Diminished matrix metalloproteinase 9 secretion in human immunodeficiency virus-infected mononuclear phagocytes: modulation of innate immunity and implications for neurological disease

Ciborowski, Paweł; Enose, Yoshimi; Mack, Andrea; Fladseth, Melissa; Gendelman, Howard Eliot

doi:10.1016/j.jneuroim.2004.08.033

Cited by 34 publications

(43 citation statements)

References 19 publications

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“…We have also previously reported a decrease in total protein synthesis concomitant with degradation of cellular mRNA (1). More recently, protein expression profiling by gel electro-phoresis coupled to MS has revealed the differential expression of cellular proteins associated with HIV-1 infection in monocyte-derived macrophages (18) as well as with the expression of HIV-1 Tat in human T cells (20) and astrocytes (71).…”

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confidence: 86%

“…16 O/ 18 O labeling and quantitative LC-FTICR analyses. Trypsin-catalyzed 16 O/ 18 O labeling was carried out as previously described (75) by incubating the tryptic peptides in either 18 O-enriched water (95%; ISOTEC) for HIV-infected samples or regular 16 O water for mock-infected samples with immobilized trypsin (Applied Biosystems) as a catalyst for oxygen exchange at the tryptic C termini.…”

mentioning

confidence: 99%

“…Trypsin-catalyzed 16 O/ 18 O labeling was carried out as previously described (75) by incubating the tryptic peptides in either 18 O-enriched water (95%; ISOTEC) for HIV-infected samples or regular 16 O water for mock-infected samples with immobilized trypsin (Applied Biosystems) as a catalyst for oxygen exchange at the tryptic C termini. The 16 O/ 18 O-labeled samples were mixed with equal amounts of mock-and HIV-1-infected samples, and the mixed sample was further fractionated into Cys and non-Cys peptides as described above. The Cys and non-Cys peptide samples were then analyzed using a custom-built capillary LC system coupled online, using an in-house-manufactured electrospray ionization interface, to an 11.5 T Fourier transform ion cyclotron resonance (FTICR) mass spectrometer.…”

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confidence: 99%

“…Peptide identities were assigned by matching the normalized elution time and accurate mass measurements to the AMT tag database within a 5-ppm mass error and a 2% NET error. For the assessment of labeling efficiency by the 16 O and 18 O isotopes, identical aliquots of cell lysates were labeled with either isotope. Peptides were then quantified based on 16 O-to- 18 O ratios, and deviations from the expected ratio of 1:1 were determined to exceed no more than 1.19-fold (Table 1).…”

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confidence: 99%

“…For the assessment of labeling efficiency by the 16 O and 18 O isotopes, identical aliquots of cell lysates were labeled with either isotope. Peptides were then quantified based on 16 O-to- 18 O ratios, and deviations from the expected ratio of 1:1 were determined to exceed no more than 1.19-fold (Table 1). All quantified peptides were rolled up to nonredundant protein groups by using ProteinProphet (60), and the abundance ratio for each protein group was calculated by averaging the ratio of multiple unique peptides stemming from the same protein group.…”

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confidence: 99%

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Quantitative Analysis of Human Immunodeficiency Virus Type 1-Infected CD4⁺Cell Proteome: Dysregulated Cell Cycle Progression and Nuclear Transport Coincide with Robust Virus Production

Chan¹,

Qian

Diamond³

et al. 2007

J Virol

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Relatively little is known at the functional genomic level about the global host response to human immunodeficiency virus type 1 (HIV-1) infection. Microarray analyses by several laboratories, including our own, have revealed that HIV-1 infection causes significant changes in host mRNA abundance and regulation of several cellular biological pathways. However, it remains unclear what consequences these changes bring about at the protein level. Here we report the expression levels of ϳ3,200 proteins in the CD4 ؉ CEMx174 cell line after infection with the LAI strain of human immunodeficiency virus type 1 (HIV-1); the proteins were assessed using liquid chromatography-mass spectrometry coupled with stable isotope labeling and the accurate mass and time tag approach. Furthermore, we found that 687 (21%) proteins changed in abundance at the peak of virus production at 36 h postinfection. Pathway analysis revealed that the differential expression of proteins was concentrated in select biological pathways, exemplified by ubiquitin-conjugating enzymes in ubiquitination, carrier proteins in nucleocytoplasmic transport, cyclin-dependent kinase in cell cycle progression, and pyruvate dehydrogenase of the citrate cycle pathways. Moreover, we observed changes in the abundance of proteins with known interactions with HIV-1 viral proteins. Our proteomic analysis captured changes in the host protein milieu at the time of robust virus production, depicting changes in cellular processes that may contribute to virus replication. Continuing analyses are expected to focus on blocking virus replication by targeting these pathways and their effector proteins.

