Thyrotropin-Releasing Hormone Precursor: Characterization in Rat Brain

Ronald M. Lechan, W. U. Ping, Ivor M D Jackson, Hugh Wolf, Sharon Cooperman, Gail Mandel, Richard Goodman

Research output: Contribution to journalArticle

301 Citations (Scopus)

Abstract

To characterize the precursor of mammalian thyrotropin-releasing hormone (TRH), a rat hypothalamic λgtll library was screened with an antiserum directed against a synthetic peptide representing a portion of the rat TRH prohormone. The nucleotide sequence of the immunopositive complementary DNA encoded a protein with a molecular weight of 29,247. This protein contained five copies of the sequence Gln-His-Pro-Gly flanked by paired basic amino acids and could therefore generate five TRH molecules. In addition, potential cleavage sites in the TRH precursor could produce other non-TRH peptides, which may be secreted. In situ hybridization to rat brain sections demonstrated that the pre-proTRH complementary DNA detected neurons concentrated in the parvocellular division of the paraventricular nucleus, the same location as cells detected by immunohistochemistry. These findings indicate that mammalian TRH arises by posttranslational processing of a larger precursor protein. The ability of the TRH prohormone to generate multiple copies of the bioactive peptide may be an important mechanism in the amplification of hormone production.

Original languageEnglish (US)
Pages (from-to)159-161
Number of pages3
JournalScience
Volume231
Issue number4734
StatePublished - 1986
Externally publishedYes

Fingerprint

Thyrotropin-Releasing Hormone
Brain
Complementary DNA
Basic Amino Acids
Peptides
Protein Precursors
Peptide Hormones
Paraventricular Hypothalamic Nucleus
Libraries
In Situ Hybridization
Immune Sera
Proteins
Molecular Weight
Immunohistochemistry
Hormones
Neurons
pro-thyrotropin releasing hormone

ASJC Scopus subject areas

  • General

Cite this

Lechan, R. M., Ping, W. U., Jackson, I. M. D., Wolf, H., Cooperman, S., Mandel, G., & Goodman, R. (1986). Thyrotropin-Releasing Hormone Precursor: Characterization in Rat Brain. Science, 231(4734), 159-161.

Thyrotropin-Releasing Hormone Precursor : Characterization in Rat Brain. / Lechan, Ronald M.; Ping, W. U.; Jackson, Ivor M D; Wolf, Hugh; Cooperman, Sharon; Mandel, Gail; Goodman, Richard.

In: Science, Vol. 231, No. 4734, 1986, p. 159-161.

Research output: Contribution to journalArticle

Lechan, RM, Ping, WU, Jackson, IMD, Wolf, H, Cooperman, S, Mandel, G & Goodman, R 1986, 'Thyrotropin-Releasing Hormone Precursor: Characterization in Rat Brain', Science, vol. 231, no. 4734, pp. 159-161.
Lechan RM, Ping WU, Jackson IMD, Wolf H, Cooperman S, Mandel G et al. Thyrotropin-Releasing Hormone Precursor: Characterization in Rat Brain. Science. 1986;231(4734):159-161.
Lechan, Ronald M. ; Ping, W. U. ; Jackson, Ivor M D ; Wolf, Hugh ; Cooperman, Sharon ; Mandel, Gail ; Goodman, Richard. / Thyrotropin-Releasing Hormone Precursor : Characterization in Rat Brain. In: Science. 1986 ; Vol. 231, No. 4734. pp. 159-161.
@article{65c04bf3c56f4f84ad65f24b859626f8,
title = "Thyrotropin-Releasing Hormone Precursor: Characterization in Rat Brain",
abstract = "To characterize the precursor of mammalian thyrotropin-releasing hormone (TRH), a rat hypothalamic λgtll library was screened with an antiserum directed against a synthetic peptide representing a portion of the rat TRH prohormone. The nucleotide sequence of the immunopositive complementary DNA encoded a protein with a molecular weight of 29,247. This protein contained five copies of the sequence Gln-His-Pro-Gly flanked by paired basic amino acids and could therefore generate five TRH molecules. In addition, potential cleavage sites in the TRH precursor could produce other non-TRH peptides, which may be secreted. In situ hybridization to rat brain sections demonstrated that the pre-proTRH complementary DNA detected neurons concentrated in the parvocellular division of the paraventricular nucleus, the same location as cells detected by immunohistochemistry. These findings indicate that mammalian TRH arises by posttranslational processing of a larger precursor protein. The ability of the TRH prohormone to generate multiple copies of the bioactive peptide may be an important mechanism in the amplification of hormone production.",
author = "Lechan, {Ronald M.} and Ping, {W. U.} and Jackson, {Ivor M D} and Hugh Wolf and Sharon Cooperman and Gail Mandel and Richard Goodman",
year = "1986",
language = "English (US)",
volume = "231",
pages = "159--161",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "4734",

}

TY - JOUR

T1 - Thyrotropin-Releasing Hormone Precursor

T2 - Characterization in Rat Brain

AU - Lechan, Ronald M.

AU - Ping, W. U.

AU - Jackson, Ivor M D

AU - Wolf, Hugh

AU - Cooperman, Sharon

AU - Mandel, Gail

AU - Goodman, Richard

PY - 1986

Y1 - 1986

N2 - To characterize the precursor of mammalian thyrotropin-releasing hormone (TRH), a rat hypothalamic λgtll library was screened with an antiserum directed against a synthetic peptide representing a portion of the rat TRH prohormone. The nucleotide sequence of the immunopositive complementary DNA encoded a protein with a molecular weight of 29,247. This protein contained five copies of the sequence Gln-His-Pro-Gly flanked by paired basic amino acids and could therefore generate five TRH molecules. In addition, potential cleavage sites in the TRH precursor could produce other non-TRH peptides, which may be secreted. In situ hybridization to rat brain sections demonstrated that the pre-proTRH complementary DNA detected neurons concentrated in the parvocellular division of the paraventricular nucleus, the same location as cells detected by immunohistochemistry. These findings indicate that mammalian TRH arises by posttranslational processing of a larger precursor protein. The ability of the TRH prohormone to generate multiple copies of the bioactive peptide may be an important mechanism in the amplification of hormone production.

AB - To characterize the precursor of mammalian thyrotropin-releasing hormone (TRH), a rat hypothalamic λgtll library was screened with an antiserum directed against a synthetic peptide representing a portion of the rat TRH prohormone. The nucleotide sequence of the immunopositive complementary DNA encoded a protein with a molecular weight of 29,247. This protein contained five copies of the sequence Gln-His-Pro-Gly flanked by paired basic amino acids and could therefore generate five TRH molecules. In addition, potential cleavage sites in the TRH precursor could produce other non-TRH peptides, which may be secreted. In situ hybridization to rat brain sections demonstrated that the pre-proTRH complementary DNA detected neurons concentrated in the parvocellular division of the paraventricular nucleus, the same location as cells detected by immunohistochemistry. These findings indicate that mammalian TRH arises by posttranslational processing of a larger precursor protein. The ability of the TRH prohormone to generate multiple copies of the bioactive peptide may be an important mechanism in the amplification of hormone production.

UR - http://www.scopus.com/inward/record.url?scp=0022621305&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022621305&partnerID=8YFLogxK

M3 - Article

C2 - 3079917

AN - SCOPUS:0022621305

VL - 231

SP - 159

EP - 161

JO - Science

JF - Science

SN - 0036-8075

IS - 4734

ER -