Corso, Carmela (2010) Identificazione di proteine con attività di legame agli mRNA degli antigeni MHC di classe II. [Tesi di dottorato] (Unpublished)

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Item Type: Tesi di dottorato
Resource language: Italiano
Title: Identificazione di proteine con attività di legame agli mRNA degli antigeni MHC di classe II
Creators:
Creators
Email
Corso, Carmela
carmelacorso@libero.it
Date: 28 November 2010
Number of Pages: 83
Institution: Università degli Studi di Napoli Federico II
Department: Biologia strutturale e funzionale
Scuola di dottorato: Scienze biologiche
Dottorato: Biologia applicata
Ciclo di dottorato: 23
Coordinatore del Corso di dottorato:
nome
email
Ricca, Ezio
ezio.ricca@unina.it
Tutor:
nome
email
Abrescia, Paolo
paolo.abrescia@unina.it
Date: 28 November 2010
Number of Pages: 83
Keywords: MHC di classe II; regolazione post-trascrizionale; RNA binding proteins; RNA operone
Settori scientifico-disciplinari del MIUR: Area 05 - Scienze biologiche > BIO/09 - Fisiologia
Date Deposited: 02 Dec 2010 10:46
Last Modified: 30 Apr 2014 19:44
URI: http://www.fedoa.unina.it/id/eprint/8039
DOI: 10.6092/UNINA/FEDOA/8039

Collection description

Major Histocompatibility Complex class II mRNAs encode heterodimeric proteins involved in the presentation of exogenous antigens during immune response. Their 3'UTRs bind a protein complex in which we identified two factors: EBP1, an Erb3 receptor-binding protein, and DRBP76, a double-stranded RNA-binding Nuclear Protein, also known as Nuclear Factor 90. Both are well characterized regulatory factors of several mRNA molecules processing. Using either EBP1 or DRBP76/NF90 specific knockdown experiments, we established that the two proteins play a role in regulating the expression of HLA-DRA, HLA-DRB1 and HLA-DQA1 mRNAs levels. Our study represents the first indication of the existence of a functional unit that includes different transcripts involved in the adaptive immune response. We propose that the concept of “RNA operon” may be suitable for our system in which MHCII mRNAs are modulated via interaction of their 3’UTR with same proteins.

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