miR-204: Molecular Regulation and Role in Cardiovascular and Renal Diseases

The field of microRNA research has evolved from studies aiming to gauge the importance of microRNAs to those focusing on understanding a subset of specific microRNAs that have emerged as potent regulators of molecular systems and pathophysiological conditions. In this article, we review the molecular features and regulation of miR-204 and the growing body of evidence for an important role of miR-204 in the regulation of cardiovascular and renal physiology and pathophysiological processes. miR-204 exhibits a highly tissue-specific expression pattern, and miR-204 abundance is regulated by several transcriptional and posttranscriptional mechanisms. Strong evidence supports a role for miR-204 in attenuating pulmonary arterial hypertension and hypertensive and diabetic renal injury while promoting hypertension and endothelial dysfunction in a wide range of model systems. miR-204 may influence these disease processes by targeting several biological pathways in a tissue-specific manner. miR-204 is dysregulated in patients with cardiovascular and renal diseases. The unequivocal functional roles and clear clinical relevance indicate that miR-204 is a high-value microRNA in cardiovascular and renal diseases.

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Tissue Distribution of ACE2 Protein in Syrian Golden Hamster (Mesocricetus auratus) and Its Possible Implications in SARS-CoV-2 Related Studies

Frontiers in Pharmacology ◽

10.3389/fphar.2020.579330 ◽

2021 ◽

Vol 11 ◽

Author(s):

Voddu Suresh ◽

Deepti Parida ◽

Aliva P. Minz ◽

Manisha Sethi ◽

Bhabani S. Sahoo ◽

...

Keyword(s):

Expression Pattern ◽

Golden Hamster ◽

Expression Patterns ◽

Mesocricetus Auratus ◽

Syrian Golden Hamster ◽

Surface Epithelium ◽

Specific Expression ◽

Tissue Specific ◽

Tissue Specific Expression ◽

Specific Expression Pattern

The Syrian golden hamster (Mesocricetus auratus) has recently been demonstrated as a clinically relevant animal model for SARS-CoV-2 infection. However, lack of knowledge about the tissue-specific expression pattern of various proteins in these animals and the unavailability of reagents like antibodies against this species hampers these models’ optimal use. The major objective of our current study was to analyze the tissue-specific expression pattern of angiotensin-converting enzyme 2, a proven functional receptor for SARS-CoV-2 in different organs of the hamster. Using two different antibodies (MA5-32307 and AF933), we have conducted immunoblotting, immunohistochemistry, and immunofluorescence analysis to evaluate the ACE2 expression in different tissues of the hamster. Further, at the mRNA level, the expression of Ace2 in tissues was evaluated through RT-qPCR analysis. Both the antibodies detected expression of ACE2 in kidney, small intestine, tongue, and liver. Epithelium of proximal tubules of kidney and surface epithelium of ileum expresses a very high amount of this protein. Surprisingly, analysis of stained tissue sections showed no detectable expression of ACE2 in the lung or tracheal epithelial cells. Similarly, all parts of the large intestine were negative for ACE2 expression. Analysis of tissues from different age groups and sex didn’t show any obvious difference in ACE2 expression pattern or level. Together, our findings corroborate some of the earlier reports related to ACE2 expression patterns in human tissues and contradict others. We believe that this study’s findings have provided evidence that demands further investigation to understand the predominant respiratory pathology of SARS-CoV-2 infection and disease.

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Discovery of a Functional Retrotransposon of the Murine Phospholipid Hydroperoxide Glutathione Peroxidase: Chromosomal Localization and Tissue-Specific Expression Pattern

Genomics ◽

10.1006/geno.2001.6715 ◽

2002 ◽

Vol 79 (3) ◽

pp. 387-394 ◽

Cited By ~ 16

Author(s):

Carolin Boschan ◽

Astrid Borchert ◽

Christoph Ufer ◽

Bernd-Joachim Thiele ◽

Hartmut Kuhn

Keyword(s):