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confidence: 86%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Quantitative Analysis of Human Immunodeficiency Virus Type 1-Infected CD4⁺Cell Proteome: Dysregulated Cell Cycle Progression and Nuclear Transport Coincide with Robust Virus Production

Chan¹,

Qian

Diamond³

et al. 2007

J Virol

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Sera proteomic biomarker profiling in HIV‐1 infected subjects with cognitive impairment

Rozek¹,

Horning²,

Anderson³

et al. 2008

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HIV-1 infection of the brain commonly leads to cognitive impairments (CI). In its most severe form, HIV-associated dementia is associated with advanced immune suppression and debilitating loss of memory, behavioral, and motor functions. Despite significant research activities, diagnosis remains one of exclusion. Bioimaging, neuropsychological testing, and viral and immune biomarkers serve to support but not define a diagnosis of HIV-1 associated CI. This is timely and required as brain injury triggered by HIV-1 can be controlled, in part, by antiretroviral medicines. The recent development of proteomics has opened new ways to study viral-host interactions which may provide new insight into treatment and disease monitoring. To this end we developed a proteomics platform for HIV-1 associated CI biomarker discovery was used it to perform a pilot study for sera-associated HIV-1 associated dementia (HAD) proteins. A 2-dimensional electrophoresis (2-DE) map of a serum proteome was focused on differentially expressed proteins. Differential expression of 2 proteins was validated by Western blot tests identifying afamin and ceruloplasmin as potential biomarkers for CI associated with advanced HIV-1 infection.

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Macrophage secretome from women with HIV‐associated neurocognitive disorders

Colón

Pérez-Laspiur

Quiles

et al. 2015

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Purpose Thirty to fifty per cent of HIV patients develop HIV associated neurocognitive disorders (HAND) despite combined antiretroviral therapy. HIV-1 infected macrophages release viral and cellular proteins that induce neuronal degeneration and death. We hypothesize that changes in the macrophage secretome of HIV-1 seropositive patients with HAND may dissect proteins related to neurotoxicity. Experimental Design Monocyte-derived macrophages (MDM) were isolated from the peripheral blood of 12 HIV+ and 4 HIV− women characterized for neurocognitive function. Serum-free MDM supernatants were collected for protein isolation and quantification with iTRAQ® labeling. Protein identification was performed using a LTQ Orbitrap Velos mass spectrometer and validated in MDM supernatants and in plasma using ELISA. Results Three proteins were different between NC and ANI, 6 between NC and HAD, and 6 between NC and HAD. Among these, S100A9 was decreased in plasma from patients with ANI, and MMP9 was decreased in the plasma of all HIV+ patients regardless of cognitive status, and was significantly reduced in supernatant of MDM isolated from patients with ANI. Conclusions and clinical relevance S100A9 and MMP9 have been associated with inflammation and cognitive impairment, and therefore represent potential targets for HAND treatment.

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Diminished matrix metalloproteinase 9 secretion in human immunodeficiency virus-infected mononuclear phagocytes: modulation of innate immunity and implications for neurological disease

Cited by 34 publications

References 19 publications

Quantitative Analysis of Human Immunodeficiency Virus Type 1-Infected CD4⁺Cell Proteome: Dysregulated Cell Cycle Progression and Nuclear Transport Coincide with Robust Virus Production

Quantitative Analysis of Human Immunodeficiency Virus Type 1-Infected CD4⁺Cell Proteome: Dysregulated Cell Cycle Progression and Nuclear Transport Coincide with Robust Virus Production

Sera proteomic biomarker profiling in HIV‐1 infected subjects with cognitive impairment

Macrophage secretome from women with HIV‐associated neurocognitive disorders

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Diminished matrix metalloproteinase 9 secretion in human immunodeficiency virus-infected mononuclear phagocytes: modulation of innate immunity and implications for neurological disease

Cited by 34 publications

References 19 publications

Quantitative Analysis of Human Immunodeficiency Virus Type 1-Infected CD4+Cell Proteome: Dysregulated Cell Cycle Progression and Nuclear Transport Coincide with Robust Virus Production

Quantitative Analysis of Human Immunodeficiency Virus Type 1-Infected CD4+Cell Proteome: Dysregulated Cell Cycle Progression and Nuclear Transport Coincide with Robust Virus Production

Sera proteomic biomarker profiling in HIV‐1 infected subjects with cognitive impairment

Macrophage secretome from women with HIV‐associated neurocognitive disorders

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Product

Resources

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Quantitative Analysis of Human Immunodeficiency Virus Type 1-Infected CD4⁺Cell Proteome: Dysregulated Cell Cycle Progression and Nuclear Transport Coincide with Robust Virus Production

Quantitative Analysis of Human Immunodeficiency Virus Type 1-Infected CD4⁺Cell Proteome: Dysregulated Cell Cycle Progression and Nuclear Transport Coincide with Robust Virus Production