메뉴 건너뛰기




Volumn 768, Issue , 2011, Pages 107-125

The Novel Role of Cathepsin L for Neuropeptide Production Illustrated by Research Strategies in Chemical Biology with Protease Gene Knockout and Expression

Author keywords

aminopeptidase; carboxypeptidase; chemical biology; gene expression; gene knockout; immunofluorescence confocal microscopy; mass spectrometry; neuroendocrine; Neuropeptides; prohormone convertase; proteases

Indexed keywords

ALPHA INTERMEDIN; BETA ENDORPHIN; CATHEPSIN L; DYNORPHIN; ENKEPHALIN; NEUROPEPTIDE; PEPTIDE HORMONE; PROENKEPHALIN; PROTEIN PRECURSOR; PROTEINASE; SERINE PROTEINASE;

EID: 80054724536     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-61779-204-5_5     Document Type: Chapter
Times cited : (12)

References (50)
  • 1
    • 0034128416 scopus 로고    scopus 로고
    • Molecular mechanisms and regulation of opioid receptor signaling
    • Law, P. Y., Wong, Y. H., and Loh, H. H. (2000) Molecular mechanisms and regulation of opioid receptor signaling Annu Rev Pharmacol Toxicol 40, 389–430.
    • (2000) Annu Rev Pharmacol Toxicol , vol.40 , pp. 389-430
    • Law, P.Y.1    Wong, Y.H.2    Loh, H.H.3
  • 2
    • 0037384118 scopus 로고    scopus 로고
    • Historical review: Opioid receptors
    • Snyder, S. H., and Pasternak, G. W. (2003) Historical review: Opioid receptors Trends Pharmacol Sci 24, 198–205.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 198-205
    • Snyder, S.H.1    Pasternak, G.W.2
  • 3
    • 0000532413 scopus 로고
    • Diseases of the anterior pituitary
    • Third Edition, P. Felig, J. D. Baxter, and L. A. Frohman, eds. New York, NY: McGraw-Hill. Health Professions Division
    • Frohman, L. A. (1995) Diseases of the anterior pituitary. In: Endocrinology and Metabolism, Third Edition, P. Felig, J. D. Baxter, and L. A. Frohman, eds. New York, NY: McGraw-Hill. Health Professions Division, pp. 293–7.
    • (1995) Endocrinology and Metabolism , pp. 293-297
    • Frohman, L.A.1
  • 5
    • 0032748141 scopus 로고    scopus 로고
    • Role of hypothalamic neuropeptide Y in feeding and obesity
    • Gehlert, D. R. (1999) Role of hypothalamic neuropeptide Y in feeding and obesity Neuropeptides 33, 329–38.
    • (1999) Neuropeptides , vol.33 , pp. 329-338
    • Gehlert, D.R.1
  • 6
    • 0034117088 scopus 로고    scopus 로고
    • The role of NPY in metabolic homeostasis: Implications for obesity therapy
    • Wieland, H. A., Hamilton, B. S., Krist, B., and Doods, H. N. (2000) The role of NPY in metabolic homeostasis: Implications for obesity therapy Expert Opin Investig Drugs 9, 1327–46.
    • (2000) Expert Opin Investig Drugs , vol.9 , pp. 1327-1346
    • Wieland, H.A.1    Hamilton, B.S.2    Krist, B.3    Doods, H.N.4
  • 7
    • 41149103075 scopus 로고    scopus 로고
    • Proteases for processing proneuropeptides into peptide neurotransmitters and hormones
    • Hook, V., Funkelstein, L., Lu, D., Bark, S., Wegrzyn, J., and Hwang, S. R. (2008) Proteases for processing proneuropeptides into peptide neurotransmitters and hormones Annu Rev Pharmacol Toxicol 48, 393–423.
    • (2008) Annu Rev Pharmacol Toxicol , vol.48 , pp. 393-423
    • Hook, V.1    Funkelstein, L.2    Lu, D.3    Bark, S.4    Wegrzyn, J.5    Hwang, S.R.6
  • 8
    • 0031995477 scopus 로고    scopus 로고
    • The proprotein convertases
    • Steiner, D. F. (1998) The proprotein convertases Curr Opin Chem Biol 2, 31–9.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 31-39
    • Steiner, D.F.1
  • 9
    • 0038394566 scopus 로고    scopus 로고
    • Precursor convertases in the secretory pathway, cytosol and extracellular milieu
    • Seidah, N. G., and Prat, A. (2002) Precursor convertases in the secretory pathway, cytosol and extracellular milieu Essays Biochem 38, 79–94.
