메뉴 건너뛰기




Volumn 377, Issue 1, 2008, Pages 307-311

The extracellular domain of luteinizing hormone receptor dictates its efficiency of maturation

Author keywords

Binding ability; Extracellular domain; LH receptor; Recycling of receptor

Indexed keywords

CYCLIC AMP; LUTEINIZING HORMONE RECEPTOR;

EID: 54449097406     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.09.136     Document Type: Article
Times cited : (8)

References (22)
  • 2
    • 0036217072 scopus 로고    scopus 로고
    • The lutropin/choriogonadotropin receptor, a 2002 perspective
    • Ascoli M., Fanelli F., and Segaloff D.L. The lutropin/choriogonadotropin receptor, a 2002 perspective. Endocr. Rev. 23 2002 (2002) 141-174
    • (2002) Endocr. Rev. , vol.23 , Issue.2002 , pp. 141-174
    • Ascoli, M.1    Fanelli, F.2    Segaloff, D.L.3
  • 3
    • 0027093726 scopus 로고
    • Identification and characterization of a luteinizing hormone/chorionic gonadotropin (LH/CG) receptor precursor in a human kidney cell line stably transfected with the rat luteal LH/CG receptor complementary DNA
    • Hipkin R.W., Sanchez-Yague J., and Ascoli M. Identification and characterization of a luteinizing hormone/chorionic gonadotropin (LH/CG) receptor precursor in a human kidney cell line stably transfected with the rat luteal LH/CG receptor complementary DNA. Mol. Endocrinol. 6 (1992) 2210-2218
    • (1992) Mol. Endocrinol. , vol.6 , pp. 2210-2218
    • Hipkin, R.W.1    Sanchez-Yague, J.2    Ascoli, M.3
  • 4
    • 0032512441 scopus 로고    scopus 로고
    • Transfected cells express mostly the intracellular precursor of the lutropin/choriogonadotropin receptor but this precursor binds choriogonadotropin with high affinity
    • Fabritz J., Ryan S., and Ascoli M. Transfected cells express mostly the intracellular precursor of the lutropin/choriogonadotropin receptor but this precursor binds choriogonadotropin with high affinity. Biochemistry 37 (1998) 664-672
    • (1998) Biochemistry , vol.37 , pp. 664-672
    • Fabritz, J.1    Ryan, S.2    Ascoli, M.3
  • 5
    • 22544435246 scopus 로고    scopus 로고
    • Inefficient maturation of the rat luteinizing hormone receptor. A putative way to regulate receptor numbers at the cell surface
    • Pietila E.M., Tuusa J.T., Apaja P.M., Aatsinki J.T., Hakalahti A.E., Rajaniemi H.J., and Petaja-Repo U.E. Inefficient maturation of the rat luteinizing hormone receptor. A putative way to regulate receptor numbers at the cell surface. J. Biol. Chem. 280 (2005) 26622-26629
    • (2005) J. Biol. Chem. , vol.280 , pp. 26622-26629
    • Pietila, E.M.1    Tuusa, J.T.2    Apaja, P.M.3    Aatsinki, J.T.4    Hakalahti, A.E.5    Rajaniemi, H.J.6    Petaja-Repo, U.E.7
  • 6
    • 14844291405 scopus 로고    scopus 로고
    • Evidence that palmitoylation of carboxyl terminus cysteine residues of the human luteinizing hormone receptor regulates postendocytic processing
    • Munshi U.M., Clouser C.L., Peegel H., and Menon K.M.J. Evidence that palmitoylation of carboxyl terminus cysteine residues of the human luteinizing hormone receptor regulates postendocytic processing. Mol. Endocrinol. 19 (2005) 749-758
    • (2005) Mol. Endocrinol. , vol.19 , pp. 749-758
    • Munshi, U.M.1    Clouser, C.L.2    Peegel, H.3    Menon, K.M.J.4
  • 7
    • 0034810859 scopus 로고    scopus 로고
    • Retention of glucose on oligosaccharide chains linked to the LH/hCG receptor prevents cell surface expression
    • Bradbury F.A., and Menon K.M.J. Retention of glucose on oligosaccharide chains linked to the LH/hCG receptor prevents cell surface expression. Biochem. Biophys. Res. Commun. 282 (2001) 454-462
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 454-462
    • Bradbury, F.A.1    Menon, K.M.J.2
  • 8
