维基百科

糖蛋白激素α亚基

（重定向自人绒毛膜促性腺激素α亚基）

糖蛋白激素α亚基（英语：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]。

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
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
RNA表达模式
更多表达数据
直系同源体
物种 人类 小鼠
Entrez 1081 12640
Ensembl ENSG00000135346 ENSMUSG00000028298
UniProt P01215 P01216
mRNA序列 NM_000735 NM_009889
蛋白序列 NP_000726 NP_034019
基因位置 Chr 6:
87.8 – 87.8 Mb		 Chr 4:
34.89 – 34.91 Mb
PubMed查询 [1] [2]

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

编辑
  1. ^ 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. 
  2. ^ Entrez Gene: CGA glycoprotein hormones, alpha polypeptide. （原始内容存档于2010-12-05）. 

延伸阅读

编辑
  • 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. 


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