    • (2002) Essays Biochem , vol.38 , pp. 79-94
    • Seidah, N.G.1    Prat, A.2
  • 11
    • 34248177365 scopus 로고    scopus 로고
    • Cathepsin L expression is directed to secretory vesicles for enkephalin neuropeptide biosynthesis and secretion
    • Hwang, S. R., Garza, C., Mosier, C., Toneff, T., Wunderlich, E., Goldsmith, P., and Hook, V. (2007) Cathepsin L expression is directed to secretory vesicles for enkephalin neuropeptide biosynthesis and secretion J Biol Chem 282, 9556–63.
    • (2007) J Biol Chem , vol.282 , pp. 9556-9563
    • Hwang, S.R.1    Garza, C.2    Mosier, C.3    Toneff, T.4    Wunderlich, E.5    Goldsmith, P.6    Hook, V.7
  • 12
    • 45249083897 scopus 로고    scopus 로고
    • Cathepsin L participates in the production of neuropeptide Y in secretory vesicles, demonstrated by protease gene knockout and expression
    • Funkelstein, L., Toneff, T., Hwang, S. R., Reinheckel, T., Peters, C., and Hook, V. (2008) Cathepsin L participates in the production of neuropeptide Y in secretory vesicles, demonstrated by protease gene knockout and expression J Neurochem 106, 384–91.
    • (2008) J Neurochem , vol.106 , pp. 384-391
    • Funkelstein, L.1    Toneff, T.2    Hwang, S.R.3    Reinheckel, T.4    Peters, C.5    Hook, V.6
  • 13
    • 58149101263 scopus 로고    scopus 로고
    • Major role of cathepsin L for producing the peptide hormones ACTH, beta-endorphin, and alpha-MSH, illustrated by protease gene knockout and expression
    • Funkelstein, L., Toneff, T., Hwang, S. R., Beuschlein, F., Lichtenauer, U. D., Reinheckel, T., Peters, C., and Hook, V. (2008) Major role of cathepsin L for producing the peptide hormones ACTH, beta-endorphin, and alpha-MSH, illustrated by protease gene knockout and expression J Biol Chem 83, 35652–9.
    • (2008) J Biol Chem , vol.83 , pp. 35652-35659
    • Funkelstein, L.1    Toneff, T.2    Hwang, S.R.3    Beuschlein, F.4    Lichtenauer, U.D.5    Reinheckel, T.6    Peters, C.7    Hook, V.8
  • 14
    • 70349443513 scopus 로고    scopus 로고
    • Cathepsin L plays a major role in cholecystokinin production in mouse brain and in pituitary AtT-20 cells: Protease gene knockout and inhibitor studies
    • Beinfeld, M. C., Funkelstein, L., Foulon, T., Cadel, S., Kitagawa, K., Toneff, T., Reinheckel, T., Peters, C., and Hook, V. (2009) Cathepsin L plays a major role in cholecystokinin production in mouse brain and in pituitary AtT-20 cells: Protease gene knockout and inhibitor studies Peptides 30, 1882–991.
    • (2009) Peptides , vol.30 , pp. 1882-1991
    • Beinfeld, M.C.1    Funkelstein, L.2    Foulon, T.3    Cadel, S.4    Kitagawa, K.5    Toneff, T.6    Reinheckel, T.7    Peters, C.8    Hook, V.9
  • 15
    • 72449157397 scopus 로고    scopus 로고
    • Cathepsin L participates in dynorphin neuropeptide production in brain cortex, illustrated by protease gene knockout and expression
    • Minokadeh, A., Funklestein, L., Toneff, T., Hwang, S. R., Reinheckel, T., Peters, C., Zadina, J., and Hook, V. (2010) Cathepsin L participates in dynorphin neuropeptide production in brain cortex, illustrated by protease gene knockout and expression Mol Cell Neurosci 43, 98–107.
    • (2010) Mol Cell Neurosci , vol.43 , pp. 98-107
    • Minokadeh, A.1    Funklestein, L.2    Toneff, T.3    Hwang, S.R.4    Reinheckel, T.5    Peters, C.6    Zadina, J.7    Hook, V.8
  • 17
    • 0031982551 scopus 로고    scopus 로고
    • Arginine and lysine aminopeptidase activities in chromaffin granules of bovine adrenal medulla: Relevance to prohormone processing
    • Yasothornsrikul, S., Toneff, T., Hwang, S. R., and Hook, V. Y. H. (1998) Arginine and lysine aminopeptidase activities in chromaffin granules of bovine adrenal medulla: Relevance to prohormone processing J Neurochem 70, 153–63.
