A highly conserved, 5′ untranslated, inverted repeat sequence is ineffective in translational control of the α1(I) collagen gene

Börnstein, Paul; McKay, John; Devarayalu, Sreelekha; Cook, Susan C.

doi:10.1093/nar/16.23.11398-a

Cited by 5 publications

(5 citation statements)

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“…Interestingly, this sequence is also found in the ␣ 2 (I) and ␣ 1 (III) collagen transcripts. However, other investigators, using a somewhat different experimental approach, examined this region and did not find regulatory activity (5). We found that PI3K inhibition decreased the levels of a transfected collagen minigene containing the 5Јstem-loop structure and the 3Ј-UTR.…”

Section: Discussionmentioning

confidence: 61%

Phosphatidylinositol 3-kinase-dependent stabilization of α₁(I) collagen mRNA in human lung fibroblasts

Ricupero

Poliks

Rishikof

et al. 2001

American Journal of Physiology-Cell Physiology

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We investigated the role of phosphatidylinositol 3-kinase (PI3K) in the expression of alpha1(I) collagen mRNA. We report that the basal level of alpha1(I) collagen mRNA was reduced when PI3K activity was inhibited by either LY-294002 or wortmannin. These PI3K inhibitors also blocked increases of alpha1(I) collagen mRNA levels after the addition of transforming growth factor-beta. The effect of PI3K inhibition was abolished by the removal of the inhibitor or by the addition of cycloheximide. Inhibition of PI3K activity decreased the stability of the alpha1(I) collagen mRNA with no change in the rate of transcription of the alpha1(I) collagen gene as assessed by Northern blotting with actinomycin D-treated fibroblasts and nuclear run-on assays. Expression of a truncated alpha1(I) collagen minigene driven by a cytomegalovirus promoter in murine fibroblasts was decreased by LY-294002 treatment. These data indicate that PI3K activation results in increased stabilization of alpha1(I) collagen mRNA. In vivo, the PI3K activity in fibroblasts may regulate basal levels of alpha1(I) collagen mRNA expression.

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Section: Discussionmentioning

confidence: 61%

Phosphatidylinositol 3-kinase-dependent stabilization of α₁(I) collagen mRNA in human lung fibroblasts

Ricupero

Poliks

Rishikof

et al. 2001

American Journal of Physiology-Cell Physiology

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“…However, utilization of a second, downstream AUG codon as start site for translation has been reported previously, and can account for up to 5% of the protein produced (Edwards et al, 1986;Peterson and Piatigorsky, 1986;Strubin et al, 1986); discussed in Kozak (1987) and Herman (1989). It has also been shown that the length of the 5'-untranslated region can influence the efficiency of translation (Kozak, 1988), and that secondary structure present in the leader region can influence the choice of start codons when more than one is present (Cough et al, 1985;Bornstein et al, 1988;Kozak, 1988;Parkin et al, 1988;van Duijn et al, 1988). Analysis of the mouse and human genomic sequences located immediately upstream of the CNS start site suggests that possible strong secondary structures (i.e., hairpin loops) could form in a longer, PNStype mRNA.…”

Section: Rat Astrocyte G F a P Rat S C H W A N N C E L L G F A Pmentioning

confidence: 82%

Isolation of cDNA clones encoding rat glial fibrillary acidic protein: Expression in astrocytes and in Schwann cells

Feinstein

Weinmaster

Milner

1992

J of Neuroscience Research

122

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Glial fibrillary acidic protein (GFAP) expressed by astrocytes in the central nervous system (CNS) has been extensively characterized but the molecular identity of related molecules in the peripheral nervous system (PNS) remains unclear. To examine possible structural differences between CNS and PNS GFAP, we have isolated cDNA clones for rat GFAP from both cultured astrocyte and Schwann cell libraries. Nucleotide sequence analysis indicated that the PNS and CNS GFAP clones contained identical coding regions, with a predicted protein product of 430 amino acids. However, the 5'-untranslated region of clone rGFA15, isolated from the Schwann cell library, was longer than that predicted for brain-derived GFAP mRNA. Primer extension analysis of RNA isolated from the RT4-D6 Schwann cell line indicated that the start site for PNS GFAP mRNA lies 169 bases upstream from that used in the CNS. In addition, tryptic peptide mapping of GFAP prepared from cultured astrocytes and Schwann cells revealed one major peptide fragment present in CNS GFAP but absent from PNS GFAP. These results suggest structural differences between GFAP in these two cell types, at both the nucleic acid and protein level, and are consistent with previous observations of immunochemical differences existing between CNS and PNS GFAP.