    • 0017189044 scopus 로고
    • Gonadotropin receptors in plasma membranes of bovine corpus luteum. II. Role of membrane phospholipids
    • Azhar S., Hajra A.K., and Menon K.M.J. Gonadotropin receptors in plasma membranes of bovine corpus luteum. II. Role of membrane phospholipids. J. Biol. Chem 251 (1976) 7405-7412
    • (1976) J. Biol. Chem , vol.251 , pp. 7405-7412
    • Azhar, S.1    Hajra, A.K.2    Menon, K.M.J.3
  • 9
    • 0027999333 scopus 로고
    • Palmitoylation of luteinizing hormone/human choriogonadotropin receptors in transfected cells. Abolition of palmitoylation by mutation of Cys-621 and Cys-622 residues in the cytoplasmic tail increases ligand-induced internalization of the receptor
    • Kawate N., and Menon K.M.J. Palmitoylation of luteinizing hormone/human choriogonadotropin receptors in transfected cells. Abolition of palmitoylation by mutation of Cys-621 and Cys-622 residues in the cytoplasmic tail increases ligand-induced internalization of the receptor. J. Biol. Chem. 269 (1994) 30651-30658
    • (1994) J. Biol. Chem. , vol.269 , pp. 30651-30658
    • Kawate, N.1    Menon, K.M.J.2
  • 10
    • 0032836647 scopus 로고    scopus 로고
    • A dileucine-based motif in the C-terminal tail of the lutropin/choriogonadotropin receptor inhibits endocytosis of the agonist-receptor complex
    • Nakamura K., and Ascoli M. A dileucine-based motif in the C-terminal tail of the lutropin/choriogonadotropin receptor inhibits endocytosis of the agonist-receptor complex. Mol. Pharmacol. 56 (1999) 728-736
    • (1999) Mol. Pharmacol. , vol.56 , pp. 728-736
    • Nakamura, K.1    Ascoli, M.2
  • 11
    • 0033529237 scopus 로고    scopus 로고
    • Evidence that constitutively active luteinizing hormone/human chorionic gonadotropin receptors are rapidly internalized
    • Bradbury F.A., and Menon K.M.J. Evidence that constitutively active luteinizing hormone/human chorionic gonadotropin receptors are rapidly internalized. Biochemistry 38 (1999) 8703-8712
    • (1999) Biochemistry , vol.38 , pp. 8703-8712
    • Bradbury, F.A.1    Menon, K.M.J.2
  • 12
    • 0031046907 scopus 로고    scopus 로고
    • Post-translational processing in the Golgi plays a critical role in the trafficking of the luteinizing hormone/human chorionic gonadotropin receptor to the cell surface
    • Bradbury F.A., Kawate N., Foster C.M., and Menon K.M.J. Post-translational processing in the Golgi plays a critical role in the trafficking of the luteinizing hormone/human chorionic gonadotropin receptor to the cell surface. J. Biol. Chem. 272 (1997) 5921-5926
    • (1997) J. Biol. Chem. , vol.272 , pp. 5921-5926
    • Bradbury, F.A.1    Kawate, N.2    Foster, C.M.3    Menon, K.M.J.4
  • 13
    • 0031734361 scopus 로고    scopus 로고
    • Association of gonadotropin receptor precursors with the protein folding chaperone calnexin
    • Rozell T.G., Davis D.P., Chai Y., and Segaloff D.L. Association of gonadotropin receptor precursors with the protein folding chaperone calnexin. Endocrinology 139 (1998) 1588-1593
    • (1998) Endocrinology , vol.139 , pp. 1588-1593
    • Rozell, T.G.1    Davis, D.P.2    Chai, Y.3    Segaloff, D.L.4
  • 14
    • 0015925767 scopus 로고
    • Spare gonadotrophin receptors in rat testis
    • Catt K.J., and Dufau M.L. Spare gonadotrophin receptors in rat testis. Nat. New Biol. 244 (1973) 219-221
    • (1973) Nat. New Biol. , vol.244 , pp. 219-221
    • Catt, K.J.1    Dufau, M.L.2
  • 15
    • 0017163710 scopus 로고
    • 125I-labelled choriogonadotropin binding cyclic adenosine 3′,5′-monophosphate formation and progesterone synthesis in the rat ovary
    • 125I-labelled choriogonadotropin binding cyclic adenosine 3′,5′-monophosphate formation and progesterone synthesis in the rat ovary. Biochim. Biophys. Acta 444 (1976) 23-32