    • (1998) J Neurochem , vol.70 , pp. 153-163
    • Yasothornsrikul, S.1    Toneff, T.2    Hwang, S.R.3    Hook, V.Y.H.4
  • 18
    • 33846964171 scopus 로고    scopus 로고
    • Secretory vesicle aminopeptidase B related to neuropeptide processing: Molecular identification and subcellular localization to enkephalin-and NPY-containing chromaffin granules
    • Hwang, S. R., O’Neill, A., Bark, S., Foulon, T., and Hook, V. (2007) Secretory vesicle aminopeptidase B related to neuropeptide processing: Molecular identification and subcellular localization to enkephalin-and NPY-containing chromaffin granules J Neurochem 100, 1340–50.
    • (2007) J Neurochem , vol.100 , pp. 1340-1350
    • Hwang, S.R.1    O’Neill, A.2    Bark, S.3    Foulon, T.4    Hook, V.5
  • 19
    • 0028325357 scopus 로고
    • Unique cleavage specificity of ‘prohormone thiol protease’ related to proenkephalin processing
    • Azaryan, A. V., and Hook, V. Y. H. (1994) Unique cleavage specificity of ‘prohormone thiol protease’ related to proenkephalin processing FEBS Lett 341, 197–202.
    • (1994) FEBS Lett , vol.341 , pp. 197-202
    • Azaryan, A.V.1    Hook, V.Y.H.2
  • 20
    • 0023864209 scopus 로고
    • Carboxypeptidase E
    • Fricker, L. D. (1988) Carboxypeptidase E Annu Rev Physiol 50, 309–21.
    • (1988) Annu Rev Physiol , vol.50 , pp. 309-321
    • Fricker, L.D.1
  • 21
    • 0002892608 scopus 로고    scopus 로고
    • Carboxypeptidase and aminopeptidase proteases in pro-neuropeptide processing
    • V. Y. H. Hook, ed. Austin, TX: Landes Bio-science Publishers
    • Hook, V. Y. H., and Yasothornsrikul, S. (1998) Carboxypeptidase and aminopeptidase proteases in pro-neuropeptide processing. In: Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing, V. Y. H. Hook, ed. Austin, TX: Landes Bio-science Publishers, pp. 121–40.
    • (1998) Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing , pp. 121-140
    • Hook, V.Y.H.1    Yasothornsrikul, S.2
  • 22
    • 0033535927 scopus 로고    scopus 로고
    • Evidence for the proenkephalin processing enzyme prohormone thiol protease (PTP) as a multicatalytic cysteine protease complex: Activation by glu-tathione localized to secretory vesicles
    • Yasothornsrikul, S., Aaron, W., Toneff, T., and Hook, V. Y. (1999) Evidence for the proenkephalin processing enzyme prohormone thiol protease (PTP) as a multicatalytic cysteine protease complex: Activation by glu-tathione localized to secretory vesicles Biochemistry 38, 7421–30.
    • (1999) Biochemistry , vol.38 , pp. 7421-7430
    • Yasothornsrikul, S.1    Aaron, W.2    Toneff, T.3    Hook, V.Y.4
  • 23
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry to proteomic chemistry
    • Cravatt, B. F., Wright, A. R., and Kozarich, J. W. (2008) Activity-based protein profiling: From enzyme chemistry to proteomic chemistry Annu Rev Biochem 77, 383–414.
    • (2008) Annu Rev Biochem , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.R.2    Kozarich, J.W.3
  • 24
    • 33846591067 scopus 로고    scopus 로고
    • Role of NPY for vasoregulation in the splanchnic circulation during portal hypertension
    • Wiest, R., Jurzik, L., Herold, T., Straub, R. H., and Scholmerich, J. (2007) Role of NPY for vasoregulation in the splanchnic circulation during portal hypertension Peptides 28, 396–404.
    • (2007) Peptides , vol.28 , pp. 396-404
    • Wiest, R.1    Jurzik, L.2    Herold, T.3    Straub, R.H.4    Scholmerich, J.5
  • 27
    • 34648832260 scopus 로고    scopus 로고
    • Dynorphin and the pathophysiology of drug addiction
    • Shippenberg, T. S., Zapata, A., and Chefer, V. I. (2007) Dynorphin and the pathophysiology of drug addiction Pharmacol Therapeut 116, 306–21.
