Transformation of Cm-ADH gene to melon genotype

2016 ◽  
pp. 137-142 ◽  
Author(s):  
E. Kocaman ◽  
Y. Yalcin Mendi ◽  
A. Latche ◽  
T. Izgu ◽  
I. El-Sharkawy
Keyword(s):  
Adh Gene

Structure, expression, chromosomal location and product of the gene encoding Adh2 in Petunia.

Genetics ◽  
1993 ◽  
Vol 133 (4) ◽  
pp. 999-1007
Author(s):  
R G Gregerson ◽  
L Cameron ◽  
M McLean ◽  
P Dennis ◽  
J Strommer
Keyword(s):  
Chromosomal Location ◽  
Higher Plants ◽  
Gene Encoding ◽  
Genomic Libraries ◽  
Regulatory Strategy ◽  
Adh1 Gene ◽  
Adh Genes ◽  
Genes Encoding ◽  
Adh Gene ◽  
Polymerase Chain

Abstract In most higher plants the genes encoding alcohol dehydrogenase comprise a small gene family, usually with two members. The Adh1 gene of Petunia has been cloned and analyzed, but a second identifiable gene was not recovered from any of three genomic libraries. We have therefore employed the polymerase chain reaction to obtain the major portion of a second Adh gene. From sequence, mapping and northern data we conclude this gene encodes ADH2, the major anaerobically inducible Adh gene of Petunia. The availability of both Adh1 and Adh2 from Petunia has permitted us to compare their structures and patterns of expression to those of the well-studied Adh genes of maize, of which one is highly expressed developmentally, while both are induced in response to hypoxia. Despite their evolutionary distance, evidenced by deduced amino acid sequence as well as taxonomic classification, the pairs of genes are regulated in strikingly similar ways in maize and Petunia. Our findings suggest a significant biological basis for the regulatory strategy employed by these distant species for differential expression of multiple Adh genes.

The plant ADH gene family

2011 ◽  
Vol 66 (1) ◽  
pp. 128-142 ◽  
Author(s):  
Judith Strommer
Keyword(s):  
Gene Family ◽  
Adh Gene

Drosophila transcriptional repressor protein that binds specifically to negative control elements in fat body enhancers

1992 ◽  
Vol 12 (9) ◽  
pp. 4093-4103
Author(s):  
D Falb ◽  
T Maniatis
Keyword(s):  
Binding Site ◽  
Fat Body ◽  
Regulatory Element ◽  
Negative Control ◽  
Nuclear Extracts ◽  
Eukaryotic Proteins ◽  
Adh Gene ◽  
A Site

Expression of the Drosophila melanogaster Adh gene in adults requires a fat body-specific enhancer called the Adh adult enhancer (AAE). We have identified a protein in Drosophila nuclear extracts that binds specifically to a site within the AAE (adult enhancer factor 1 [AEF-1]). In addition, we have shown that AEF-1 binds specifically to two other Drosophila fat body enhancers. Base substitutions in the AEF-1 binding site that disrupt AEF-1 binding in vitro result in a significant increase in the level of Adh expression in vivo. Thus, the AEF-1 binding site is a negative regulatory element within the AAE. A cDNA encoding the AEF-1 protein was isolated and shown to act as a repressor of the AAE in cotransfection studies. The AEF-1 protein contains four zinc fingers and an alanine-rich sequence. The latter motif is found in other eukaryotic proteins known to be transcriptional repressors.

scholarly journals Genome-wide identification and comparative analysis of the ADH gene family in Chinese white pear (Pyrus bretschneideri) and other Rosaceae species

Genomics ◽  
2020 ◽  
Vol 112 (5) ◽  
pp. 3484-3496
Author(s):  
Weiwei Zeng ◽  
Xin Qiao ◽  
Qionghou Li ◽  
Chunxin Liu ◽  
Jun Wu ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Gene Family ◽  
Rosaceae Species ◽  
Chinese White ◽  
Genome Wide ◽  
Adh Gene

605 COMBINATION OF ADH GENE POLYMORPHISM AND ALCOHOL CONSUMPTION CONSTITUTES A NOVEL PROSTATE CANCER RISK FACTOR IN AFRICAN-AMERICAN MEN

2011 ◽  
Vol 185 (4S) ◽  
Author(s):  
Lionel L. Bañez ◽  
Cathrine Hoyo ◽  
Elizabeth M. Masko ◽  
Elizabeth E. Calloway ◽  
Kathleen H. Shuler ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
African American ◽  
Risk Factor ◽  
Alcohol Consumption ◽  
Cancer Risk ◽  
Gene Polymorphism ◽  
African American Men ◽  
Prostate Cancer Risk ◽  
Cancer Risk Factor ◽  
Adh Gene

scholarly journals Role of UGT1A1 and ADH gene polymorphisms in pegvisomant-induced liver toxicity in acromegalic patients