Glutathione Peroxidase ◽

Expression Pattern ◽

Chromosomal Localization ◽

Phospholipid Hydroperoxide Glutathione Peroxidase ◽

Specific Expression ◽

Tissue Specific ◽

Tissue Specific Expression ◽

Phospholipid Hydroperoxide ◽

Specific Expression Pattern

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The Arabidopsis L-Type Amino Acid Transporter 5 (LAT5/PUT5) Is Expressed in the Phloem and Alters Seed Nitrogen Content When Knocked Out

Plants ◽

10.3390/plants9111519 ◽

2020 ◽

Vol 9 (11) ◽

pp. 1519

Author(s):

Rowshon A. Begam ◽

Jayne D’Entremont ◽

Allen Good

Keyword(s):

Amino Acid ◽

Nitrogen Content ◽

Amino Acid Transport ◽

Amino Acid Transporter ◽

Acid Transport ◽

Specific Expression ◽

Tissue Specific ◽

Tissue Specific Expression ◽

Wide Range ◽

Acid Transporter

The Arabidopsis L-type Amino Acid Transporter-5 (LAT5; At3g19553) was recently studied for its role in developmental responses such as flowering and senescence, under an assumption that it is a polyamine uptake transporter (PUT5). The LATs in Arabidopsis have a wide range of substrates, including amino acids and polyamines. This report extensively studied the organ and tissue-specific expression of the LAT5/PUT5 and investigated its role in mediating amino acid transport. Organ-specific quantitative RT-PCR detected LAT5/PUT5 transcripts in all organs with a relatively higher abundance in the leaves. Tissue-specific expression analysis identified GUS activity in the phloem under the LAT5/PUT5 promoter. In silico analysis identified both amino acid transporter and antiporter domains conserved in the LAT5/PUT5 protein. The physiological role of the LAT5/PUT5 was studied through analyzing a mutant line, lat5-1, under various growth conditions. The mutant lat5-1 seedlings showed increased sensitivity to exogenous leucine in Murashige and Skoog growth medium. In soil, the lat5-1 showed reduced leaf growth and altered nitrogen content in the seeds. In planta radio-labelled leucine uptake studies showed increased accumulation of leucine in the lat5-1 plants compared to the wild type when treated in the dark prior to the isotopic feeding. These studies suggest that LAT5/PUT5 plays a role in mediating amino acid transport.

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Structural Studies on Different Ligand Binding Ability of Sialoadhesin Using Molecular Modeling Techniques

Asian Journal of Organic & Medicinal Chemistry ◽

10.14233/ajomc.2020.ajomc-p279 ◽

2020 ◽

Vol 5 (4) ◽

pp. 277-282

Author(s):

Madhumita Dandopath Patra

Keyword(s):

Molecular Modeling ◽

Stable Complex ◽

Free Energies ◽

Specific Expression ◽

Functional Roles ◽

Modeling Techniques ◽

Cell Type Specific Expression ◽

Cell Type Specific ◽

Specific Expression Pattern ◽

Inflammatory Macrophages

Siglecs are the major homologous subfamily of I-type lectins with an ability to recognize sialylated glycans. Siglecs are attractive therapeutic targets because of their endocytic properties, ability to modulate receptor signaling and cell-type specific expression pattern. Sialoadhesin (Sn/ Siglec-1/ CD169), a member of the Siglec family expressed on subsets of resident and inflammatory macrophages and involves in modulation of inflammation and immunity. In this work, 3-D structure of human Siglec-1 (hSiglec-1) was predicted based on X-ray crystallo-graphically determined structure of mouse Siglec-1[mSiglec-1(PDB ID: 1QFP)] using molecular modeling techniques. The structure of complexes in solution of hSiglec-1 with ligands, glycopeptide and 3′-sialyllactose were predicted using a novel docking technique comprising of repeated cycles of molecular dynamics and energy minimization. Calculation of the free energies of binding of complexes suggested that glycopeptide can form stable complex with dissociation constant value of 3.31 μM whereas complex formation of 3′-sialyllactose with the protein in aqueous medium is thermodynamically unfavorable. The structural analysis of theses complexes represent the functional recognition interactions of this protein with the bound sugar molecule and as such provide detailed information about functional roles of such sugar binding protein.

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