HIV infection is associated with reduced serum alpha-1-antitrypsin concentrations

Bryan, Courtney; Beard, K. Scott; Pott, Gregory B.; Rahkola, Jeremy; Gardner, Edward M.; Janoff, Edward N.; Shapiro, Leland

doi:10.25011/cim.v33i6.14589

Cited by 35 publications

(37 citation statements)

References 16 publications

(20 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Low a 1 -antitrypsin levels have been associated with HIV infection and elevated plasma sCD14 levels. 41,42 To assess emphysema severity, we used a validated, semiquantitative approach. 5,7,43 Consistent with other studies, CT scans were scored by a single radiologist.…”

Section: Discussionmentioning

confidence: 99%

Increased Risk of Radiographic Emphysema in HIV Is Associated With Elevated Soluble CD14 and Nadir CD4

Attia

Akgün

Wongtrakool

et al. 2014

Chest

120

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Increased Risk of Radiographic Emphysema in HIV Is Associated With Elevated Soluble CD14 and Nadir CD4

Attia

Akgün

Wongtrakool

et al. 2014

Chest

120

View full text Add to dashboard Cite

“…Subsequently, a screening study of ultra-filtered human plasma and protein sequencing revealed that, indeed, the major plasma-derived inhibitor of HIV-1 is circulating human AAT (51). Accordingly, it was later demonstrated that HIV-1 infection is associated with reduced serum AAT concentrations (52). A C-terminal 26-residue peptide fragment of AAT, the result of internalized and cleaved AAT, was found to be a direct inhibitor of viral infection (53).…”

Section: Binding Targets That Are Unrelated To Protease Inhibitionmentioning

confidence: 99%

Expanding the Clinical Indications for α1-Antitrypsin Therapy

Lewis

2012

Mol Med

146

115

View full text Add to dashboard Cite

α 1 -Antitrypsin (AAT) is a 52-kDa circulating serine protease inhibitor. Production of AAT by the liver maintains 0.9-1.75 mg/mL circulating levels. During acute-phase responses, circulating AAT levels increase more than fourfold. In individuals with one of several inherited mutations in AAT, low circulating levels increase the risk for lung, liver and pancreatic destructive diseases, particularly emphysema. These individuals are treated with lifelong weekly infusions of human plasma-derived AAT. An increasing amount of evidence appears to suggest that AAT possesses not only the ability to inhibit serine proteases, such as elastase and proteinase-3 (PR-3), but also to exert antiinflammatory and tissue-protective effects independent of protease inhibition. AAT modifies dendritic cell maturation and promotes T regulatory cell differentiation, induces interleukin (IL)-1 receptor antagonist and IL-10 release, protects various cell types from cell death, inhibits caspases-1 and -3 activity and inhibits IL-1 production and activity. Importantly, unlike classic immunosuppressants, AAT allows undeterred isolated T-lymphocyte responses. On the basis of preclinical and clinical studies, AAT therapy for nondeficient individuals may interfere with disease progression in type 1 and type 2 diabetes, acute myocardial infarction, rheumatoid arthritis, inflammatory bowel disease, cystic fibrosis, transplant rejection, graft versus host disease and multiple sclerosis. AAT also appears to be antibacterial and an inhibitor of viral infections, such as influenza and human immunodeficiency virus (HIV), and is currently evaluated in clinical trials for type 1 diabetes, cystic fibrosis and graft versus host disease. Thus, AAT therapy appears to have advanced from replacement therapy, to a safe and potential treatment for a broad spectrum of inflammatory and immune-mediated diseases.

show abstract

“…It may play a role as an endogenous HIV suppressor. The diminished circulating alpha-1-antitrypsin concentration observed in HIV infection is consistent with a role as an endogenous HIV suppressor (Bryan et al 2010).…”

Section: Trypsin Inhibitorsmentioning

confidence: 54%

Proteins, peptides, polysaccharides, and nucleotides with inhibitory activity on human immunodeficiency virus and its enzymes

Cheung

Wong

et al. 2015

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Human immunodeficiency virus (HIV), the causative agent of acquired immune deficiency syndrome, has claimed innumerable lives in the past. Many biomolecules which suppress HIV replication and also other biomolecules that inhibit enzymes essential to HIV replication have been reported. Proteins including a variety of milk proteins, ribosome-inactivating proteins, ribonucleases, antifungal proteins, and trypsin inhibitors; peptides comprising cathelicidins, defensins, synthetic peptides, and others; polysaccharides and polysaccharopeptides; nucleosides, nucleotides, and ribozymes, demonstrated anti-HIV activity. In many cases, the mechanism of anti-HIV action has been elucidated. Strategies have been devised to augment the anti-HIV potency of these compounds.

show abstract

HIV infection is associated with reduced serum alpha-1-antitrypsin concentrations

Cited by 35 publications

References 16 publications

Increased Risk of Radiographic Emphysema in HIV Is Associated With Elevated Soluble CD14 and Nadir CD4

Increased Risk of Radiographic Emphysema in HIV Is Associated With Elevated Soluble CD14 and Nadir CD4

Expanding the Clinical Indications for α1-Antitrypsin Therapy

Proteins, peptides, polysaccharides, and nucleotides with inhibitory activity on human immunodeficiency virus and its enzymes

Contact Info

Product

Resources

About