Abstract
Two prolactin-like proteins (bPLP-I and bPLP-II) were deduced from the nucleotide sequence analyses of the cDNA clones derived from a bovine (Bos taurus) term placenta. These proteins resembled bovine prolactin but were different from the reported bovine placental lactogens or prolactin-related proteins. The predicted amino acid sequences of these clones showed 45-51% identity with bovine prolactin and 23-24% with bovine growth hormone. The two new clones show 62 and 39% overall homology with each other at the levels of nucleotide and amino acid sequences, respectively. bPLP-I, bPLP-II, placental lactogens, prolactins (PRLs), and other prolactin-like proteins isolated from cow, mouse, and rat share 7 common amino acid residues. Five of the 7 residues are conserved by other members of the family such as growth hormones, suggesting that they may be essential for the common structural features of the gene family. The other 2 residues are uniquely conserved in bovine, mouse, and rat placental lactogens, PRLs, and PRL-like proteins, predicting their indispensable roles in binding to the specific receptors. bPLP-I and bPLP-II, as well as bPLP-III, are shown to be expressed stage specifically and predominantly in full-term bovine placentas.
Highlights
Were deduced from the nucleotide sequence analyses of the cDNA clones derived from a bovine (Bos taurus) term placenta
Clones-The bovine placental cDNA library was first screened with the Bovine GH (bGH) cDNA probe
We report here the isolation and characterization of two novel prolactin-like cDNA clones, bPLP-I and bPLP-II, from bovine (B. taurus) term placenta
Summary
’ Tbe abbreviations used are: PL, placental lactogen; PRL, prolactin; GH, growth hormone; PLP, prolactin-like protein; PRC, prolactin-related cDNA; PD, prolactin domain; GD, growth hormone domain; LD, lactogen domain; SDS, sodium dodecyl sulfate. II were determined by the dideoxy chain termination method as described under “Experimental. The open and dotted areas indicate putative signal peptide and mature protein regions, respectively. The solid areas represent the 5’- and 3’-noncoding regions. Upper and lowerpanels are for bPLP-I and bPLP-II, respectively. The termination codons are marked with czsterisks. Potential glycosylation sites are underlined with dashed lines. The polyadenylation signals are shown by solid underlines
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