Cloning the Polymorphic Gene for the Mammary Mucin Abnormally Glycosylated in Carcinomas

Author(s):  
S. Gendler ◽  
J. Burchell ◽  
A. Girling ◽  
R. Millis ◽  
T. Duhig ◽  
...  
Keyword(s):  
2019 ◽  
Vol 22 (09) ◽  
pp. 154-160
Author(s):  
Hasanain Khaleel Shareef ◽  
Ahmed Adil Ali ◽  
Rafah F. Al-Jebori

1990 ◽  
Vol 265 (10) ◽  
pp. 5573-5578 ◽  
Author(s):  
M J Ligtenberg ◽  
H L Vos ◽  
A M Gennissen ◽  
J Hilkens

Genetika ◽  
2013 ◽  
Vol 45 (2) ◽  
pp. 611-619
Author(s):  
Oindrila Raha ◽  
B Sarkar ◽  
P. Veerraju ◽  
G. Sudhakar ◽  
P. Raychaudhuri ◽  
...  

Background. The major histocompatibility complex class I chain-related gene A (MICA) (OMIM-600169) is a polymorphic gene in the HLA region expressed mainly by epithelial cells. The MICA protein encoded by the allele influences the activation of NK cells, which modify ?-cells destruction and has been found to be involved in susceptibility of T1DM. Objective. The aim of this study was to find the association of MICA alleles with T1DM among eastern Indian population. Subjects and methods.Study was conducted in 134 eastern Indian patients and with 137 healthy controls for the possible role of MICA gene in T1DM pathogenesis. Results. The MICA*A5 microsatellite allele, showed significantly higher frequencies in patients than controls (p=0.003, OR= 1.746, CI= 1.206-2.528). MICA A*6 was found to be protective in our study (p=<0.01, OR=0.406, CI= 0.268-0.616).


2019 ◽  
Vol 64 (2) ◽  
pp. 165-174
Author(s):  
G. Sh. Safuanova ◽  
N. R. Ryabchikova ◽  
E. K. Khusnutdinova ◽  
D. O. Karimov ◽  
I. R. Minniakhmetov

2016 ◽  
Vol 1 (1) ◽  
Author(s):  
Mulusew Kassa Bitew ◽  
Emmanouil Domazakis

AbstractPhytophthora infestans is the causal agent of late blight, the most devastating disease of potato worldwide. The P. infestans genome encodes potentially polymorphic genes that evolve continually to evade the recognition of plant R genes, though it has hundreds of predicted and conserved effector proteins recognised by the plant. The gene Scr74 encodes a predicted 74-amino acid secreted cysteine-rich protein belonging to a highly polymorphic gene family within P. infestans. This study screened the recognition of Scr74 genes in wild potato genotypes from August 2013 to January 2014 in the Plant Breeding Laboratory of Wageningen University, the Netherlands. To identify the recognition of the Scr74 gene, we grew potato genotypes in the green house for PVX assays, detached leaf assays and molecular work. Twenty-seven good-quality sequences of the Scr74 gene variant with a length of 74 amino acids were found and more frequent amino acid variation was detected on the mature protein. Seventeen Scr74 constructs were identified as diversified and two effectors were strongly recognised by wild S. verrucosum genotypes via effectoromics from the PVX assay. A strong plant cell death hypersensitive response (HR) was recorded on wild S. verrucosum and S. tuberosum genotypes from the detached leaf assay. This recognition seems to be a useful indicator for the presence of a resistance gene (s) to the polymorphic effectors of P. infestans (as it has seen on Scr74 gene) in the wild potato genotypes.


1977 ◽  
Vol 18 (3) ◽  
pp. 237-246 ◽  
Author(s):  
I. Okada ◽  
Y. Yamada ◽  
M. Akiyama ◽  
I. Nishimura ◽  
N. Kano

2020 ◽  
Vol 46 (1) ◽  
pp. 60-64
Author(s):  
D. K. Karimova ◽  
G. N. Sobirova ◽  
M. M. Karimov

In recent years, there has been an increase in the prevalence of inflammatory and destructive diseases of the gastroduodenal zone, which is primarily explained by Helicobacter pylori (H. pylori) infection. One of the main factors of H. pylori pathogenicity is presence of cytotoxin-associated gene — CagA. It is known that CagA-positive H. pylori strains are associated with the development of atrophy, tumor invasion and rapid metastasis. A number of recently published studies have revealed that CagA is a polymorphic gene which contains a different number of repetitive sequences located in the 3’ region. Each repetitive region of CagA contains Glu-Pro-Ile-Tyr-Ala (EPIYA) profiles including tyrosine phosphorylation. Depending on the sequence of the EPIYA profile, there are 4 segments: EPIYA-A, EPIYA-B, EPIYA-C, EPIYA-D, each containing a repetitive region. Geographical features of the prevalence of H. pylori strains depending on the sequence of EPIYA have been revealed: EPIYA-A region of the western isolates of this bacterium is associated with EPIYA-A, EPIYA-B, EPIYA-C segments, while the eastern CagA-positive H. pylori isolates are characterized by the A-B-D type of the CagA gene. Data illustrating the strong correlation between the western CagA-positive H. pylori strains, which have a repeating EPIYA-C segment, and the development of precancerous states, as well as gastric cancer, are presented. H. pylori strains containing simultaneously A-B motives of EPIYA or one C-type of the CagA gene are associated with a 7-fold increase of risk of gastric cancer compared to CagA-negative strains; presence of two or more EPIYA-C motives is associated with a 30-fold increase of this risk.


1991 ◽  
Vol 11 (4) ◽  
pp. 2133-2148
Author(s):  
A Sutton ◽  
D Immanuel ◽  
K T Arndt

Saccharomyces cerevisiae strains containing temperature-sensitive mutations in the SIT4 protein phosphatase arrest in late G1 at the nonpermissive temperature. Order-of-function analysis shows that SIT4 is required in late G1 for progression into S phase. While the levels of SIT4 do not change in the cell cycle, SIT4 associates with two high-molecular-weight phosphoproteins in a cell-cycle-dependent fashion. In addition, we have identified a polymorphic gene, SSD1, that in some versions can suppress the lethality due to a deletion of SIT4 and can also partially suppress the phenotypic defects due to a null mutation in BCY1. The SSD1 protein is implicated in G1 control and has a region of similarity to the dis3 protein of Schizosaccharomyces pombe. We have also identified a gene, PPH2alpha, that in high copy number can partially suppress the growth defect of sit4 strains. The PPH2 alpha gene encodes a predicted protein that is 80% identical to the catalytic domain of mammalian type 2A protein phosphatases but also has an acidic amino-terminal extension not present in other phosphatases.


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