scholarly journals Histological Analysis, Bioinformatics Profile, and Expression of Methylenetetrahydrofolate Reductase (MTHFR) in Bovine Testes

Animals ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 1731
Author(s):  
Seth Afedo ◽  
Yan Cui ◽  
Sijiu Yu ◽  
Bo Liao ◽  
Zihan Zhao ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Expression ◽  
Methylenetetrahydrofolate Reductase ◽  
Protein Structures ◽  
Zebu Cattle ◽  
Reading Frame ◽  
Physico Chemical ◽  
Yellow Cattle ◽  
Mrna And Protein Expression ◽  
Sequence Encoding

Methylenetetrahydrofolate reductase (MTHFR), an enzyme expressed in mammalian testes, exerts a direct effect on spermatogenesis; however, its protein characteristics in bovine testes remain unknown. Here, we analysed bovine testicular structure, MTHFR bioinformatics profile, mRNA, and protein expression characteristics in yellow-cattle (y-c) and yak testis using histological procedures, bioinformatics analysis, qRT-PCR, and western blot. Testes from 13 bovines, ≤2 years juvenile (y-c, n = 3; yak, n = 3) and ≥3 years adult (y-c, n = 3; yak, n = 4) were collected and analysed. Anatomical characteristics of testis in y-c and yak were similar except the weight or size for which that of y-c was significantly higher or greater than yak. In y-c, an open reading frame (ORF) for 2600 nucleotides sequence, encoding 655 amino acids showed high homology with zebu cattle (99.51%) and wild yak (98.68%). Secondary and 3D protein structures were similar to that of humans with differences in the number of nucleotides, amino acids, and some physico-chemical characteristics. MTHFR mRNA expression in y-c and yak were significantly higher in adult testes compared with juvenile ones. However, its protein expression was higher, but not statistically significant, in adult y-c and yak compared to the juvenile ones. The highlights and inferences of these and other findings are discussed.

scholarly journals Histological Analysis, Bioinformatics Profile, and Expression of Methylenetetrahydrofolate Reductase (MTHFR) in Bovine Testes

2020 ◽  
Author(s):  
Seth Yaw Afedo ◽  
Yan Cui ◽  
Sijiu Yu ◽  
Bo Liao ◽  
Zihan Zhao ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Expression ◽  
Methylenetetrahydrofolate Reductase ◽  
Protein Structures ◽  
Zebu Cattle ◽  
Reading Frame ◽  
Physico Chemical ◽  
Yellow Cattle ◽  
Mrna And Protein Expression ◽  
Sequence Encoding

Methylenetetrahydrofolate reductase (MTHFR), an enzyme expressed in mammalian testes exerts direct effect on spermatogenesis; however, its protein characteristics in bovine testes remain unknown. Here, we analysed bovine testicular structure, MTHFR bioinformatics profile, mRNA, and protein expression characteristics in yellow-cattle (y-c) and yak testis using histological procedures, bioinformatics analysis, qRT-PCR, and western blot. Testes from 13 bovines, ≤ 2 years juvenile (y-c, n = 3; yak, n=3) and ≥ 3 years adult (y-c, n = 3; yak, n = 4) were collected and analysed. Anatomical characteristics of testis in y-c and yak were similar except the weight or size for which that of y-c was significantly higher or greater than yak. In y-c, an open reading frame (ORF) for 2600 nucleotides sequence, encoding 655 amino acids showed high homology with zebu cattle (99.51%) and wild yak (98.68%). Secondary and 3D protein structures were similar to that of humans with differences in number of nucleotides, amino acids, and some physico-chemical characteristics. MTHFR mRNA expression in y-c and yak were significantly higher in adult testes compared with juvenile ones. However, its protein expression was higher but not statistically significant in adult y-c and yak compared to the juvenile ones. The highlights and inferences of these and other findings are discussed.

scholarly journals Cloning and Expression Analysis of Two Kdm Lysine Demethylases in the Testes of Mature Yaks and Their Sterile Hybrids

Animals ◽  
2020 ◽  
Vol 10 (3) ◽  
pp. 521
Author(s):  
Zhenhua Shen ◽  
Lin Huang ◽  
Suyu Jin ◽  
Yucai Zheng
Keyword(s):  
Amino Acids ◽  
Protein Expression ◽  
Male Sterility ◽  
Histone Methylation ◽  
Real Time Pcr ◽  
Cloning And Expression ◽  
Rt Pcr ◽  
Coding Sequences ◽  
Mrna And Protein Expression ◽  
Sterile Hybrids