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“…A slightly different SL structure is also found around the translation start codon of the sea urchin collagen gene (14). A previous report did not demonstrate a regulatory role for this structure in mRNA steady-state levels or translation based on transfections of hybrid collagen-human growth hormone genes into fibroblasts and measurement of human growth hormone protein in cell medium (6).…”

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confidence: 77%

Regulatory Role of the Conserved Stem-Loop Structure at the 5′ End of Collagen α1(I) mRNA

Stefanovic

Hellerbrand

Brenner

1999

Molecular and Cellular Biology

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Three fibrillar collagen mRNAs, alpha1(I), alpha2(I), and alpha1(III), are coordinately upregulated in the activated hepatic stellate cell (hsc) in liver fibrosis. These three mRNAs contain sequences surrounding the start codon that can be folded into a stem-loop structure. We investigated the role of this stem-loop structure in expression of collagen alpha1(I) reporter mRNAs in hsc's and fibroblasts. The stem-loop dramatically decreases accumulation of mRNAs in quiescent hsc's and to a lesser extent in activated hsc's and fibroblasts. The stem-loop decreases mRNA stability in fibroblasts. In activated hsc's and fibroblasts, a protein complex binds to the stem-loop, and this binding requires the presence of a 7mG cap on the RNA. Placing the 3' untranslated region (UTR) of collagen alpha1(I) mRNA in a reporter mRNA containing this stem-loop further increases the steady-state level in activated hsc's. This 3' UTR binds alphaCP, a protein implicated in increasing stability of collagen alpha1(I) mRNA in activated hsc's (B. Stefanovic, C. Hellerbrand, M. Holcik, M. Briendl, S. A. Liebhaber, and D. A. Brenner, Mol. Cell. Biol. 17:5201-5209, 1997). A set of protein complexes assembles on the 7mG capped stem-loop RNA, and a 120-kDa protein is specifically cross-linked to this structure. Thus, collagen alpha1(I) mRNA is regulated by a complex interaction between the 5' stem-loop and the 3' UTR, which may optimize collagen production in activated hsc's.

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A highly conserved, 5′ untranslated, inverted repeat sequence is ineffective in translational control of the α1(I) collagen gene

Cited by 5 publications

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Phosphatidylinositol 3-kinase-dependent stabilization of α₁(I) collagen mRNA in human lung fibroblasts

Phosphatidylinositol 3-kinase-dependent stabilization of α₁(I) collagen mRNA in human lung fibroblasts

Isolation of cDNA clones encoding rat glial fibrillary acidic protein: Expression in astrocytes and in Schwann cells

Regulatory Role of the Conserved Stem-Loop Structure at the 5′ End of Collagen α1(I) mRNA

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A highly conserved, 5′ untranslated, inverted repeat sequence is ineffective in translational control of the α1(I) collagen gene

Cited by 5 publications

References 0 publications

Phosphatidylinositol 3-kinase-dependent stabilization of α1(I) collagen mRNA in human lung fibroblasts

Phosphatidylinositol 3-kinase-dependent stabilization of α1(I) collagen mRNA in human lung fibroblasts

Isolation of cDNA clones encoding rat glial fibrillary acidic protein: Expression in astrocytes and in Schwann cells

Regulatory Role of the Conserved Stem-Loop Structure at the 5′ End of Collagen α1(I) mRNA

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Phosphatidylinositol 3-kinase-dependent stabilization of α₁(I) collagen mRNA in human lung fibroblasts

Phosphatidylinositol 3-kinase-dependent stabilization of α₁(I) collagen mRNA in human lung fibroblasts