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Article: Clinical Proteomics: From Biological Sample to Clinical Exploitation.

Lasonder, Edwin

2017 Volume 5, Issue 2

Abstract: n/a. ...

Abstract	n/a.
Language	English
Publishing date	2017-04-06
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2720995-7
ISSN	2227-7382
ISSN	2227-7382
DOI	10.3390/proteomes5020010
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Article ; Online: Plasmodium berghei LAPs form an extended protein complex that facilitates crystalloid targeting and biogenesis.

Tremp, Annie Z / Saeed, Sadia / Sharma, Vikram / Lasonder, Edwin / Dessens, Johannes T

Journal of proteomics

2020 Volume 227, Page(s) 103925

Abstract: Passage of malaria parasites through mosquitoes involves multiple developmental transitions, from gametocytes that are ingested with the blood meal, through to sporozoites that are transmitted by insect bite to the host. During the transformation from ... ...

Abstract	Passage of malaria parasites through mosquitoes involves multiple developmental transitions, from gametocytes that are ingested with the blood meal, through to sporozoites that are transmitted by insect bite to the host. During the transformation from gametocyte to oocyst, the parasite forms a unique transient organelle named the crystalloid, which is involved in sporozoite formation. In Plasmodium berghei, a complex of six LCCL domain-containing proteins (LAPs) reside in the crystalloid and are required for its biogenesis. However, little else is known about the molecular mechanisms that underlie the crystalloid's role in sporogony. In this study, we have used transgenic parasites stably expressing LAP3 fused to GFP, combined with GFP affinity pulldown and high accuracy mass spectrometry, to identify an extended LAP interactome of some fifty proteins. We show that many of these are targeted to the crystalloid, including members of two protein families with CPW-WPC and pleckstrin homology-like domains, respectively. Our findings indicate that the LAPs are part of an intricate protein complex, the formation of which facilitates both crystalloid targeting and biogenesis. SIGNIFICANCE: Reducing malaria parasite transmission by mosquitoes is a key component of malaria eradication and control strategies. This study sheds important new light on the molecular composition of the crystalloid, an enigmatic parasite organelle that is essential for sporozoite formation and transmission from the insect to the vertebrate host. Our findings provide new mechanistic insight into how proteins are delivered to the crystalloid, and indicate that the molecular mechanisms that underlie crystalloid function are complex, involving several protein families unique to Plasmodium and closely related organisms. The new crystalloid proteins identified will form a useful starting point for studies aimed at unravelling how the crystalloid organelle facilitates sporogony and transmission.
MeSH term(s)	Animals ; Crystalloid Solutions ; Humans ; Malaria ; Organelles ; Plasmodium berghei ; Protozoan Proteins
Chemical Substances	Crystalloid Solutions ; Protozoan Proteins
Language	English
Publishing date	2020-07-28
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2400835-7
ISSN	1876-7737 ; 1874-3919
ISSN (online)	1876-7737
ISSN	1874-3919
DOI	10.1016/j.jprot.2020.103925
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Article ; Online: NAD(P) transhydrogenase has vital non-mitochondrial functions in malaria parasite transmission.

Saeed, Sadia / Tremp, Annie Z / Sharma, Vikram / Lasonder, Edwin / Dessens, Johannes T

EMBO reports

2020 Volume 21, Issue 3, Page(s) e47832

Abstract: Nicotinamide adenine dinucleotide (NAD) and its phosphorylated form (NADP) are vital for cell function in all organisms and form cofactors to a host of enzymes in catabolic and anabolic processes. NAD(P) transhydrogenases (NTHs) catalyse hydride ion ... ...

Abstract	Nicotinamide adenine dinucleotide (NAD) and its phosphorylated form (NADP) are vital for cell function in all organisms and form cofactors to a host of enzymes in catabolic and anabolic processes. NAD(P) transhydrogenases (NTHs) catalyse hydride ion transfer between NAD(H) and NADP(H). Membrane-bound NTH isoforms reside in the cytoplasmic membrane of bacteria, and the inner membrane of mitochondria in metazoans, where they generate NADPH. Here, we show that malaria parasites encode a single membrane-bound NTH that localises to the crystalloid, an organelle required for sporozoite transmission from mosquitos to vertebrates. We demonstrate that NTH has an essential structural role in crystalloid biogenesis, whilst its enzymatic activity is required for sporozoite development. This pinpoints an essential function in sporogony to the activity of a single crystalloid protein. Its additional presence in the apicoplast of sporozoites identifies NTH as a likely supplier of NADPH for this organelle during liver infection. Our findings reveal that Plasmodium species have co-opted NTH to a variety of non-mitochondrial organelles to provide a critical source of NADPH reducing power.
MeSH term(s)	Animals ; Malaria/transmission ; Mitochondria/genetics ; NAD ; NADP ; NADP Transhydrogenases/genetics
Chemical Substances	NAD (0U46U6E8UK) ; NADP (53-59-8) ; NADP Transhydrogenases (EC 1.6.1.-)
Language	English
Publishing date	2020-01-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.201947832
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Article: Plasmodium berghei LAPs form an extended protein complex that facilitates crystalloid targeting and biogenesis

