Preparation, purification, and determination of the biological activities of 12 N terminus-truncated recombinant analogues of bovine placental lactogen.

Gertler, Arieh; Hauser, Scott D.; Sakal, Edna; Vashdi, Dorit; Staten, Nicholas R.; Freeman, John J.; Krivi, Gwen G.

doi:10.1016/s0021-9258(18)42327-7

Cited by 41 publications

(2 citation statements)

References 26 publications

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“…It has been found experimentally that the deletion of the N-terminal tail of PL greatly reduces the activity of the ligand . From the crystal structure (Figure ), one can see that oPL is mainly associated with the D N -A domain and only the N-terminal end of placental lactogen binds to the D N -B domain.…”

Section: Discussionmentioning

confidence: 94%

“…It has been found experimentally that the deletion of the N-terminal tail of PL greatly reduces the activity of the ligand. 29 From the crystal structure (Figure 1), one can see that oPL is mainly associated with the D N -A domain and only the N-terminal end of placental lactogen binds to the D N -B domain. Thus, it is likely that it is the binding of the N-terminal tail to the D N -B domain that stabilizes the rotated (activated) form of the complex.…”

Section: Abbreviationsmentioning

confidence: 99%

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Activating the Prolactin Receptor: Effect of the Ligand on the Conformation of the Extracellular Domain

Groothuizen

Poger

Mark

2010

J. Chem. Theory Comput.

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The prolactin receptor resides on the surface of the cell as a preformed dimer. This suggests that cell signaling is triggered by conformational changes within the extracellular domain of the receptors. Here, by using atomistic molecular dynamics simulations, we show that the removal of the ligand placental lactogen from the dimeric form of the prolactin receptor results in a relative reorientation of the two extracellular domains by 20-30°, which corresponds to a clockwise rotation of the domains with respect to each other. Such a mechanism of activation for the prolactin receptor is similar to that proposed previously in the case of the growth hormone receptor. In addition to the effect of the removal of the ligand, the mechanical coupling between the extracellular and transmembrane domains within a model membrane was also examined.

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Section: Discussionmentioning

confidence: 94%

Section: Abbreviationsmentioning

confidence: 99%

Activating the Prolactin Receptor: Effect of the Ligand on the Conformation of the Extracellular Domain

Groothuizen

Poger

Mark

2010

J. Chem. Theory Comput.

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Temporospatial expression of placental lactogen and prolactin‐related protein‐1 genes in the bovine placenta and uterus during pregnancy

Patel

Kizaki

Todoroki

et al. 2004

Molecular Reproduction Devel

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The anatomical location of binucleate cells (BNC) influences protein expression but not steroid synthesis in ruminants. In order to determine if BNC in disparate locations differentially express bovine placental lactogen (bPL) and prolactin-related protein-1 (bPRP-1), we quantitated bPL and bPRP-1 transcripts in placentomal (cotyledonary, caruncular) and interplacentomal (intercotyledonary, intercaruncular) tissues throughout pregnancy in the bovine using real-time reverse transcription PCR (RT-PCR) and in situ hybridization. Levels of both bPL and bPRP-1 transcripts at peri-implantation were significantly higher (P < 0.01) in the fetal membrane than in caruncular and intercaruncular tissues. Thereafter, mRNA for these related proteins demonstrated different spatial as well as temporal patterns of expression. Levels of bPRP-1 transcripts peaked at day 60 of pregnancy. Between day 60 and 100, bPRP-1 transcripts fell by approximately sevenfold (P < 0.01) in cotyledonary and intercotyledonary tissues, and fourfold in caruncular (P < 0.01) tissue. Levels of bPRP-1 transcripts remained low in the cotyledonary, intercotyledonary, and caruncular tissues until peripartum. In contrast, bPL expression in placentomes increased with progression of gestation (P < 0.01), but decreased in interplacentomal tissue around peripartum. To conclude, disparate patterns of bPRP-1 and bPL genes are transcribed in the placentomal and interplacentomal tissues during gestation in the bovine, suggesting that these prolactin-like hormones serve distinct functions and are regulated differently in the uteroplacental unit in this species.

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Preparation of Recombinant Gilthead Seabream (Sparus aurata) Growth Hormone and Its Use for Stimulation of Larvae Growth by Oral Administration

Ben‐Atia

Fine

Tandler

et al. 1999

General and Comparative Endocrinology

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Preparation, purification, and determination of the biological activities of 12 N terminus-truncated recombinant analogues of bovine placental lactogen.

Cited by 41 publications

References 26 publications

Activating the Prolactin Receptor: Effect of the Ligand on the Conformation of the Extracellular Domain

Activating the Prolactin Receptor: Effect of the Ligand on the Conformation of the Extracellular Domain

Temporospatial expression of placental lactogen and prolactin‐related protein‐1 genes in the bovine placenta and uterus during pregnancy

Preparation of Recombinant Gilthead Seabream (Sparus aurata) Growth Hormone and Its Use for Stimulation of Larvae Growth by Oral Administration

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