    • (2007) Pharmacol Therapeut , vol.116 , pp. 306-321
    • Shippenberg, T.S.1    Zapata, A.2    Chefer, V.I.3
  • 30
    • 0017597440 scopus 로고
    • Conversion of proinsulin into insulin by cathepsins B and L from rat liver lysosomes
    • Ansorge, S., Kirschke, H., and Friedrich, K. (1977) Conversion of proinsulin into insulin by cathepsins B and L from rat liver lysosomes Acta Biol Med Ger 36, 1723–7.
    • (1977) Acta Biol Med Ger , vol.36 , pp. 1723-1727
    • Ansorge, S.1    Kirschke, H.2    Friedrich, K.3
  • 31
    • 0024217731 scopus 로고
    • Localization of cathepsin L in rat kidney revealed by immunoenzyme and immunogold techniques
    • Yokota, S., Nishimura, Y., and Kato, K. (1988) Localization of cathepsin L in rat kidney revealed by immunoenzyme and immunogold techniques Histochemistry 90, 277–83.
    • (1988) Histochemistry , vol.90 , pp. 277-283
    • Yokota, S.1    Nishimura, Y.2    Kato, K.3
  • 32
    • 4344639552 scopus 로고    scopus 로고
    • Electron histochemical localization of cathepsin L in the liver
    • Ryvnyak, V. V., Ryvnyak, E. I., and Tudos, R. V. (2004) Electron histochemical localization of cathepsin L in the liver Bull Exp Biol Med 137, 90–1.
    • (2004) Bull Exp Biol Med , vol.137 , pp. 90-91
    • Ryvnyak, V.V.1    Ryvnyak, E.I.2    Tudos, R.V.3
  • 33
    • 0028990820 scopus 로고
    • Cysteine proteinases in GH4C1 cells, a rat pituitary tumor cell line, are secreted by the constitutive and regulated secretory pathways
    • Waguri, S., Sato, N., Watanabe, T., Ishidoh, K., Kominami, E., Sato, K., and Uchiyama, Y. (1995) Cysteine proteinases in GH4C1 cells, a rat pituitary tumor cell line, are secreted by the constitutive and regulated secretory pathways Eur J Cell Biol 67, 308–18.
    • (1995) Eur J Cell Biol , vol.67 , pp. 308-318
    • Waguri, S.1    Sato, N.2    Watanabe, T.3    Ishidoh, K.4    Kominami, E.5    Sato, K.6    Uchiyama, Y.7
  • 35
    • 0025789665 scopus 로고
    • Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking
    • Fukuda, M. (1991) Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking J Biol Chem 266, 21327–30.
    • (1991) J Biol Chem , vol.266 , pp. 21327-21330
    • Fukuda, M.1
  • 36
    • 70149114788 scopus 로고    scopus 로고
    • Hyman pituitary contains dual cathepsin L and prohormone convertase processing pathway components involved in converting POMC into the peptide hormones ACTH, alpha-MSH, and beta-endorphin
    • Hook, V., Funkelstein, L., Toneff, T., Mosier, C., and Hwang, S. R. (2009) Hyman pituitary contains dual cathepsin L and prohormone convertase processing pathway components involved in converting POMC into the peptide hormones ACTH, alpha-MSH, and beta-endorphin Endocrine 35, 429–37.
    • (2009) Endocrine , vol.35 , pp. 429-437
    • Hook, V.1    Funkelstein, L.2    Toneff, T.3    Mosier, C.4    Hwang, S.R.5
  • 37
    • 0030032833 scopus 로고    scopus 로고
    • Nuclear localization of procathepsin L/MEP in ras-transformed mouse fibroblasts
    • Hiwasa, T., and Sakiyama, S. (1996) Nuclear localization of procathepsin L/MEP in ras-transformed mouse fibroblasts Cancer Lett 99, 87–91.
    • (1996) Cancer Lett , vol.99 , pp. 87-91
    • Hiwasa, T.1    Sakiyama, S.2
  • 38
  • 39
    • 70149114788 scopus 로고    scopus 로고
    • Human pituitary contains dual cathepsin L and prohormone convertase processing pathway components involved in converting POMC into the peptide hormones ACTH, alpha-MSH, and beta-endorphin
    • Hook, V., Funkelstein, L., Toneff, T., Mosier, C., and Hwang, S. R. (2009) Human pituitary contains dual cathepsin L and prohormone convertase processing pathway components involved in converting POMC into the peptide hormones ACTH, alpha-MSH, and beta-endorphin Endocrine 35, 429–37.
