Serpin A1 and CD91 as host instruments against HIV-1 infection: Are extracellular antiviral peptides acting as intracellular messengers?

Congote, L.F.

doi:10.1016/j.virusres.2006.12.018

Cited by 27 publications

(27 citation statements)

References 149 publications

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“…8). Recently, the C-terminal of α1-antitrypsin was proposed to inhibit HIV-1 long-terminalrepeat-driven transcription by translocation to the nucleus and interacted with nuclear proteins (Congote, 2006(Congote, , 2007. Further investigations on how and when α1-antitrypsin activates common carp IGF-II gene are warranted.…”

Section: Discussionmentioning

confidence: 99%

Cloning, characterization and promoter analysis of the common carp IGF-II gene

Tse

Chan

Chen

2008

Gene

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Section: Discussionmentioning

confidence: 99%

Cloning, characterization and promoter analysis of the common carp IGF-II gene

Tse

Chan

Chen

2008

Gene

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“…33 AAT has also been shown to interfere with viral protein late processing, specifically through interference with gp120 formation and processing of p55(gal) to p24. 6 Serpins reduce HIV-induced inflammation through indirect mechanisms. Serpin C1 and AAT both interfere with NF-kb signal transduction.…”

Section: Serpins Role In Hiv Infection and Inflammationmentioning

confidence: 99%

“…Serpin A1 has been shown to inhibit directional neutrophil migration towards the site of infection. 64 6. Serpin A1 inhibits the dissociation of NF-jb from Ijb, preventing migration of NF-jb to the nucleus and subsequent initiation of transcription of the HIV genes, thereby slowing the reproductive ability of HIV-1 as well as numerous other microbial species.…”

Section: Serpins Role In Hiv Infection and Inflammationmentioning

confidence: 99%

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The Role of Serpin and Cystatin Antiproteases in Mucosal Innate Immunity and their Defense against HIV

Aboud

Ball

Tjernlund

et al. 2013

American J Rep Immunol

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Antiproteases play diverse roles in nature, from regulating protease activity to innate defense against microorganisms. Recently, antiproteases have been shown to play important roles in HIV pathogenesis including, inhibiting HIV binding and replication and reducing activation and inflammation of susceptible cells. They have also been implicated as one of the initial host responders, in plasma, to control replication of HIV. More recently, antiproteases expressed at the mucosal surface have been linked to reduced susceptibility to HIV infection in HIV-exposed sero-negative individuals. These factors are expressed in the epithelial layer of the female genital tract, thus at the frontline of defense against mucosal infection. This review focuses on the specific antimicrobial roles of antiproteases, focusing on serpins and cystatins, with an emphasis on their known and potential roles in HIV infection. Their potential as therapeutic interventions to combat HIV is also discussed.

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“…3). This unusual fate of an extracellular ligand is not uncommon (Congote, 2007). A very fast (3 min) internalization and nuclear localization of extracellular peptides has been demonstrated with peptide analogues of serpin A1 (Rhee and Davis, 2006).…”

Section: Discussionmentioning

confidence: 92%

Regulator of differentiation 1 (ROD1) binds to the amphipathic C‐terminal peptide of thrombospondin‐4 and is involved in its mitogenic activity

Sadvakassova

Dobocan

DiFalco

et al. 2009

Journal Cellular Physiology

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The matrix protein thrombospondin-4 has an acidic amphipathic C-terminal peptide (C21) which stimulates erythroid cell proliferation. Here we show that C21 stimulates red cell formation in anemic mice in vivo. In vitro experiments indicated that the peptide-mediated increase of erythroid colony formation in cultures of human CD34+ hematopoietic progenitor cells was possible only under continuous presence of erythropoietin. In the absence of this cytokine, C21 stimulated exclusively myeloid colony formation. Therefore, the peptide is not a specific erythroid differentiation factor. In fact, it is mitogenic in non-erythroid cells, such as skin fibroblasts and kidney epithelial cells. In erythroleukemic TF-1 cells, it actually decreased the production of the erythroid differentiation marker glycophorin A. C21-affinity chromatography revealed regulator of differentiation 1 (ROD1) as a major C21-binding protein. ROD1 is the hematopoietic cell paralog of polypyrimidine tract binding proteins (PTBs), RNA splice regulators which regulate differentiation by repressing tissue-specific exons. ROD1 binding to C21 was strongly inhibited by synthetic RNAs in the order poly A > poly U > poly G = poly C and was weakly inhibited by a synthetic phosphorylated peptide mimicking the C-terminal domain of RNA polymerase II. Cellular overexpression or knockdown experiments of ROD1 suggest a role for this protein in the mitogenic activity of C21. Since the nuclear proteins ROD1 and PTBs regulate differentiation at a posttranscriptional level and there is a fast nuclear uptake of C21, we put forward the idea that the peptide is internalized, goes to the nucleus and maintains cells in a proliferative state by supporting ROD1-mediated inhibition of differentiation.

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Serpin A1 and CD91 as host instruments against HIV-1 infection: Are extracellular antiviral peptides acting as intracellular messengers?

Cited by 27 publications

References 149 publications

Cloning, characterization and promoter analysis of the common carp IGF-II gene

Cloning, characterization and promoter analysis of the common carp IGF-II gene

The Role of Serpin and Cystatin Antiproteases in Mucosal Innate Immunity and their Defense against HIV

Regulator of differentiation 1 (ROD1) binds to the amphipathic C‐terminal peptide of thrombospondin‐4 and is involved in its mitogenic activity

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