Requirement of tyrosine residues 333 and 338 of the growth hormone (GH) receptor for selected GH-stimulated function

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Standard

Requirement of tyrosine residues 333 and 338 of the growth hormone (GH) receptor for selected GH-stimulated function. / Lobie, P E; Allevato, G; Norstedt, G; Billestrup, N; Nielsen, Jens Høiriis.

I: The Journal of Biological Chemistry, Bind 270, Nr. 37, 15.09.1995, s. 21745-50.

Publikation: Bidrag til tidsskriftTidsskriftartikelfagfællebedømt

Harvard

Lobie, PE, Allevato, G, Norstedt, G, Billestrup, N & Nielsen, JH 1995, 'Requirement of tyrosine residues 333 and 338 of the growth hormone (GH) receptor for selected GH-stimulated function', The Journal of Biological Chemistry, bind 270, nr. 37, s. 21745-50.

APA

Lobie, P. E., Allevato, G., Norstedt, G., Billestrup, N., & Nielsen, J. H. (1995). Requirement of tyrosine residues 333 and 338 of the growth hormone (GH) receptor for selected GH-stimulated function. The Journal of Biological Chemistry, 270(37), 21745-50.

Vancouver

Lobie PE, Allevato G, Norstedt G, Billestrup N, Nielsen JH. Requirement of tyrosine residues 333 and 338 of the growth hormone (GH) receptor for selected GH-stimulated function. The Journal of Biological Chemistry. 1995 sep. 15;270(37):21745-50.

Author

Lobie, P E ; Allevato, G ; Norstedt, G ; Billestrup, N ; Nielsen, Jens Høiriis. / Requirement of tyrosine residues 333 and 338 of the growth hormone (GH) receptor for selected GH-stimulated function. I: The Journal of Biological Chemistry. 1995 ; Bind 270, Nr. 37. s. 21745-50.

Bibtex

@article{729a38bb79ef49859fd85d01d536c2d0,
title = "Requirement of tyrosine residues 333 and 338 of the growth hormone (GH) receptor for selected GH-stimulated function",
abstract = "We have examined the involvement of tyrosine residues 333 and 338 of the growth hormone (GH) receptor in the cellular response to GH. Stable Chinese hamster ovary (CHO) cell clones expressing a receptor with tyrosine residues at position 333 and 338 of the receptor substituted for phenylalanine (CHO-GHR1-638 Y333F, Y338F) were generated by cDNA transfection. Compared with the wild type receptor the Y333F,Y338F mutant possessed normal high affinity ligand binding, hormone internalization, and ligand-induced receptor down-regulation. GH activation of mitogen-associated protein kinase was also similar in CHO clones expressing similar wild type and Y333F,Y338F receptor number. However, two GH-regulated cellular events (lipogenesis, and protein synthesis) were deficient in the tyrosine substituted receptor. In contrast, transcriptional regulation by GH (as evidenced by chloramphenicol acetyltransferase cDNA expression driven by the GH-responsive region of the SPI 2.1 gene) was not affected by Y333F,Y338F substitution. Thus we provide the first experimental evidence that specific tyrosine residues of the GH receptor are required for selected cellular responses to GH.",
keywords = "Amino Acid Sequence, Animals, CHO Cells, Calcium-Calmodulin-Dependent Protein Kinases, Chloramphenicol O-Acetyltransferase, Cricetinae, Down-Regulation, Growth Hormone, Humans, Kinetics, Leucine, Point Mutation, Protein Biosynthesis, Rats, Receptors, Somatotropin, Recombinant Proteins, Transfection, Tyrosine",
author = "Lobie, {P E} and G Allevato and G Norstedt and N Billestrup and Nielsen, {Jens H{\o}iriis}",
year = "1995",
month = sep,
day = "15",
language = "English",
volume = "270",
pages = "21745--50",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "37",

}

RIS

TY - JOUR

T1 - Requirement of tyrosine residues 333 and 338 of the growth hormone (GH) receptor for selected GH-stimulated function

AU - Lobie, P E

AU - Allevato, G

AU - Norstedt, G

AU - Billestrup, N

AU - Nielsen, Jens Høiriis

PY - 1995/9/15

Y1 - 1995/9/15

N2 - We have examined the involvement of tyrosine residues 333 and 338 of the growth hormone (GH) receptor in the cellular response to GH. Stable Chinese hamster ovary (CHO) cell clones expressing a receptor with tyrosine residues at position 333 and 338 of the receptor substituted for phenylalanine (CHO-GHR1-638 Y333F, Y338F) were generated by cDNA transfection. Compared with the wild type receptor the Y333F,Y338F mutant possessed normal high affinity ligand binding, hormone internalization, and ligand-induced receptor down-regulation. GH activation of mitogen-associated protein kinase was also similar in CHO clones expressing similar wild type and Y333F,Y338F receptor number. However, two GH-regulated cellular events (lipogenesis, and protein synthesis) were deficient in the tyrosine substituted receptor. In contrast, transcriptional regulation by GH (as evidenced by chloramphenicol acetyltransferase cDNA expression driven by the GH-responsive region of the SPI 2.1 gene) was not affected by Y333F,Y338F substitution. Thus we provide the first experimental evidence that specific tyrosine residues of the GH receptor are required for selected cellular responses to GH.

AB - We have examined the involvement of tyrosine residues 333 and 338 of the growth hormone (GH) receptor in the cellular response to GH. Stable Chinese hamster ovary (CHO) cell clones expressing a receptor with tyrosine residues at position 333 and 338 of the receptor substituted for phenylalanine (CHO-GHR1-638 Y333F, Y338F) were generated by cDNA transfection. Compared with the wild type receptor the Y333F,Y338F mutant possessed normal high affinity ligand binding, hormone internalization, and ligand-induced receptor down-regulation. GH activation of mitogen-associated protein kinase was also similar in CHO clones expressing similar wild type and Y333F,Y338F receptor number. However, two GH-regulated cellular events (lipogenesis, and protein synthesis) were deficient in the tyrosine substituted receptor. In contrast, transcriptional regulation by GH (as evidenced by chloramphenicol acetyltransferase cDNA expression driven by the GH-responsive region of the SPI 2.1 gene) was not affected by Y333F,Y338F substitution. Thus we provide the first experimental evidence that specific tyrosine residues of the GH receptor are required for selected cellular responses to GH.

KW - Amino Acid Sequence

KW - Animals

KW - CHO Cells

KW - Calcium-Calmodulin-Dependent Protein Kinases

KW - Chloramphenicol O-Acetyltransferase

KW - Cricetinae

KW - Down-Regulation

KW - Growth Hormone

KW - Humans

KW - Kinetics

KW - Leucine

KW - Point Mutation

KW - Protein Biosynthesis

KW - Rats

KW - Receptors, Somatotropin

KW - Recombinant Proteins

KW - Transfection

KW - Tyrosine

M3 - Journal article

C2 - 7665593

VL - 270

SP - 21745

EP - 21750

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 37

ER -

ID: 47973103