Molecular cloning and characterization of a novel human protein phosphatase, LMW-DSP3

Cheng, Haipeng; Gao, Qi; Jiang, Min; Ma, Yangyang; Ni, Xiaohua; Guo, Li; Jin, Wei; Cao, Gentao; Ji, Chaoneng; Kong, Ying; Xu, Weiwen; Gu, Shaohua; Ma, Yuhong; Xie, Yun; Mao, Yumin

doi:10.1016/s1357-2725(02)00127-9

Cited by 9 publications

(5 citation statements)

References 21 publications

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“…These results were obtained by repeated experiments. A similar result was seen in the study of human protein phosphatase, LMW-DSP3, which proved that the higher sensitivity of RT-PCR makes it possible to detect some transcripts that cannot be detected in the Northern blot [24]. These findings show the haemocytic production of antimicrobial peptides in Chinese shrimps are consistent with the results shown in horseshoe Labelling appears in some haemocytes (B) and gills (C), the arrow shows a haemocyte located in gill blood vessels.…”

Section: Tissue Distribution and Expression Of Ch-penaeidinsupporting

confidence: 86%

Molecular cloning and expression analysis of Ch-penaeidin, an antimicrobial peptide from Chinese shrimp, Fenneropenaeus chinensis

Kang

Wang

Zhao

et al. 2004

Fish & Shellfish Immunology

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Section: Tissue Distribution and Expression Of Ch-penaeidinsupporting

confidence: 86%

Molecular cloning and expression analysis of Ch-penaeidin, an antimicrobial peptide from Chinese shrimp, Fenneropenaeus chinensis

Kang

Wang

Zhao

et al. 2004

Fish & Shellfish Immunology

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“…The present study demonstrates that LDP-3 is a novel member of the small DSP family, which also contains VHR [6], LDP-1/ TMDP (testis-and skeletal-muscle-specific DSP). [14], LDP-2/ SKRP1/LMW-DSP3 [9,10,21], DUSP-18 [22], and JSP-1/VHX (VHR-related MKPX)/LMW-DSP2 and its splice variant, JKAP (JNK pathway-associated phosphatase) [11,[23][24][25]. In vitro characterization of the enzyme activity of bacterially expressed LDP-3 revealed its preferential dephosphorylation of tyrosine residues in proteins, as reported previously for LDP-2, DUSP-18 and JSP-1 [9,21,23].…”

Section: Discussionsupporting

confidence: 74%

“…[14], LDP-2/ SKRP1/LMW-DSP3 [9,10,21], DUSP-18 [22], and JSP-1/VHX (VHR-related MKPX)/LMW-DSP2 and its splice variant, JKAP (JNK pathway-associated phosphatase) [11,[23][24][25]. In vitro characterization of the enzyme activity of bacterially expressed LDP-3 revealed its preferential dephosphorylation of tyrosine residues in proteins, as reported previously for LDP-2, DUSP-18 and JSP-1 [9,21,23]. Some small DSPs have been shown to be involved in negative regulation of the MAPK pathway [7][8][9][10].…”

Section: Discussionmentioning

confidence: 99%

Characterization of a novel low-molecular-mass dual-specificity phosphatase-3 (LDP-3) that enhances activation of JNK and p38

Takagaki

Satoh

Tanuma

et al. 2004

Biochemical Journal

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We have isolated a mouse cDNA for a novel dual-specificity phosphatase designated LDP-3 (low-molecular-mass dual-specificity phosphatase 3). The 450 bp open reading frame encodes a protein of 150 amino acids with a predicted molecular mass of 16 kDa. Northern blot and reverse transcription-PCR analyses show that LDP-3 transcripts are expressed in almost all mouse tissues examined. In vitro analyses using several substrates and inhibitors indicate that LDP-3 possesses intrinsic dual-specificity phosphatase activity. When expressed in mammalian cells, LDP-3 protein is localized mainly to the apical submembrane area. Forced expression of LDP-3 does not alter activation of ERK (extracellular-signal-regulated kinase), but rather enhances activation of JNK (c-Jun N-terminal kinase) and p38 and their respective upstream kinases MKK4 (mitogen-activated protein kinase kinase 4) and MKK6 in cells treated with 0.4 M sorbitol. By screening with a variety of stimuli, we found that LDP-3 specifically enhances the osmotic stress-induced activation of JNK and p38.

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“…A less obvious example is the dual specificity phosphatase 19 (DUSP19), a phosphatase added by the extension procedure to MAPK pathways, the Fc epsilon receptor I signalling pathway and to a pathway known to be activated in response to HIV Nef protein (negative effector of Fas and TNF). This protein is highly expressed in the pancreas [30] and displays a frameshift mutation in pancreatic tumours [28]. …”

Section: Resultsmentioning

confidence: 99%

Extending pathways and processes using molecular interaction networks to analyse cancer genome data

et al. 2010

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BackgroundCellular processes and pathways, whose deregulation may contribute to the development of cancers, are often represented as cascades of proteins transmitting a signal from the cell surface to the nucleus. However, recent functional genomic experiments have identified thousands of interactions for the signalling canonical proteins, challenging the traditional view of pathways as independent functional entities. Combining information from pathway databases and interaction networks obtained from functional genomic experiments is therefore a promising strategy to obtain more robust pathway and process representations, facilitating the study of cancer-related pathways.ResultsWe present a methodology for extending pre-defined protein sets representing cellular pathways and processes by mapping them onto a protein-protein interaction network, and extending them to include densely interconnected interaction partners. The added proteins display distinctive network topological features and molecular function annotations, and can be proposed as putative new components, and/or as regulators of the communication between the different cellular processes. Finally, these extended pathways and processes are used to analyse their enrichment in pancreatic mutated genes. Significant associations between mutated genes and certain processes are identified, enabling an analysis of the influence of previously non-annotated cancer mutated genes.ConclusionsThe proposed method for extending cellular pathways helps to explain the functions of cancer mutated genes by exploiting the synergies of canonical knowledge and large-scale interaction data.

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Molecular cloning and characterization of a novel human protein phosphatase, LMW-DSP3

Cited by 9 publications

References 21 publications

Molecular cloning and expression analysis of Ch-penaeidin, an antimicrobial peptide from Chinese shrimp, Fenneropenaeus chinensis

Molecular cloning and expression analysis of Ch-penaeidin, an antimicrobial peptide from Chinese shrimp, Fenneropenaeus chinensis

Characterization of a novel low-molecular-mass dual-specificity phosphatase-3 (LDP-3) that enhances activation of JNK and p38

Extending pathways and processes using molecular interaction networks to analyse cancer genome data

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