High impact information on Prl4a1

• We have determined that at least one of the prolactin-like proteins, PLP-A, is recognized by the protein-specific GalNAc-transferase [1].
• Binding of PLP-A to serum proteins was specific for PLP-A and not effectively competed by other members of the prolactin/growth hormone family [2].
• Cross-linking analyses of radioiodinated PLP-A with serum harvested from late gestation rats indicated the presence of two major cross-linked complexes migrating under reducing conditions at 130 and 250 kDa and two minor cross-linked complexes migrating at 70 and 110 kDa [2].
• CHO cell and native placental PLP-A showed similar immunoreactive characteristics and electrophoretic mobilities [2].
• Five oligopeptides corresponding to different regions of the predicted PLP-A amino acid sequence (peptides 1-13, 62-76, 101-114, 129-145, and 152-164) were chemically synthesized by solid phase methodology [3].

Biological context of Prl4a1

• In summary, trophoblast cell-derived PLP-A contributes to the regulation of NK cells at the maternal-fetal interface to ensure appropriate embryonic growth and development [4].

Anatomical context of Prl4a1

• Prolactin-like protein-A is a functional modulator of natural killer cells at the maternal-fetal interface [4].
• Placental PLP-A expression is reciprocal to mesometrial decidua expression of IFNgamma [4].
• The 29 kDa nuclear immunoreactive protein had an equivalent electrophoretic mobility to the 29 kDa PLP-A protein of junctional zone cytosol [5].
• We have specifically identified a 29 kDa protein species in placental cell nuclei with three antibodies directed to three different regions of the predicted amino acid sequence of PLP-A [5].
• Placental lactogen-Iv and -II, and prolactin-like protein-A and -C mRNA levels were significantly decreased in the placentas of A1254-treated rats in a dose-dependent manner [6].

Associations of Prl4a1 with chemical compounds

• Furthermore, tunicamycin shifted the synthesis of PLP-A by placental explants from the Mr 29,000 and 33,000 forms to the Mr 25,000 species [3].
• Placental prolactin-like protein A. Identification and characterization of two major glycoprotein species with antipeptide antibodies [3].
• Prolactin-like protein-A (PLP-A) was purified from medium conditioned by junctional zone explants dissected from the rat chorioallantoic placenta via concanavalin A affinity chromatography, sodium dodecyl sulfate-gel electrophoresis and two-dimensional gel electrophoresis [5].

Other interactions of Prl4a1

• Recombinant PLP-A lacked activity in standardized prolactin and growth hormone in vitro bioassays [2].
• The immunochemical analyses used antipeptide antisera directed to amino acids 56-70 of PL-II and amino acids 152-164 of PLP-A [7].

References