The objective of this study was to explore the molecular mechanism for male sterility of yak hybrids based on two demethylases. Total RNA was extracted from the testes of adult yaks (n = 10) and yak hybrids (cattle–yaks, n = 10). The coding sequences (CDS) of two lysine demethylases (KDMs), KDM1A and KDM4B, were cloned by RT-PCR. The levels of KDM1A and KDM4B in yaks and cattle–yaks testes were detected using Real-time PCR and Western blotting for mRNA and protein, respectively. In addition, the histone methylation modifications of H3K36me3 and H3K27me3 were compared between testes of yaks and cattle–yaks using ELISA. The CDS of KDM1A and KDM4B were obtained from yak testes. The results showed that the CDS of KDM1A exhibited two variants: variant 1 has a CDS of 2622 bp, encoding 873 amino acids, while variant 2 has a CDS of 2562 bp, encoding 853 amino acids. The CDS of the KDM4B gene was 3351 bp in length, encoding 1116 amino acids. The mRNA and protein expression of KDM1A and KDM4B, as well as the level of H3K36me3, were dramatically decreased in the testes of cattle–yaks compared with yaks. The present results suggest that the male sterility of cattle–yaks might be associated with reduced histone methylation modifications.

The effect of miR-6523a on growth hormone secretion in pituitary cells of Yanbian yellow cattle

2020 ◽  
Vol 100 (4) ◽  
pp. 657-664
Author(s):  
Jiuxiu Ji ◽  
Taihua Jin ◽  
Rui Zhang ◽  
Angang Lou ◽  
Yingying Chen ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Protein Expression ◽  
Luciferase Reporter ◽  
Control Group ◽  
Pituitary Cells ◽  
Expression Levels ◽  
Gh Secretion ◽  
Yellow Cattle ◽  
Mrna And Protein Expression ◽  
In Cells

Yanbian yellow cattle breeding is limited by its slow growth. We previously found that the miRNA miR-6523a is differentially expressed between Yanbian yellow cattle and Han Yan cattle, which differ in growth characteristics. In this study, we evaluated the effects of miR-6523a on growth hormone (GH) secretion in pituitary cells of Yanbian yellow cattle. Bioinformatics analyses using TargetScan and RNAhybrid, as well as dual luciferase reporter assays, showed that miR-6523a targets the 3′ untranslated region of somatostatin receptor 5 (SSTR5). We further found that the mRNA and protein expression levels of GH in pituitary cells were significantly higher in cells treated with miR-6523a mimic than in the control group (P = 0.0082 and P = 0.0069). The GH mRNA and protein expression levels were lower in cells treated with miR-6523a inhibitor than in the control group, but the difference was not significant (P = 0.064 and P = 0.089). SSTR5 mRNA and protein levels were inhibited by miR-6523a mimic compared with the control group (P = 0.0024 and P = 0.0028) and were elevated slightly by miR-6523a inhibitor (P = 0.093 and P = 0.091). These results prove that miR-6523a regulates GH secretion in pituitary cells by SSTR5. More broadly, these findings provide a basis for studies of the roles of miRNAs in animal growth and development.

Structure and expression of a tandem gene pair in Leishmania donovani that encodes a protein structurally homologous to eucaryotic cation-transporting ATPases

1987 ◽  
Vol 7 (11) ◽  
pp. 3937-3946
Author(s):  
J C Meade ◽  
J Shaw ◽  
S Lemaster ◽  
G Gallagher ◽  
J R Stringer
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Tandem Repeat ◽  
Base Pair ◽  
Leishmania Donovani ◽  
Oligonucleotide Probe ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Atpase Gene ◽  
Sequence Encoding

An oligonucleotide probe was used to clone a cation-transporting ATPase gene from the genome of Leishmania donovani. The nucleotide sequence of the gene contained a 2,922-base-pair open reading frame that was predicted to encode a 107,406-dalton protein composed of 974 amino acids. The predicted L. donovani protein contained all the structural and functional domains expected to be present in a cation-transporting ATPase of the aspartyl phosphate class. The nucleotide sequence encoding the ATPase gene was duplicated in tandem in the parasite genome. Partial sequenation of the second member of the tandem repeat, which lay 2 kilobase pairs downstream of the ATPase gene, indicated that it was either identical to the first gene or very closely related to it. RNA homologous to either the ATPase gene or its adjacent relative was 5 kilobases in size and was approximately equally abundant in both promastigote and amastigote forms of the organism.

Cloning and sequence analysis of a cDNA encoding an androgen-dependent mouse seminal vesicle secretory protein

1993 ◽  
Vol 10 (3) ◽  
pp. 279-288 ◽  
Author(s):  
C Guilbaud ◽  
A M Simon ◽  
G Veyssière ◽  
C Jean
Keyword(s):  
Amino Acids ◽  
Seminal Vesicle ◽  
Cdna Sequence ◽  
Northern Blot Analysis ◽  
Secretory Protein ◽  
Calculated Molecular Mass ◽  
Reading Frame ◽  
The Family ◽  
Sequence Encoding ◽  
High Degree

ABSTRACT We report the cloning and sequencing of a new cDNA sequence encoding a protein from the mouse seminal vesicle. An open reading frame of 297 nucleotides encoded a protein of 99 amino acids with a calculated molecular mass of 11·454 kDa. The first 21 amino acids constituted a signal peptide followed by 78 amino acids encoding the secreted protein. The cDNA sequence comprised a 3′ untranslated region of 226 bp and the polyadenylation signal AATAAA, 19 bp upstream from the poly(A)+ tail. A high degree of homology was found between this protein and members of the family of seminal vesicle secretory (SVS) proteins, especially rat SVS VI. Northern blot analysis indicated the presence of a 0·7 kb mRNA species in the mRNAs of seminal vesicle tissue. Castration resulted in a marked decrease in the level of the 0·7 kb mRNA encoding the protein, whereas administration of testosterone to castrated males restored the 0·7 kb mRNA.

scholarly journals Structure and expression of a tandem gene pair in Leishmania donovani that encodes a protein structurally homologous to eucaryotic cation-transporting ATPases.

