糖蛋白激素α亚基

Glycoprotein hormones, alpha polypeptide; 绒毛膜促性腺激素，α多肽
	PDB rendering based on 1dz7.
有效结构
PDB	直系同源检索：PDBe, RCSB
PDB查询代码列表
	1DZ7, 1E9J, 1FL7, 1HCN, 1HD4, 1HRP, 1QFW, 1XWD, 4AY9
标识
代号	CGA; CG-ALPHA; FSHA; GPHA1; GPHa; HCG; LHA; TSHA
扩展标识	遗传学：118850 鼠基因：88390 同源基因：587 GeneCards: CGA Gene
基因本体论描述
分子功能	· hormone activity; · protein binding;
细胞成分	· extracellular region;
生物过程	· thyroid hormone generation; · signal transduction; · cell-cell signaling; · positive regulation of cell proliferation; · gonad development; · peptide hormone processing; · positive regulation of cell migration; · thyroid gland development; · luteinizing hormone secretion; · cellular response to hormone stimulus; · cellular protein metabolic process; · positive regulation of transcription from RNA polymerase II promoter; · negative regulation of organ growth; · follicle-stimulating hormone secretion; · developmental growth;
	Sources: Amigo / QuickGO
RNA表达模式
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糖蛋白激素α亚基（英語：Alpha subunit of glycoprotein hormones，或称为绒毛膜促性腺激素α亚基，Glycoprotein hormones alpha chain）是一个由人类基因CGA 编码的蛋白质^[1]。

人体的四种糖蛋白激素（英语：glycoprotein hormones）--人绒毛膜促性腺激素（hCG）、黄体生成素（LH）、促卵泡激素（FSH）和促甲状腺激素（TSH）都是以同样的该α亚基和各自不同的β亚基组成的二聚体。^[2]

此α链的92个氨基酸残基的序列为：

NH₂ - Ala - Pro - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys - Thr - Leu - Gln - Glu - Asn - Pro - Phe - Phe - Ser - Gln - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys - Val - Ala - Lys - Ser - Tyr - Asn - Arg - Val - Thr - Val - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His - Lys - Ser - COOH

参考文献

^ Fiddes JC, Goodman HM. The gene encoding the common alpha subunit of the four human glycoprotein hormones. J Mol Appl Genet. Oct 1982, 1 (1): 3–18. PMID 6286817.
^ Entrez Gene: CGA glycoprotein hormones, alpha polypeptide. （原始内容存档于2010-12-05）.

延伸阅读

Roger M, Lahlou N, Couzinet B; et al. [Free alpha-subunit glycoprotein hormones: physiological and pathological data]. J. Steroid Biochem. 1990, 33 (4B): 763–9. PMID 2481154. doi:10.1016/0022-4731(89)90489-5.
Pierce JG. Eli Lilly lecture. The subunits of pituitary thyrotropin--their relationship to other glycoprotein hormones.. Endocrinology. 1972, 89 (6): 1331–44. PMID 5002675. doi:10.1210/endo-89-6-1331.
Kourides IA, Gurr JA, Wolf O. The regulation and organization of thyroid stimulating hormone genes.. Recent Prog. Horm. Res. 1984, 40: 79–120. PMID 6207569.
Miyoshi I, Kasai N, Hayashizaki Y. [Structure and regulation of human thyroid-stimulating hormone (TSH) gene]. Nippon Rinsho. 1994, 52 (4): 940–7. PMID 8196184.
Barrios-De-Tomasi J, Timossi C, Merchant H; et al. Assessment of the in vitro and in vivo biological activities of the human follicle-stimulating isohormones.. Mol. Cell. Endocrinol. 2002, 186 (2): 189–98. PMID 11900895. doi:10.1016/S0303-7207(01)00657-8.
Moyle WR, Bahl OP, März L. Role of carbohydrate of human chorionic gonadotropin in the mechanism of hormone action.. J. Biol. Chem. 1976, 250 (23): 9163–9. PMID 172504.
Fiddes JC, Goodman HM. Isolation, cloning and sequence analysis of the cDNA for the alpha-subunit of human chorionic gonadotropin.. Nature. 1979, 281 (5730): 351–6. PMID 481597. doi:10.1038/281351a0.
Sairam MR, Li CH. Human pituitary thyrotropin. The primary structure of the alpha and beta subunits.. Can. J. Biochem. 1977, 55 (7): 755–60. PMID 890569. doi:10.1139/o77-108.
Morgan FJ, Birken S, Canfield RE. The amino acid sequence of human chorionic gonadotropin. The alpha subunit and beta subunit.. J. Biol. Chem. 1975, 250 (13): 5247–58. PMID 1150658.
Rathnam P, Saxena BB. Primary amino acid sequence of follicle-stimulating hormone from human pituitary glands. I. alpha subunit.. J. Biol. Chem. 1975, 250 (17): 6735–46. PMID 1158880.
Weisshaar G, Hiyama J, Renwick AG, Nimtz M. NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.. Eur. J. Biochem. 1991, 195 (1): 257–68. PMID 1991473. doi:10.1111/j.1432-1033.1991.tb15702.x.
Sakakibara R, Yokoo Y, Yoshikoshi K; et al. Subcellular localization of intracellular forms of human chorionic gonadotropin in first trimester placenta.. J. Biochem. 1988, 102 (5): 993–1001. PMID 2449427.
Matzuk MM, Keene JL, Boime I. Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction.. J. Biol. Chem. 1989, 264 (5): 2409–14. PMID 2536708.
Lustbader JW, Birken S, Pileggi NF; et al. Crystallization and characterization of human chorionic gonadotropin in chemically deglycosylated and enzymatically desialylated states.. Biochemistry. 1990, 28 (24): 9239–43. PMID 2611225. doi:10.1021/bi00450a001.
Harris DC, Machin KJ, Evin GM; et al. Preliminary X-ray diffraction analysis of human chorionic gonadotropin.. J. Biol. Chem. 1989, 264 (12): 6705–6. PMID 2708337.
Hayashizaki Y, Miyai K, Kato K, Matsubara K. Molecular cloning of the human thyrotropin-beta subunit gene.. FEBS Lett. 1985, 188 (2): 394–400. PMID 3839756. doi:10.1016/0014-5793(85)80409-9.
Bellisario R, Carlsen RB, Bahl OP. Human chorionic gonadotropin. Linear amino acid sequence of the alpha subunit.. J. Biol. Chem. 1973, 248 (19): 6796–809. PMID 4745444.
Shome B, Parlow AF. Human follicle stimulating hormone (hFSH): first proposal for the amino acid sequence of the alpha-subunit (hFSHa) and first demonstration of its identity with the alpha-subunit of human luteinizing hormone (hLHa).. J. Clin. Endocrinol. Metab. 1974, 39 (1): 199–202. PMID 4835135. doi:10.1210/jcem-39-1-199.