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Molecular Endocrinology, Vol 6, 2210-2218, Copyright © 1992 by Endocrine Society
ARTICLES |
RW Hipkin, J Sanchez-Yague and M Ascoli
Department of Pharmacology, University of Iowa College of Medicine, Iowa City 52242.
It is well established that the LH/CG receptor expressed in gonadal cells is an 85- to 92-kilodalton (kDa) glycoprotein. Additionally, however, a number of reports have noted the existence of other putative receptor species, but few attempts have been made to characterize these variant receptor species. A cell line [293L(wt1)] had previously been isolated which expresses large numbers of high affinity cell surface LH/CG receptors. Visualization of the LH/CG receptor species expressed in these cells and in rat luteal cells using ligand blots revealed 85- and 90-kDa LH/CG receptors, respectively, while immunoblots revealed another 68-kDa glycoprotein receptor in both cell types. The presence of both the 85- and 68-kDa receptor species was confirmed using immunoprecipitation and affinity purification of metabolically labeled 293L(wt1) cells. Enzymatic deglycosylations established that the 85-kDa receptor is a sialoprotein, while the 68-kDa species contains exposed high mannose residues. Protease digestion before LH/CG receptor immunoprecipitations localized the 85-kDa receptor on the plasma membrane, while the 68-kDa receptor was shown to be located intracellularly. Pulse-chase experiments were then used to positively establish that the 68-kDa receptor protein is actually a precursor of the 85-kDa LH/CG receptor species.
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C. Galet, L. Min, R. Narayanan, M. Kishi, N. L. Weigel, and M. Ascoli 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., March 1, 2003; 17(3): 411 - 422. [Abstract] [Full Text] [PDF]
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J. W. M. Martens, S. Lumbroso, M. Verhoef-Post, V. Georget, A. Richter-Unruh, M. Szarras-Czapnik, T. E. Romer, H. G. Brunner, A. P. N. Themmen, and Ch. Sultan Mutant Luteinizing Hormone Receptors in a Compound Heterozygous Patient with Complete Leydig Cell Hypoplasia: Abnormal Processing Causes Signaling Deficiency J. Clin. Endocrinol. Metab., June 1, 2002; 87(6): 2506 - 2513. [Abstract] [Full Text] [PDF]
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T. Hirakawa, C. Galet, and M. Ascoli MA-10 Cells Transfected with the Human Lutropin/Choriogonadotropin Receptor (hLHR): A Novel Experimental Paradigm to Study the Functional Properties of the hLHR Endocrinology, March 1, 2002; 143(3): 1026 - 1035. [Abstract] [Full Text] [PDF]
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L. Min and M. Ascoli Effect of Activating and Inactivating Mutations on the Phosphorylation and Trafficking of the Human Lutropin/Choriogonadotropin Receptor Mol. Endocrinol., November 1, 2000; 14(11): 1797 - 1810. [Abstract] [Full Text]
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S. Li, X. Liu, and M. Ascoli p38JAB1 Binds to the Intracellular Precursor of the Lutropin/Choriogonadotropin Receptor and Promotes Its Degradation J. Biol. Chem., April 28, 2000; 275(18): 13386 - 13393. [Abstract] [Full Text] [PDF]
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U. E. Petaja-Repo, M. Hogue, A. Laperriere, P. Walker, and M. Bouvier 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., April 28, 2000; 275(18): 13727 - 13736. [Abstract] [Full Text] [PDF]
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K.-S. Min, X. Liu, J. Fabritz, J. Jaquette, A. N. Abell, and M. Ascoli Mutations That Induce Constitutive Activation and Mutations That Impair Signal Transduction Modulate the Basal and/or Agonist-stimulated Internalization of the Lutropin/Choriogonadotropin Receptor J. Biol. Chem., December 25, 1998; 273(52): 34911 - 34919. [Abstract] [Full Text] [PDF]
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T. G. Rozell, D. P. Davis, Y. Chai, and D. L. Segaloff Association of Gonadotropin Receptor Precursors with the Protein Folding Chaperone Calnexin Endocrinology, April 1, 1998; 139(4): 1588 - 1593. [Abstract] [Full Text] [PDF]
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D. P. Davis, T. G. Rozell, X. Liu, and D. L. Segaloff The Six N-linked Carbohydrates of the Lutropin/Choriogonadotropin Receptor Are Not Absolutely Required for Correct Folding, Cell Surface Expression, Hormone Binding, or Signal Transduction Mol. Endocrinol., May 1, 1997; 11(5): 550 - 562. [Abstract] [Full Text]
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F. A. Bradbury, N. Kawate, C. M. Foster, and K. M.J. Menon 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., February 28, 1997; 272(9): 5921 - 5926. [Abstract] [Full Text] [PDF]
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Z. Wang, X. Liu, and M. Ascoli Phosphorylation of the Lutropin/Choriogonadotropin Receptor Facilitates Uncoupling of the Receptor from Adenylyl Cyclase and Endocytosis of the Bound Hormone Mol. Endocrinol., February 1, 1997; 11(2): 183 - 192. [Abstract] [Full Text]
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A. Abell, X. Liu, and D. L. Segaloff Deletions of Portions of the Extracellular Loops of the Lutropin/Choriogonadotropin Receptor Decrease the Binding Affinity for Ovine Luteinizing Hormone, but Not Human Choriogonadotropin, by Preventing the Formation of Mature Cell Surface Receptor J. Biol. Chem., February 23, 1996; 271(8): 4518 - 4527. [Abstract] [Full Text] [PDF]
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L. M. Fernandez and D. Puett Lys[IMAGE] in the Third Extracellular Loop of the Lutropin/Choriogonadotropin Receptor Is Critical for Signaling J. Biol. Chem., January 12, 1996; 271(2): 925 - 930. [Abstract] [Full Text] [PDF]
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J. Huang and D. Puett Identification of Two Amino Acid Residues on the Extracellular Domain of the Lutropin/Choriogonadotropin Receptor Important in Signaling J. Biol. Chem., December 15, 1995; 270(50): 30023 - 30028. [Abstract] [Full Text] [PDF]
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