1987 ◽  
Vol 7 (11) ◽  
pp. 3937-3946 ◽  
Author(s):  
J C Meade ◽  
J Shaw ◽  
S Lemaster ◽  
G Gallagher ◽  
J R Stringer
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Tandem Repeat ◽  
Base Pair ◽  
Leishmania Donovani ◽  
Oligonucleotide Probe ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Atpase Gene ◽  
Sequence Encoding

An oligonucleotide probe was used to clone a cation-transporting ATPase gene from the genome of Leishmania donovani. The nucleotide sequence of the gene contained a 2,922-base-pair open reading frame that was predicted to encode a 107,406-dalton protein composed of 974 amino acids. The predicted L. donovani protein contained all the structural and functional domains expected to be present in a cation-transporting ATPase of the aspartyl phosphate class. The nucleotide sequence encoding the ATPase gene was duplicated in tandem in the parasite genome. Partial sequenation of the second member of the tandem repeat, which lay 2 kilobase pairs downstream of the ATPase gene, indicated that it was either identical to the first gene or very closely related to it. RNA homologous to either the ATPase gene or its adjacent relative was 5 kilobases in size and was approximately equally abundant in both promastigote and amastigote forms of the organism.

CLASSIFICATIONS OF AMINO ACIDS IN PROTEINS BY THE SELF-ORGANIZING MAP

2005 ◽  
Vol 16 (10) ◽  
pp. 1609-1616 ◽  
Author(s):  
MOOKYUNG CHEON ◽  
MUYOUNG HEO ◽  
IKSOO CHANG ◽  
CHOONGRAK KIM
Keyword(s):  
Amino Acids ◽  
Secondary Structure ◽  
Protein Structures ◽  
Building Blocks ◽  
Side Chain ◽  
Self Organizing Map ◽  
Energy Parameters ◽  
Physico Chemical ◽  
Body Energy ◽  
Self Organizing

We present the clustering properties of amino acids, which are building blocks of proteins, according to their physico-chemical characters. To classify the 20 kinds of amino acids, we employ a Self-Organizing Map (SOM) analysis for the Miyazawa-Jernigan (MJ) pairwise-contact matrix, the Environment-dependent One-body energy Parameters (EOP) and the one-body energy parameters incorporating the Ramachandran angle information (EOPR) over the EOP in proteins. We provide the new result of the SOM clustering for amino acids based on the EOPR and compare that with those from the MJ and the EOP matrix. All three kinds of energy parameters capture the leading role played by the hydrophobicity and the hydrophilicity of amino acids in protein folding. Our SOM analysis generally illustrates that both the EOP and the EOPR can provide the collective clustering of amino acids by the side chain characteristics and the secondary structure information. However, EOP is better at classifying amino acids according to their side chain characteristics whereas EOPR is better with secondary structure. We show that the EOP and the EOPR matrix manifests more detailed physico-chemical classification of amino acids than those from the MJ matrix, which does not contain a local environmental information of amino acids in the protein structures.

Bone sialoprotein mRNA and protein expression in human multiple myeloma cell lines and patients

2000 ◽  
Vol 111 (4) ◽  
pp. 1118-1121 ◽  
Author(s):  
A. Bellahcene ◽  
I. Van Riet ◽  
C. de Greef ◽  
N. Antoine ◽  
M. F. Young ◽  
...  
Keyword(s):  
Multiple Myeloma ◽  
Protein Expression ◽  
Cell Lines ◽  
Myeloma Cell ◽  
Bone Sialoprotein ◽  
Multiple Myeloma Cell ◽  
Human Multiple Myeloma ◽  
Mrna And Protein Expression

Changes in mRNA and Protein Expression of Antioxidant Enzymes in Leukocytes of Children with Bronchial Asthma after Interval Hypoxic Training

2012 ◽  
Vol 3 (2) ◽  
pp. 125-134
Author(s):  
Klaudia V. Nesvitaylova ◽  
Olga A. Gonchar ◽  
Tatyana I. Drevitskaya ◽  
Ludmila P. Arabskaya ◽  
Mikhail M. Steshenko ◽  
...  
Keyword(s):  
Antioxidant Enzymes ◽  
Protein Expression ◽  
Bronchial Asthma ◽  
Hypoxic Training ◽  
Mrna And Protein Expression
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