    • (2009) Endocrine , vol.35 , pp. 429-437
    • Hook, V.1    Funkelstein, L.2    Toneff, T.3    Mosier, C.4    Hwang, S.R.5
  • 40
    • 19544393760 scopus 로고    scopus 로고
    • Cutting back on pro-protein convertases: The latest approaches to pharmacological inhibition
    • Fugere, M., and Day, R. (2005) Cutting back on pro-protein convertases: The latest approaches to pharmacological inhibition Trends Pharmacol Sci 26, 294–301.
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 294-301
    • Fugere, M.1    Day, R.2
  • 42
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: From protein traffic to embryogenesis and disease
    • Thomas, G. (2002) Furin at the cutting edge: From protein traffic to embryogenesis and disease Nature Rev 3, 753–66.
    • (2002) Nature Rev , vol.3 , pp. 753-766
    • Thomas, G.1
  • 43
    • 19644394871 scopus 로고    scopus 로고
    • The novel bovine serpin endopin 2C demonstrates selective inhibition of the cysteine protease cathepsin L compared to the serine protease elastase, in cross-class inhibition
    • Hwang, S. R., Stoka, V., Turk, V., and Hook, V. Y. (2005) The novel bovine serpin endopin 2C demonstrates selective inhibition of the cysteine protease cathepsin L compared to the serine protease elastase, in cross-class inhibition Biochemistry 44, 7757–67.
    • (2005) Biochemistry , vol.44 , pp. 7757-7767
    • Hwang, S.R.1    Stoka, V.2    Turk, V.3    Hook, V.Y.4
  • 46
    • 0035980127 scopus 로고    scopus 로고
    • Inhibitory specificity and potency of proSAAS-derived peptides toward proprotein convertase 1
    • Basak, A., Koch, P., Dupelle, M., Fricker, L. D., Devi, L. A. et al. (2001) Inhibitory specificity and potency of proSAAS-derived peptides toward proprotein convertase 1 J Biol Chem 276, 32720–8.
    • (2001) J Biol Chem , vol.276 , pp. 32720-32728
    • Basak, A.1    Koch, P.2    Dupelle, M.3    Fricker, L.D.4    Devi, L.A.5
  • 47
    • 0032819395 scopus 로고    scopus 로고
    • The role of the 7B2 CT peptide in the inhibition of prohormone convertase 2 in endocrine cell lines
    • Fortenberry, Y., Liu, J., and Lindberg, I. (1999) The role of the 7B2 CT peptide in the inhibition of prohormone convertase 2 in endocrine cell lines J Neurochem 73, 994–1003.
    • (1999) J Neurochem , vol.73 , pp. 994-1003
    • Fortenberry, Y.1    Liu, J.2    Lindberg, I.3
  • 48
    • 33746216577 scopus 로고    scopus 로고
    • The proprotein convertases and their implication in sterol and/or lipid metabolism
    • Seidah, N. G., Khatib, A. M., and Prat, A. (2006) The proprotein convertases and their implication in sterol and/or lipid metabolism Biol Chem 387, 871–7.
    • (2006) Biol Chem , vol.387 , pp. 871-877
    • Seidah, N.G.1    Khatib, A.M.2    Prat, A.3
  • 49
    • 27644521904 scopus 로고    scopus 로고
    • Proprotein convertases: “master switches” in the regulation of tumor growth and progression
    • Bassi, D. E., Fu, J., Lopez de Cicco, R., and Klein-Szanto, A. J. (2005) Proprotein convertases: “master switches” in the regulation of tumor growth and progression Mol Carcinogen 44, 151–61.
    • (2005) Mol Carcinogen , vol.44 , pp. 151-161
    • Bassi, D.E.1    Fu, J.2    Lopez de Cicco, R.3    Klein-Szanto, A.J.4
  • 50
    • 27744607688 scopus 로고    scopus 로고
    • Proprotein convertases furin and PC5: Targeting atherosclerosis and restenosis at multiple levels
    • Stawowy, P., and Fleck, E. (2005) Proprotein convertases furin and PC5: Targeting atherosclerosis and restenosis at multiple levels J Molec Med 83, 865–75.
    • (2005) J Molec Med , vol.83 , pp. 865-875
    • Stawowy, P.1    Fleck, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.