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Science 10 January 1986:
Vol. 231. no. 4734, pp. 159 - 161
DOI: 10.1126/science.3079917
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Articles

Science, Vol 231, Issue 4734, 159-161
Copyright © 1986 by American Association for the Advancement of Science

articles

Thyrotropin-releasing hormone precursor: characterization in rat brain

RM Lechan, P Wu, IM Jackson, H Wolf, S Cooperman, G Mandel, and RH Goodman

To characterize the precursor of mammalian thyrotropin-releasing hormone (TRH), a rat hypothalamic lambda gt11 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.


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