    • (1976) Biochim. Biophys. Acta , vol.444 , pp. 23-32
    • Clark, M.R.1    Menon, K.M.J.2
  • 16
    • 0037341727 scopus 로고    scopus 로고
    • Identification of a transferable two-amino-acid motif (GT) present in the C-terminal tail of the human lutropin receptor that redirects internalized G protein-coupled receptors from a degradation to a recycling pathway
    • Galet C., Min L., Narayanan R., Kishi M., Weigel N.L., and Ascoli M. Identification of a transferable two-amino-acid motif (GT) present in the C-terminal tail of the human lutropin receptor that redirects internalized G protein-coupled receptors from a degradation to a recycling pathway. Mol. Endocrinol. 17 (2003) 411-422
    • (2003) Mol. Endocrinol. , vol.17 , pp. 411-422
    • Galet, C.1    Min, L.2    Narayanan, R.3    Kishi, M.4    Weigel, N.L.5    Ascoli, M.6
  • 17
    • 3042788953 scopus 로고    scopus 로고
    • Intracellularly located misfolded glycoprotein hormone receptors associate with different chaperone proteins than their cognate wild-type receptors
    • Mizrachi D., and Segaloff D.L. Intracellularly located misfolded glycoprotein hormone receptors associate with different chaperone proteins than their cognate wild-type receptors. Mol. Endocrinol. 18 (2004) 1768-1777
    • (2004) Mol. Endocrinol. , vol.18 , pp. 1768-1777
    • Mizrachi, D.1    Segaloff, D.L.2
  • 18
    • 23044484256 scopus 로고    scopus 로고
    • Expression of the mature luteinizing hormone receptor in rodent urogenital and adrenal tissues is developmentally regulated at a posttranslational level
    • Apaja P.M., Aatsinki J.T., Rajaniemi H.J., and Petaja-Repo U.E. Expression of the mature luteinizing hormone receptor in rodent urogenital and adrenal tissues is developmentally regulated at a posttranslational level. Endocrinology 146 (2005) 3224-3232
    • (2005) Endocrinology , vol.146 , pp. 3224-3232
    • Apaja, P.M.1    Aatsinki, J.T.2    Rajaniemi, H.J.3    Petaja-Repo, U.E.4
  • 19
    • 0034607918 scopus 로고    scopus 로고
    • Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor
    • Petaja-Repo U.E., Hogue M., Laperriere A., Walker P., and Bouvier M. Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor. J. Biol. Chem. 275 (2000) 13727-13736
    • (2000) J. Biol. Chem. , vol.275 , pp. 13727-13736
    • Petaja-Repo, U.E.1    Hogue, M.2    Laperriere, A.3    Walker, P.4    Bouvier, M.5
  • 20
    • 34447633217 scopus 로고    scopus 로고
    • The endoplasmic reticulum Ca2+-pump SERCA2b interacts with G protein-coupled receptors and enhances their expression at the cell surface
    • Tuusa J.T., Markkanen P.M., Apaja P.M., Hakalahti A.E., and Petaja-Repo U.E. The endoplasmic reticulum Ca2+-pump SERCA2b interacts with G protein-coupled receptors and enhances their expression at the cell surface. J. Mol. Biol. 371 (2007) 622-638
    • (2007) J. Mol. Biol. , vol.371 , pp. 622-638
    • Tuusa, J.T.1    Markkanen, P.M.2    Apaja, P.M.3    Hakalahti, A.E.4    Petaja-Repo, U.E.5
  • 22
    • 6344231396 scopus 로고    scopus 로고
    • Leydig cell hypoplasia: absent luteinizing hormone receptor cell surface expression caused by a novel homozygous mutation in the extracellular domain
    • Richter-Unruh A., Verhoef-Post M., Malak S., Homoki J., Hauffa B.P., and Themmen A.P. Leydig cell hypoplasia: absent luteinizing hormone receptor cell surface expression caused by a novel homozygous mutation in the extracellular domain. J. Clin. Endocrinol. Metab. 89 (2004) 5161-5167
    • (2004) J. Clin. Endocrinol. Metab. , vol.89 , pp. 5161-5167
    • Richter-Unruh, A.1    Verhoef-Post, M.2    Malak, S.3    Homoki, J.4    Hauffa, B.P.5    Themmen, A.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.