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Three distinct human thymopoietins are derived from alternatively spliced mRNAs.

Thymopoietin (TP) was originally isolated as a 5-kDa 49-aa protein from bovine thymus in studies of the effects of thymic extracts on neuromuscular transmission and was subsequently observed to affect T-cell differentiation and function. We now report the isolation of cDNA clones for three alternati...

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Main Authors: Harris, C A, Andryuk, P J, Cline, S, Chan, H K, Natarajan, A, Siekierka, J J, Goldstein, G
Formato: Artigo
Idioma:en
Publicado em: 1994
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC44185/
https://ncbi.nlm.nih.gov/pubmed/7517549
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spelling pubmed-441852001-08-25 Three distinct human thymopoietins are derived from alternatively spliced mRNAs. Harris, C A Andryuk, P J Cline, S Chan, H K Natarajan, A Siekierka, J J Goldstein, G Proc Natl Acad Sci U S A Research Article Thymopoietin (TP) was originally isolated as a 5-kDa 49-aa protein from bovine thymus in studies of the effects of thymic extracts on neuromuscular transmission and was subsequently observed to affect T-cell differentiation and function. We now report the isolation of cDNA clones for three alternatively spliced mRNAs that encode three distinct human T-cell TPs. Proteins encoded by these mRNAs, which we have named TP alpha (75 kDa), TP beta (51 kDa), and TP gamma (39 kDa), contain identical N-terminal regions, including sequences nearly identical to that of the originally isolated 49-aa protein, but divergent C-terminal regions. TP mRNAs are expressed in many tissues, most abundantly in adult thymus and fetal liver of the tissues so far examined. Distinct structural domains and functional motifs in TPs alpha, beta, and gamma suggest that the proteins have unique functions and may be directed to distinct subcellular compartments. 1994-07-05 /pmc/articles/PMC44185/ /pubmed/7517549 Text en
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Research Article
spellingShingle Research Article
Harris, C A
Andryuk, P J
Cline, S
Chan, H K
Natarajan, A
Siekierka, J J
Goldstein, G
Three distinct human thymopoietins are derived from alternatively spliced mRNAs.
description Thymopoietin (TP) was originally isolated as a 5-kDa 49-aa protein from bovine thymus in studies of the effects of thymic extracts on neuromuscular transmission and was subsequently observed to affect T-cell differentiation and function. We now report the isolation of cDNA clones for three alternatively spliced mRNAs that encode three distinct human T-cell TPs. Proteins encoded by these mRNAs, which we have named TP alpha (75 kDa), TP beta (51 kDa), and TP gamma (39 kDa), contain identical N-terminal regions, including sequences nearly identical to that of the originally isolated 49-aa protein, but divergent C-terminal regions. TP mRNAs are expressed in many tissues, most abundantly in adult thymus and fetal liver of the tissues so far examined. Distinct structural domains and functional motifs in TPs alpha, beta, and gamma suggest that the proteins have unique functions and may be directed to distinct subcellular compartments.
author Harris, C A
Andryuk, P J
Cline, S
Chan, H K
Natarajan, A
Siekierka, J J
Goldstein, G
author_facet Harris, C A
Andryuk, P J
Cline, S
Chan, H K
Natarajan, A
Siekierka, J J
Goldstein, G
author_sort Harris, C A
title Three distinct human thymopoietins are derived from alternatively spliced mRNAs.
title_short Three distinct human thymopoietins are derived from alternatively spliced mRNAs.
title_full Three distinct human thymopoietins are derived from alternatively spliced mRNAs.
title_fullStr Three distinct human thymopoietins are derived from alternatively spliced mRNAs.
title_full_unstemmed Three distinct human thymopoietins are derived from alternatively spliced mRNAs.
title_sort three distinct human thymopoietins are derived from alternatively spliced mrnas.
publishDate 1994
url https://ncbi.nlm.nih.gov/pmc/articles/PMC44185/
https://ncbi.nlm.nih.gov/pubmed/7517549
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