5A11/Basigin Gene Products Are Necessary for Proper Maturation and Function of the Retina

2004 ◽  
Vol 26 (5-6) ◽  
pp. 380-387 ◽  
Author(s):  
Judith D. Ochrietor ◽  
Paul J. Linser
1983 ◽  
pp. 181-202 ◽  
Author(s):  
Graham C. Walker ◽  
Stephen J. Elledge ◽  
Karen L. Perry ◽  
Anne Bagg ◽  
Cynthia J. Kenyon

1988 ◽  
Vol 26 (1) ◽  
pp. 123-143 ◽  
Author(s):  
W G Dougherty ◽  
J C Carrington
Keyword(s):  

1991 ◽  
pp. 87-164 ◽  
Author(s):  
Mone Zaidi ◽  
Baljit S. Moonga ◽  
Peter J.R. Bevis ◽  
A.S.M. Towhidul Alam ◽  
Stephen Legon ◽  
...  

2020 ◽  
Author(s):  
Leanne Jones ◽  
Michael Naidoo ◽  
Lee R. Machado ◽  
Karen Anthony

Abstract Background Mutation of the Duchenne muscular dystrophy (DMD) gene causes Duchenne and Becker muscular dystrophy, degenerative neuromuscular disorders that primarily affect voluntary muscles. However, increasing evidence implicates DMD in the development of all major cancer types. DMD is a large gene with 79 exons that codes for the essential muscle protein dystrophin. Alternative promotor usage drives the production of several additional dystrophin protein products with roles that extend beyond skeletal muscle. The importance and function(s) of these gene products outside of muscle are not well understood. Conclusions We highlight a clear role for DMD in the pathogenesis of several cancers, including sarcomas, leukaemia’s, lymphomas, nervous system tumours, melanomas and various carcinomas. We note that the normal balance of DMD gene products is often disrupted in cancer. The short dystrophin protein Dp71 is, for example, typically maintained in cancer whilst the full-length Dp427 gene product, a likely tumour suppressor, is frequently inactivated in cancer due to a recurrent loss of 5’ exons. Therefore, the ratio of short and long gene products may be important in tumorigenesis. In this review, we summarise the tumours in which DMD is implicated and provide a hypothesis for possible mechanisms of tumorigenesis, although the question of cause or effect may remain. We hope to stimulate further study into the potential role of DMD gene products in cancer and the development of novel therapeutics that target DMD.


EPPO Bulletin ◽  
2006 ◽  
Vol 36 (2) ◽  
pp. 229-238 ◽  
Author(s):  
B. Salvador ◽  
J. A. García ◽  
C. Simón-Mateo

2019 ◽  
Vol 116 (25) ◽  
pp. 12343-12352 ◽  
Author(s):  
David C. Lamb ◽  
Alec H. Follmer ◽  
Jared V. Goldstone ◽  
David R. Nelson ◽  
Andrew G. Warrilow ◽  
...  

Genes encoding cytochrome P450 (CYP; P450) enzymes occur widely in the Archaea, Bacteria, and Eukarya, where they play important roles in metabolism of endogenous regulatory molecules and exogenous chemicals. We now report that genes for multiple and unique P450s occur commonly in giant viruses in the Mimiviridae, Pandoraviridae, and other families in the proposed order Megavirales. P450 genes were also identified in a herpesvirus (Ranid herpesvirus 3) and a phage (Mycobacterium phage Adler). The Adler phage P450 was classified as CYP102L1, and the crystal structure of the open form was solved at 2.5 Å. Genes encoding known redox partners for P450s (cytochrome P450 reductase, ferredoxin and ferredoxin reductase, and flavodoxin and flavodoxin reductase) were not found in any viral genome so far described, implying that host redox partners may drive viral P450 activities. Giant virus P450 proteins share no more than 25% identity with the P450 gene products we identified in Acanthamoeba castellanii, an amoeba host for many giant viruses. Thus, the origin of the unique P450 genes in giant viruses remains unknown. If giant virus P450 genes were acquired from a host, we suggest it could have been from an as yet unknown and possibly ancient host. These studies expand the horizon in the evolution and diversity of the enormously important P450 superfamily. Determining the origin and function of P450s in giant viruses may help to discern the origin of the giant viruses themselves.


2017 ◽  
Vol 59 (3) ◽  
pp. 269-283 ◽  
Author(s):  
Zhigang Hu ◽  
Wen-Jun Shen ◽  
Fredric B Kraemer ◽  
Salman Azhar

miR-132 is hormonally regulated in steroidogenic cells of the adrenal gland, ovary and testis. Here, we examined the potential role of miR-132 in the control of steroidogenesis. Transfection of Y1 adrenal cells with miR-132 increased mRNAs of 3β-HSD and 20α-HSD enzymes, which catalyze the sequential conversion of pregnenolone to progesterone to biologically inactive 20α-hydroxyprogesterone (20α-OHP). Overexpression of miR-132 reduced MeCP2 and StAR protein expression, basal progestin (progesterone and 20α-OHP) production, but enhanced their production in response to cAMP stimulation. Use of [3H] pregnenolone and free-diffusible 22(R)-hydroxycholesterol further confirmed that miR-132 promotes the production of 20α-OHP by upregulating 3β-HSD and 20α-HSD. Evidence is also presented that StAR is a direct target of miR-132. Transient transfection of Y1 cells with miR-132 demonstrated that miR-132 induction of 3β-HSD and 20α-HSD was accompanied by significant suppression of one of its target gene products, MeCP2. In contrast, co-expression of miR-132 plus MeCP2 protein partially blocked the ability of miR-132 to upregulate the expression and function of 3β-HSD and 20α-HSD. Moreover, suppression of MeCP2 protein with siRNA resulted in increased expression of 3β-HSD and 20α-HSD, further demonstrating that miR-132 induces the expression of these two enzymes via inhibition of MeCP2. Likewise, overexpression of miR-132 increased 20α-OHP production with and without HDL loading, while knockdown of miR-132 resulted in a significant decrease of 20α-OHP production by granulosa cells. In conclusion, our data suggest that miR-132 attenuates steroidogenesis by repressing StAR expression and inducing 20α-HSD via inhibition of MeCP2 to generate a biologically inactive 20α-OHP.


2013 ◽  
Vol 92 (7) ◽  
pp. 622-628 ◽  
Author(s):  
P. Atsawasuwan ◽  
X. Lu ◽  
Y. Ito ◽  
Y. Chen ◽  
G. Gopinathan ◽  
...  

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