Tremp, Annie Z / Saeed, Sadia / Sharma, Vikram / Lasonder, Edwin / Dessens, Johannes T

Journal of proteomics. 2020 Sept. 15, v. 227

2020

Abstract	Passage of malaria parasites through mosquitoes involves multiple developmental transitions, from gametocytes that are ingested with the blood meal, through to sporozoites that are transmitted by insect bite to the host. During the transformation from gametocyte to oocyst, the parasite forms a unique transient organelle named the crystalloid, which is involved in sporozoite formation. In Plasmodium berghei, a complex of six LCCL domain-containing proteins (LAPs) reside in the crystalloid and are required for its biogenesis. However, little else is known about the molecular mechanisms that underlie the crystalloid's role in sporogony. In this study, we have used transgenic parasites stably expressing LAP3 fused to GFP, combined with GFP affinity pulldown and high accuracy mass spectrometry, to identify an extended LAP interactome of some fifty proteins. We show that many of these are targeted to the crystalloid, including members of two protein families with CPW-WPC and pleckstrin homology-like domains, respectively. Our findings indicate that the LAPs are part of an intricate protein complex, the formation of which facilitates both crystalloid targeting and biogenesis.Reducing malaria parasite transmission by mosquitoes is a key component of malaria eradication and control strategies. This study sheds important new light on the molecular composition of the crystalloid, an enigmatic parasite organelle that is essential for sporozoite formation and transmission from the insect to the vertebrate host. Our findings provide new mechanistic insight into how proteins are delivered to the crystalloid, and indicate that the molecular mechanisms that underlie crystalloid function are complex, involving several protein families unique to Plasmodium and closely related organisms. The new crystalloid proteins identified will form a useful starting point for studies aimed at unravelling how the crystalloid organelle facilitates sporogony and transmission.
Keywords	Culicidae ; Plasmodium berghei ; biogenesis ; blood meal ; gametocytes ; insects ; malaria ; mass spectrometry ; oocysts ; parasites ; pleckstrin ; sporogony ; sporozoites ; vertebrates
Language	English
Dates of publication	2020-0915
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	2400835-7
ISSN	1876-7737 ; 1874-3919
ISSN (online)	1876-7737
ISSN	1874-3919
DOI	10.1016/j.jprot.2020.103925
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Article: Vesiculation of Red Blood Cells in the Blood Bank: A Multi-Omics Approach towards Identification of Causes and Consequences.

Freitas Leal, Joames K / Lasonder, Edwin / Sharma, Vikram / Schiller, Jürgen / Fanelli, Giuseppina / Rinalducci, Sara / Brock, Roland / Bosman, Giel

Proteomes

2020 Volume 8, Issue 2

Abstract: Microvesicle generation is an integral part of the aging process of red blood cells in vivo and in vitro. Extensive vesiculation impairs function and survival of red blood cells after transfusion, and microvesicles contribute to transfusion reactions. ... ...

Abstract	Microvesicle generation is an integral part of the aging process of red blood cells in vivo and in vitro. Extensive vesiculation impairs function and survival of red blood cells after transfusion, and microvesicles contribute to transfusion reactions. The triggers and mechanisms of microvesicle generation are largely unknown. In this study, we combined morphological, immunochemical, proteomic, lipidomic, and metabolomic analyses to obtain an integrated understanding of the mechanisms underlying microvesicle generation during the storage of red blood cell concentrates. Our data indicate that changes in membrane organization, triggered by altered protein conformation, constitute the main mechanism of vesiculation, and precede changes in lipid organization. The resulting selective accumulation of membrane components in microvesicles is accompanied by the recruitment of plasma proteins involved in inflammation and coagulation. Our data may serve as a basis for further dissection of the fundamental mechanisms of red blood cell aging and vesiculation, for identifying the cause-effect relationship between blood bank storage and transfusion complications, and for assessing the role of microvesicles in pathologies affecting red blood cells.
Language	English
Publishing date	2020-03-31
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2720995-7
ISSN	2227-7382
ISSN	2227-7382
DOI	10.3390/proteomes8020006
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Article: cAMP-Dependent Signaling Pathways as Potential Targets for Inhibition of

Lasonder, Edwin / More, Kunal / Singh, Shailja / Haidar, Malak / Bertinetti, Daniela / Kennedy, Eileen J / Herberg, Friedrich W / Holder, Anthony A / Langsley, Gordon / Chitnis, Chetan E

Frontiers in microbiology

2021 Volume 12, Page(s) 684005

Abstract: We review the role of signaling pathways in regulation of the key processes of merozoite egress and red blood cell invasion ... ...

