Mol. Biol. 3, 199-205.
    • (1990) Am. J. Respir. Cell Mol. Biol. , vol.3 , pp. 199-205
    • Sunday, M.E.1    Hua, J.2    Dai, H.B.3    Nusrat, A.4    Torday, J.S.5
  • 26
    • 13344253289 scopus 로고
    • Calcitonin gene-related peptide and amidating enzyme in developing and adult mouse lung
    • Córdoba, Spain. Abstract no 251
    • [26] Guembe, L., Saldise, L. and Villaro, A.C. (1994) Calcitonin gene-related peptide and amidating enzyme in developing and adult mouse lung. 17th Conference of Comparative Endocrinologists. Córdoba, Spain. Abstract no 251.
    • (1994) 17th Conference of Comparative Endocrinologists
    • Guembe, L.1    Saldise, L.2    Villaro, A.C.3
  • 27
    • 0028050404 scopus 로고
    • Growth-promoting effects of glycine-extended progastrin
    • [27] Seva, C., Dickinson, C.J. and Yamada, T. (1994) Growth-promoting effects of glycine-extended progastrin. Science 265, 410-412.
    • (1994) Science , vol.265 , pp. 410-412
    • Seva, C.1    Dickinson, C.J.2    Yamada, T.3
  • 29
    • 0020079479 scopus 로고
    • Mechanism of C-terminal amide formation by pituitary enzymes
    • [29] Bradbury, A.F., Finnie, M.D.A. and Smyth, D.G. (1982) Mechanism of C-terminal amide formation by pituitary enzymes. Nature 298, 686-688.
    • (1982) Nature , vol.298 , pp. 686-688
    • Bradbury, A.F.1    Finnie, M.D.A.2    Smyth, D.G.3
  • 30
    • 0027979265 scopus 로고
    • Glycine-extended post-translational processing intermediates of gastrin and cholecystokinin in the gut
    • [30] Marino, L., Muglia, B. and Dickinson, C.J. (1994) Glycine-extended post-translational processing intermediates of gastrin and cholecystokinin in the gut. Regul. Pept. 50, 73-85.
    • (1994) Regul. Pept. , vol.50 , pp. 73-85
    • Marino, L.1    Muglia, B.2    Dickinson, C.J.3
  • 31
    • 0024359370 scopus 로고
    • Complete sequence of glucagon-like peptide-1 from human and pig small intestine
    • [31] Orskov, C., Bersani, M., Johnsen, A.H., Hojrup, P. and Holst, J.J. (1989) Complete sequence of glucagon-like peptide-1 from human and pig small intestine. J. Biol. Chem. 264, 12826-12829.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12826-12829
    • Orskov, C.1    Bersani, M.2    Johnsen, A.H.3    Hojrup, P.4    Holst, J.J.5
  • 32
    • 0009516914 scopus 로고
    • Cloning, characterization and DNA sequence of a human cDNA encoding neuropeptide tyrosine
    • [32] Minth, C.D.E., Bloom, S.R., Polak, J.M. and Dixon, J.E. (1984) Cloning, characterization and DNA sequence of a human cDNA encoding neuropeptide tyrosine. Proc. Natl. Acad. Sci. USA 81, 4577-4581.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4577-4581
    • Minth, C.D.E.1    Bloom, S.R.2    Polak, J.M.3    Dixon, J.E.4
  • 33
    • 0000613769 scopus 로고
    • Isolation and characterization of peptide YY (PYY), a candidate gut hormone that inhibits pancreatic exocrine secretion
    • [33] Tatemoto, K. (1982) Isolation and characterization of peptide YY (PYY), a candidate gut hormone that inhibits pancreatic exocrine secretion. Proc. Natl. Acad. Sci. USA 79, 2514-2518.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2514-2518
    • Tatemoto, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.