Dataset Information

Phoneutria nigriventer Proteome

ABSTRACT: We used a bottom up to obtain a proteomic overview of the venomous extract of the Phoneutria nigriventer venom.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Phoneutria Nigriventer

TISSUE(S): Venom

SUBMITTER: Marcia Borges

LAB HEAD: Márcia Helena Borges

PROVIDER: PXD008909 | Pride | 2018-08-08

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	20131105_Pn_Silv_10.RAW	Raw
	20131105_Pn_Silv_10.mgf	Mgf
	20131105_Pn_Silv_10.mzid.gz	Mzid
	20131105_Pn_Silv_10.pride.mgf.gz	Mgf
	20131105_Pn_Silv_10.pride.mztab.gz	Mztab

Items per page:

1 - 5 of 50

Publications

An overview of Phoneutria nigriventer spider venom using combined transcriptomic and proteomic approaches.

Diniz Marcelo R V MRV Paiva Ana L B ALB Guerra-Duarte Clara C Nishiyama Milton Y MY Mudadu Mauricio A MA Oliveira Ursula de U Borges Márcia H MH Yates John R JR Junqueira-de-Azevedo Inácio de L IL

PloS one 20180801 8

Phoneutria nigriventer is one of the largest existing true spiders and one of the few considered medically relevant. Its venom contains several neurotoxic peptides that act on different ion channels and chemical receptors of vertebrates and invertebrates. Some of these venom toxins have been shown as promising models for pharmaceutical or biotechnological use. However, the large diversity and the predominance of low molecular weight toxins in this venom have hampered the identification and deep ...[more]

PMID: 30067761

Similar Datasets

Project description:Background: Maspin (SERPINB5) is a potential tumor suppressor gene with pleiotropic biological activities, including regulation of cell proliferation, death, adhesion, migration and gene expression. Several studies indicate that nuclear localization is essential for maspin tumor suppression activity. We have previously shown that the EGFR activation leads to maspin nuclear localization in MCF-10A cells. The present study investigated which EGFR downstream signaling molecules are involved in maspin nuclear localization and explored a possible role of cell-cell contact in this process. Methods: MCF-10A cells were treated with pharmacological inhibitors against EGFR downstream pathways followed by EGF treatment. Maspin subcellular localization was determined by immunofluorescence. To investigate the role of cell-cell contact these cells were either treated with chelating agents or plated on different cell densities. Maspin and E-cadherin subcellular localization was determined by immunofluorescence. In addition, proteomic and interactome analyses were conducted in order to identify molecular partners which interact with maspin in EGF-treated cells only. Results: EGFR activation regulates cell behavior via de extracellular signal–related kinase (ERK)/MAP kinase, phosphatidyl-inositol-3 (PI 3) kinase- AKT and Jak-STAT pathways. Using pharmacological inhibitors against key components of these signaling pathways we found that PI3K-AKT and Jak-STAT, but not MAP kinase pathway, regulate EGF-induced maspin nuclear accumulation in MCF-10A cells. Interestingly, we observed that maspin is predominantly nuclear in sparse cell culture, but it is redistributed to the cytoplasm in confluent cells even in the presence of EGF. Proteomic and interactome results suggest a role of maspin on post-transcriptional and translation regulation, protein folding and cell-cell adhesion.Conclusions: Maspin nuclear accumulation is determined by an interplay between EGFR (via PI3K-AKT and Jak-STAT pathways) and cell-to-cell contact.