Abstract	We review the role of signaling pathways in regulation of the key processes of merozoite egress and red blood cell invasion by
Language	English
Publishing date	2021-05-24
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2021.684005
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Article ; Online: LCCL protein complex formation in Plasmodium is critically dependent on LAP1.

Tremp, Annie Z / Sharma, Vikram / Carter, Victoria / Lasonder, Edwin / Dessens, Johannes T

Molecular and biochemical parasitology

2017 Volume 214, Page(s) 87–90

Abstract: Successful sporogony of Plasmodium berghei in vector mosquitoes requires expression of a family of six modular proteins named LCCL lectin domain adhesive-like proteins (LAPs). The LAPs share a subcellular localization in the crystalloid, a unique ... ...

Abstract	Successful sporogony of Plasmodium berghei in vector mosquitoes requires expression of a family of six modular proteins named LCCL lectin domain adhesive-like proteins (LAPs). The LAPs share a subcellular localization in the crystalloid, a unique parasite organelle that forms during ookinete development. Here, LAP interactions in P. berghei were studied using a series of parasite lines stably expressing reporter-tagged LAPs combined with affinity purification and high accuracy label free quantitative mass spectrometry. Our results show that abundant complexes containing LAP1, LAP2 and LAP3 are formed in gametocytes through high avidity interactions. Following fertilization, LAP4, LAP5 and LAP6 are recruited to this complex, a process that is facilitated by LAP1 chiefly through its scavenger receptor cysteine-rich modules. These collective findings provide new insight into the temporal and molecular dynamics of protein complex formation that lead up to, and are required for, crystalloid biogenesis and downstream sporozoite transmission of malaria parasites.
Language	English
Publishing date	2017-06
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	756166-0
ISSN	1872-9428 ; 0166-6851
ISSN (online)	1872-9428
ISSN	0166-6851
DOI	10.1016/j.molbiopara.2017.04.005
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Article ; Online: Proteomic analysis discovers the differential expression of novel proteins and phosphoproteins in meningioma including NEK9, HK2 and SET and deregulation of RNA metabolismResearch in context

Jemma Dunn / Sara Ferluga / Vikram Sharma / Matthias Futschik / David A. Hilton / Claire L. Adams / Edwin Lasonder / C. Oliver Hanemann

EBioMedicine, Vol 40, Iss , Pp 77-

2019 Volume 91

Abstract: Background: Meningioma is the most frequent primary intracranial tumour. Surgical resection remains the main therapeutic option as pharmacological intervention is hampered by poor knowledge of their proteomic signature. There is an urgent need to ... ...

Abstract	Background: Meningioma is the most frequent primary intracranial tumour. Surgical resection remains the main therapeutic option as pharmacological intervention is hampered by poor knowledge of their proteomic signature. There is an urgent need to identify new therapeutic targets and biomarkers of meningioma. Methods: We performed proteomic profiling of grade I, II and III frozen meningioma specimens and three normal healthy human meninges using LC-MS/MS to analyse global proteins, enriched phosphoproteins and phosphopeptides. Differential expression and functional annotation of proteins was completed using Perseus, IPA® and DAVID. We validated differential expression of proteins and phosphoproteins by Western blot on a meningioma validation set and by immunohistochemistry. Findings: We quantified 3888 proteins and 3074 phosphoproteins across all meningioma grades and normal meninges. Bioinformatics analysis revealed commonly upregulated proteins and phosphoproteins to be enriched in Gene Ontology terms associated with RNA metabolism. Validation studies confirmed significant overexpression of proteins such as EGFR and CKAP4 across all grades, as well as the aberrant activation of the downstream PI3K/AKT pathway, which seems differential between grades. Further, we validated upregulation of the total and activated phosphorylated form of the NIMA-related kinase, NEK9, involved in mitotic progression. Novel proteins identified and validated in meningioma included the nuclear proto-oncogene SET, the splicing factor SF2/ASF and the higher-grade specific protein, HK2, involved in cellular metabolism. Interpretation: Overall, we generated a proteomic thesaurus of meningiomas for the identification of potential biomarkers and therapeutic targets. Fund: This study was supported by Brain Tumour Research. Keywords: Meningioma, Proteomics, Phosphoproteins, Differential expression, Grade-specific, RNA metabolism
Keywords	Medicine ; R ; Medicine (General) ; R5-920
Subject code	616
Language	English
Publishing date	2019-02-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: Proteomic analysis discovers the differential expression of novel proteins and phosphoproteins in meningioma including NEK9, HK2 and SET and deregulation of RNA metabolism.

