Involvement of lysine residues in the binding of ovine prolactin and human growth hormone to lactogenic receptors

Chêne, N.; Martal, J.

doi:10.1016/0014-5793(85)80010-7

Cited by 10 publications

(3 citation statements)

References 18 publications

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“…Several studies, aimed at determining which region of PRL interacts with the receptor, have been reported. Sequence comparisons (Nicoll et al, 1986;Luck et al, 1989), chemical modifications (Doonen and Bewley, 1979;Andersen and Ebner, 1979;Necessary et al, 1985;de la Llosa et al, 1985; for review, see Nicoll et al, 1986) or mutational studies (Luck et al, 1989(Luck et al, , 1990(Luck et al, , 1991Goffin et al, 1992) characterized some structural features potentially involved in the biological properties of PRL but none of these data unequivocally localized the global PRL binding site.…”

mentioning

confidence: 99%

The addition of nine residues at the C‐terminus of human prolactin drastically alters its biological properties

Goffin

Struman

Goormaghtigh

et al. 1993

European Journal of Biochemistry

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We have added nine extra residues to the C-terminal of human prolactin and analysed the effect of this mutation on the ability of the hormone to bind to its lactogenic receptor and to induce Nb2 cell division. Both properties are markedly affected when compared to the natural 23-kDa human prolactin. Since no alteration of the global protein folding was detected either by circular dichroism or by infrared spectroscopy, the decrease in biological potency can be exclusively attributed to an effect of the nine additional residues on their near environment. From infrared analysis and secondary structure prediction, the elongated tail is assumed to be involved in a B-sheet with a few residues initially belonging to the fourth helix. Moreover, from the X-ray structures of porcine and human growth hormones, two proteins homologous to prolactins, the nine extra residues are likely to fold within a concave pocket delimited by helices 1 and 4, and the second half of the loop connecting helices 1 and 2 (loop 1). Thereby, we suggest that the additional residues prevent some residues belonging to this pocket from interacting with the lactogenic receptor. This is in perfect agreement with our earlier proposal that the binding site of prolactin to the lactogenic receptor is homologous to that of growth hormone to the somatogenic receptor, i.e. essentially composed of residues belonging to this concave pocket.

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mentioning

confidence: 99%

The addition of nine residues at the C‐terminus of human prolactin drastically alters its biological properties

Goffin

Struman

Goormaghtigh

et al. 1993

European Journal of Biochemistry

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“…The fact that the binding activity was not fully restored after 0-deacetylation indicates that there are also lysine residues involved in the hormone-receptor interaction, as was previously reported by De la Llosa et al (12). 0-Deacetylation ceptors.…”

Section: Resultsmentioning

confidence: 51%

Chemical modification of ovine prolactin with N‐acetylimidazole

Cymes

Iglesias

Wolfenstein‐Todel

1993

International Journal of Peptide and Protein Research

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Reaction of ovine prolactin (oPRL) with a 150-fold molar excess of N-acetylimidazole over protein content resulted in the modification of 2.5 tyrosine residues and 1.2 lysine residues. Acetylation greatly decreased the in vitro binding capacity to lactogenic sites. This binding capacity was partially restored by ammonium bicarbonate treatment, which removes 0-acetyl groups from tyrosine residues but not N-acetyl groups from lysine residues. The modification extent of the tyrosine residues was determined. The results suggest that acetylation of tyrosine 4 4 or of tyrosine 96 is likely to be responsible for the decrease in binding activity of acetylated oPRL, and that one of these residues may play a role in the interaction of oPRL with lactogenic receptors. 0 Munksgaard 1993.

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“…The chemical modifications of PRL and the receptor (with specificity towards histidine, lysine, tryptophan or tyrosine residues) resulted in a loss of receptor-and PRL-binding activity respectively De la Llosa et al, 1985;Mahajan & Ebner, 1986a,b). These amino acids play an important role in interacting through non-covalent bonds both intra-and inter-molecularly.…”

Section: Free Energy Enthalpy Entropy Of Prl-receptor Reactionmentioning

confidence: 99%

Thermodynamic analysis of the interaction of prolactin with its receptor in the rabbit mammary-gland microsomes

Sakai

Suzuki

Kohmoto

1990

Biochemical Journal

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The interaction of prolactin (PRL) with its membrane receptor depends markedly on temperature. Thermodynamic parameters for this reaction have been-evaluated from data for time-course kinetics and equilibrium binding at multiple temperatures between 19 and 31 'C. The free-energy change with temperature and the van't Hoff plot were found to be linear. These suggest that there are minimal structure changes at the PRL-receptor contact site over this temperature range. The positive signs of the entropy and enthalpy of reaction, and of the entropy of activation (AST) for association, indicate that the hydrophobic bonding is the most significant force involved in PRL-receptor formation. The AS-for dissociation was negative, and the enthalpy of activation for dissociation was about 20.3 kJ mol-' larger than that for association, indicating that the PRL-receptor complex is further stabilized by contributions of hydrogen bonds and van der Waals contacts after the initial interaction. The free energy of activation for dissociation, at 25 'C, was about 2.5-fold larger than that for association. This would cause slow dissociation of PRL from its receptor.

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Involvement of lysine residues in the binding of ovine prolactin and human growth hormone to lactogenic receptors

Cited by 10 publications

References 18 publications

The addition of nine residues at the C‐terminus of human prolactin drastically alters its biological properties

The addition of nine residues at the C‐terminus of human prolactin drastically alters its biological properties

Chemical modification of ovine prolactin with N‐acetylimidazole

Thermodynamic analysis of the interaction of prolactin with its receptor in the rabbit mammary-gland microsomes

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