Migfilin, α-parvin and β-parvin are differentially expressed in ovarian serous carcinoma effusions, primary tumors and solid metastases
نویسندگان
چکیده
منابع مشابه
Functional analysis of α-Parvin in vivo
The focal adhesion (FA) protein α-Parvin (αPv) has been shown to regulate integrin signalingand integrin-actin linkage. Here we report that the conditional deletion of the αPv gene inkeratinocytes leads to impaired hair follicle (HF) morphogenesis, epidermal hyperplasia andmicro-blistering. Expression of integrin α6 was reduced on αPv-deficient keratinocytes,leading to defects i...
متن کاملParvin-ILK
Integrin-linked kinase (ILK), PINCH and Parvin proteins form the IPP-complex that has been established as a core component of the integrin-actin link. Our recent genetic studies on Drosophila parvin, reveal that loss of function mutant defects phenocopy those observed upon loss of ILK or PINCH in the muscle and the wing, strengthening the notion that these proteins function together in the orga...
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BACKGROUND The oncogenesis of ovarian cancer is poorly understood. The aim of this study was to identify mRNAs differentially expressed between moderately and poorly differentiated (MD/PD) serous ovarian carcinomas (SC), serous ovarian borderline tumours (SBOT) and superficial scrapings from normal ovaries (SNO), and to correlate these mRNAs with clinical parameters including survival. METHOD...
متن کاملSplicing factors are differentially expressed in tumors.
Although alternative splicing of many genes has been found associated with different stages of tumorigenesis and splicing variants have been characterized as tumor markers, it is still not known whether these examples are sporadic or whether there is a broader association between the two phenomena. In this report we evaluated, through a bioinformatics approach, the expression of splicing factor...
متن کاملStructural Analysis of the Interactions Between Paxillin LD Motifs and α-Parvin
The adaptor protein paxillin contains five conserved leucine-rich (LD) motifs that interact with a variety of focal adhesion proteins, such as alpha-parvin. Here, we report the first crystal structure of the C-terminal calponin homology domain (CH(C)) of alpha-parvin at 1.05 A resolution and show that it is able to bind all the LD motifs, with some selectivity for LD1, LD2, and LD4. Cocrystal s...
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ژورنال
عنوان ژورنال: Gynecologic Oncology
سال: 2013
ISSN: 0090-8258
DOI: 10.1016/j.ygyno.2012.10.015