2014 ◽  
Vol 170 (2) ◽  
pp. 247-254 ◽  
Author(s):  
M Filopanti ◽  
A M Barbieri ◽  
G Mantovani ◽  
S Corbetta ◽  
V Gasco ◽  
...  
Keyword(s):  
Liver Toxicity ◽  
Tertiary Care ◽  
Somatostatin Analogs ◽  
Liver Function Tests ◽  
Regression Analyses ◽  
Increased Risk ◽  
Adh Gene ◽  
Concomitant Medications

ContextHepatotoxicity is one of the most serious adverse effects in acromegalic patients treated with pegvisomant (PEG-V). Recent studies have found an association between this adverse event and the UGT1A1 allele 28 polymorphism associated with Gilbert's syndrome.ObjectiveTo determine whether UGT1A1*28 and alcohol dehydrogenase (ADH) polymorphisms influence liver toxicity during PEG-V treatment.Design and settingMulticenter observational retrospective study conducted in 13 tertiary care endocrinology units in Italy.PatientsA total of 112 patients with active disease resistant to somatostatin analogs (SSTa) and 108 controls were enrolled.InterventionsClinical and biochemical data were recorded by electronic clinical reporting forms. Blood or DNA samples were sent to the coordinating center for genotyping.ResultsNo differences in genotypes between patients and controls were found. During PEG-V therapy liver function tests (LFT), abnormalities and overt hepatotoxicity developed in 17 and 4.5% of patients respectively. Logistic and linear regression analyses showed an association between LFT abnormalities during the follow-up visit and prior events of LFT abnormalities in medical history (odds ratio=1.25;P=0.04) and the number of concomitant medications, other than SSTa (B=3.9;P=0.03). No correlation between LFT alterations and UGT1A1 allele 28 as well as ADH1C and B polymorphisms was found.ConclusionsUGT1A1 allele 28 and ADH1C and B polymorphisms do not predict increased risk of hepatotoxicity during PEG-V therapy. Conversely, patients with multi-therapies and with previous episodes of liver disease should be carefully managed, due to the observed association between these conditions and LFT abnormalities during PEG-V therapy.

scholarly journals Induced ADH gene expression and enzyme activity in pollinated pistils of Solanum tuberosum

1997 ◽  
Vol 10 (2) ◽  
pp. 107-109 ◽  
Author(s):  
G. J. van Eldik ◽  
R. K. Ruiter ◽  
Marinus M. A. van Herpen ◽  
J. A. M. Schrauwen ◽  
George J. Wullems
Keyword(s):  
Gene Expression ◽  
Enzyme Activity ◽  
Solanum Tuberosum ◽  
Adh Gene

Expression profile and co-expression analysis of ADH1A in human solid tumors.

2020 ◽  
Vol 38 (15_suppl) ◽  
pp. e13533-e13533
Author(s):  
Wenqi Huang ◽  
Mi Yang ◽  
Xixi Wu ◽  
Lu Yuan ◽  
Yuting Wu ◽  
...  
Keyword(s):  
Solid Tumors ◽  
Lung Squamous Cell Carcinoma ◽  
Normal Tissues ◽  
Adh1 Gene ◽  
Regulation Network ◽  
Human Solid Tumors ◽  
Adh Gene ◽  
Colon And Rectum ◽  
Biology Process ◽  
Liver Hepatocellular Carcinoma

e13533 Background: The human alcohol dehydrogenase (ADH) gene family is associated with various solid cancers. It seems that the ADH1 gene cluster plays an important role in various solid tumors, so it aroused our interest in studying these genes to find out their functions and biological process within different solid tumors. Methods: Paired tumor and normal tissues gathered from 38 tumor patients, and 5 male BALB/c mice tissues were collected and Immunohistochemistry (IHC) assay was performed. The expression of ADH1A at RNA level in normal tissues and pan-solid tumors and the main functions of ADH1A in different solid tumors were analyzed by Bioinformatics mining. Results: At the RNA level, ADH1A was highly expressed in normal hepatocytes and was expressed lower in the tumor tissues than in the adjacent normal tissues or the corresponding normal tissues, suggesting the At the protein level, ADH1A was expressed to varying degrees in human alveoli, kidney, stomach, colon, and rectum. We predicted three major conserved functions of ADH1A, including angiogenesis, cell adhesion, and leukocyte migration function which might influence the prognosis of the immunotherapy and the immune response, and constructed an upstream regulation network of ADH1A and a downstream protein network. Besides, we also explored the functional differences of ADH1A in lung adenocarcinoma and lung squamous cell carcinoma and its effect on overall survival. And for investigating ADH1A, the BALB/c mice might be an option to consider in constructing an animal model of gastric cancer (GC), esophageal carcinoma (ESCA), liver hepatocellular carcinoma (LIHC), and pancreatic adenocarcinoma (PAAD). Conclusions: ADH1A has potential diagnostic and prognostic value in various solid tumors. Our findings highlight new avenues for further investigation of ADH1A biology process and provide a novel potential prognostic biomarker of immunotherapy.

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