A synthetic peptide representing residues 7 to 21 of human luteinizing hormone β-subunit binds calcium, facilitates calcium uptake by liposomes and possesses sequence similarity to calcium-binding domains of calmodulin

Regulatory Peptides

Volumn 65, Issue 2, 1996, Pages 109-114

  Grasso, Patricia ^a  

^a ALBANY MEDICAL COLLEGE   (United States)

Author keywords

Calcium flux; Calcium binding domains of calmodulin; hLH subunit; Liposome; Synthetic peptide

Indexed keywords

CALCIUM CHANNEL; CALCIUM CHANNEL BLOCKING AGENT; LIPOSOME; LUTEINIZING HORMONE DERIVATIVE; LUTEINIZING HORMONE RECEPTOR; NIFEDIPINE;

ARTICLE; CALCIUM TRANSPORT; CONTROLLED STUDY; PRIORITY JOURNAL;

EID: 0030576712     PISSN: 01670115     EISSN: None     Source Type: Journal    
DOI: 10.1016/0167-0115(96)00079-1     Document Type: Article

References (26)

1. [1] Bousfield, G.R., Perry, W.M. and Ward, D.N., Gonadotropins: chemistry and biosynthesis. In E. Knobil and J.D. Neill (Eds.), The Physiology of Reproduction, 2nd Edn. Raven Press, New York, NY, 1994, pp. 1749-1792.
2. [2] Combarnous, Y., Molecular basis of the specificity of binding of glycoprotin hormones to their receptors, Endocrine Rev., 13 (1992) 670-691.
3. [3] Sanzo, M. and Reichert Jr., L.E., Gonadotropin receptor binding regulators in serum, J. Biol. Chem., 257 (1982) 6033-6040.
4. [4] Sluss, P.M. and Reichert Jr., L.E., Differential effects of calcium on LH binding to intact cells and membranes from rat testes, IRCS Med. Sci., 12 (1984) 748-749.
5. [5] Andersen, T.T. and Reichert Jr., L.E., Follitropin binding to receptors in testis, J. Biol. Chem., 257 (1982) 11551-11557.
6. 2+ by proteoliposomes and cultured rat Sertoli cells: evidence for involvement of voltage-activated and voltage-independent calcium channels, Endocrinology, 125 (1989) 3029-3036.
7. [7] Grasso, P. and Reichert Jr., L.E., Induction of calcium transport into cultured rat Sertoli cells and liposomes by follicle-stimulating hormone, Rec. Prog. Hormone Res., 48 (1993) 517-521.
8. 2+ and possesses sequence similarity to calcium binding sites of calmodulin, Endocrinology, 130 (1992) 1103-1107.
9. 2+ by liposomes: evidence for calcium-conducting transmembrane channel formation. Endocrinology, 128 (1991) 2745-2751.
10. [10] Grasso, P., Snata-Coloma, T.A. and Reichert Jr., L.E., Correlation of follicle-stimulating hormone (FSH)-receptor complex internalization with the sustained phase of FSH-induced calcium uptake by cultured rat Sertoli cells, Endocrinology, 131 (1992) 2622-2628.
11. [11] Grasso, P. and Reichert Jr., L.E., Evidence that a calmodulin-like calcium-binding domain of the FSH-β-subunit is involved in FSH-induced calcium uptake by Sertoli cells, J. Mol. Endocrinol., 13 (1994) 149-155.
12. [12] Merrifield, R.D., Solid phase peptide synthesis. I. The synthesis of a tetrapeptide, J. Am. Chem. Soc., 85 (1963) 2149-2154.
13. [13] Santa-Coloma, T.A. and Reichert Jr., L.E., Determination of alpha-subunit contact regions of hFSH-β subunit using synthetic peptides, J. Biol. Chem., 266 (1991) 2759-2762.
14. [14] Munson, P.J. and Rodbard, D., LIGAND: a versatile computerized approach for characterization of ligand-binding systems, Anal. Biochem., 107 (1980) 220-239.
15. [15] Klee, C.B., Crouch, T.H. and Richman, P.G., Calmodulin, Annu. Rev. Biochem., 49 (1980) 489-515.
16. [16] Reid, R.E., Synthetic fragments of calmodulin calcium-binding site III. A test of the acid pair hypothesis, J. Biol. Chem., 265 (1990) 5971-5976.
17. 2 antagonist binding site from human platelets, Proc. Natl. Acad. Sci. USA, 82 (1985) 7434-7438.
18. [18] Reed, K.C. and Bygrave, F.L., The inhibition of mitochondrial calcium transport by lanthanides and ruthenium red, Biochem. J., 140 (1974) 143-155.
19. [19] Babu, Y.S., Bugg, C.E. and Cook, W.J., Structure of calmodulin refined at 2.2 Å resolution, J. Mol. Biol., 204 (1988) 191-204.
20. [20] Storch, J. and Kleinfield, A.M., The lipid structure of biological membranes, Trends Biochem. Sci., 19 (1985) 418-421.
21. [21] Shai, Y., Bach, D. and Yanousky, A., Channel formation properties of synthetic paradoxin and analogues, J. Biol. Chem., 265 (1990) 20202-20209.
22. [22] Harshman, S., Bpquet, P., Duflot, E., Alouf, J.E., Montecucco, C. and Papini, E., Staphylococcal a-toxin: a study of membrane penetration and pore fromation, J. Biol. Chem., 264 (1989) 14978-14984.
23. [23] Krasne, S., Eisenman, G. and Szabo, G., Freezing and melting of lipid bilayers and the mode of action of nonactin, valinmycin, and gramicidin, Science, 174 (1971) 412-415.
24. [24] Schiffer, M. and Edmundson, A.B., Use of helical wheels to represent the structures of proteins and to identify segments with helical potential, Biophys. J., 7 (1967) 121-135.
25. [25] O'Connell, A.M., Koeppe, II, R.E. and Andersen, O.S., Kinetics of gramicidin channel formation in lipid bilayers: transmembrane monomer association, Science, 250 (1990) 1256-1259.
26. 13C-labeled synthetic melittin and melittin analogues in isotropic solvents by circular dichroism, fluorescence, and NMR spectroscopy, Biochemistry, 28 (1989) 8614-8623.