Dunn, Jemma / Ferluga, Sara / Sharma, Vikram / Futschik, Matthias / Hilton, David A / Adams, Claire L / Lasonder, Edwin / Hanemann, C Oliver

EBioMedicine

2018 Volume 40, Page(s) 77–91

Abstract	Background: Meningioma is the most frequent primary intracranial tumour. Surgical resection remains the main therapeutic option as pharmacological intervention is hampered by poor knowledge of their proteomic signature. There is an urgent need to identify new therapeutic targets and biomarkers of meningioma. Methods: We performed proteomic profiling of grade I, II and III frozen meningioma specimens and three normal healthy human meninges using LC-MS/MS to analyse global proteins, enriched phosphoproteins and phosphopeptides. Differential expression and functional annotation of proteins was completed using Perseus, IPA® and DAVID. We validated differential expression of proteins and phosphoproteins by Western blot on a meningioma validation set and by immunohistochemistry. Findings: We quantified 3888 proteins and 3074 phosphoproteins across all meningioma grades and normal meninges. Bioinformatics analysis revealed commonly upregulated proteins and phosphoproteins to be enriched in Gene Ontology terms associated with RNA metabolism. Validation studies confirmed significant overexpression of proteins such as EGFR and CKAP4 across all grades, as well as the aberrant activation of the downstream PI3K/AKT pathway, which seems differential between grades. Further, we validated upregulation of the total and activated phosphorylated form of the NIMA-related kinase, NEK9, involved in mitotic progression. Novel proteins identified and validated in meningioma included the nuclear proto-oncogene SET, the splicing factor SF2/ASF and the higher-grade specific protein, HK2, involved in cellular metabolism. Interpretation: Overall, we generated a proteomic thesaurus of meningiomas for the identification of potential biomarkers and therapeutic targets. FUND: This study was supported by Brain Tumour Research.
MeSH term(s)	Cell Line, Tumor ; Chromatography, Liquid ; Computational Biology/methods ; DNA-Binding Proteins ; Gene Expression Regulation, Neoplastic ; Histone Chaperones/genetics ; Histone Chaperones/metabolism ; Humans ; Kinesin/genetics ; Kinesin/metabolism ; Meningioma/genetics ; Meningioma/metabolism ; Meningioma/pathology ; Mutation ; NIMA-Related Kinases/genetics ; NIMA-Related Kinases/metabolism ; Phosphopeptides/metabolism ; Phosphoproteins/metabolism ; Proteome ; Proteomics/methods ; RNA Stability ; Reproducibility of Results ; Tandem Mass Spectrometry ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Tumor Microenvironment/genetics
Chemical Substances	DNA-Binding Proteins ; Histone Chaperones ; KIF2A protein, human ; Phosphopeptides ; Phosphoproteins ; Proteome ; SET protein, human ; Transcription Factors ; NEK9 protein, human (EC 2.7.11.1) ; NIMA-Related Kinases (EC 2.7.11.1) ; Kinesin (EC 3.6.4.4)
Language	English
Publishing date	2018-12-26
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2851331-9
ISSN	2352-3964
ISSN (online)	2352-3964
DOI	10.1016/j.ebiom.2018.12.048
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Article: LCCL protein complex formation in Plasmodium is critically dependent on LAP1

Tremp, Annie Z / Edwin Lasonder / Johannes T. Dessens / Victoria Carter / Vikram Sharma

Molecular and biochemical parasitology. 2017,

2017

Abstract	Successful sporogony of Plasmodium berghei in vector mosquitoes requires expression of a family of six modular proteins named LCCL lectin domain adhesive-like proteins (LAPs). The LAPs share a subcellular localization in the crystalloid, a unique parasite organelle that forms during ookinete development. Here, LAP interactions in P. berghei were studied using a series of parasite lines stably expressing reporter-tagged LAPs combined with affinity purification and high accuracy label free quantitative mass spectrometry. Our results show that abundant complexes containing LAP1, LAP2 and LAP3 are formed in gametocytes through high avidity interactions. Following fertilization, LAP4, LAP5 and LAP6 are recruited to this complex, a process that is facilitated by LAP1 chiefly through its scavenger receptor cysteine-rich modules. These collective findings provide new insight into the temporal and molecular dynamics of protein complex formation that lead up to, and are required for, crystalloid biogenesis and downstream sporozoite transmission of malaria parasites.
Keywords	biogenesis ; gametocytes ; lectins ; malaria ; mass spectrometry ; molecular dynamics ; ookinetes ; parasites ; Plasmodium berghei ; sporogony ; sporozoites
Language	English
Size	p. .
Publishing place	Elsevier B.V.
Document type	Article
Note	Pre-press version
ZDB-ID	756166-0
ISSN	1872-9428 ; 0166-6851
ISSN (online)	1872-9428
ISSN	0166-6851
DOI	10.1016/j.molbiopara.2017.04.005
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