A Igout, F Frankenne, M L'Hermite-Balériaux, A Martin, G Hennen
{"title":"Somatogenic and lactogenic activity of the recombinant 22 kDa isoform of human placental growth hormone.","authors":"A Igout, F Frankenne, M L'Hermite-Balériaux, A Martin, G Hennen","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>During pregnancy, the human placenta secretes a variant of pituitary growth hormone (hGH-V) differing in sequence from the pituitary growth hormone (hGH-N) by 13 amino acids substitutions. HGH-V replaces hGH-N in the maternal bloodstream during the second half of pregnancy. HGH-V is produced in two, possibly three, isoforms: a 22 kDa form, a glycosylated 25 kDa form, and a probable 26 kDa form resulting from alternative splicing of the mRNA. Here we have studied the somatogenic and lactogenic activity of recombinant 22 kDa hGH-V isoform produced in Escherichia coli and compared it with the 22 kDa form of hGH-N. The two variants exert a similar somatogenic effect on rabbit and rat cells, but differ as regards their lactogenic activity in the rat.</p>","PeriodicalId":77148,"journal":{"name":"Growth regulation","volume":"5 1","pages":"60-5"},"PeriodicalIF":0.0000,"publicationDate":"1995-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Growth regulation","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
During pregnancy, the human placenta secretes a variant of pituitary growth hormone (hGH-V) differing in sequence from the pituitary growth hormone (hGH-N) by 13 amino acids substitutions. HGH-V replaces hGH-N in the maternal bloodstream during the second half of pregnancy. HGH-V is produced in two, possibly three, isoforms: a 22 kDa form, a glycosylated 25 kDa form, and a probable 26 kDa form resulting from alternative splicing of the mRNA. Here we have studied the somatogenic and lactogenic activity of recombinant 22 kDa hGH-V isoform produced in Escherichia coli and compared it with the 22 kDa form of hGH-N. The two variants exert a similar somatogenic effect on rabbit and rat cells, but differ as regards their lactogenic activity in the rat.