miR-378a Modulates Macrophages Phagocytosis and Differentiation through targeting CD47-SIRPα axis in Atherosclerosis.

08:00 EDT 31st March 2019 | BioPortfolio

Summary of "miR-378a Modulates Macrophages Phagocytosis and Differentiation through targeting CD47-SIRPα axis in Atherosclerosis."

Signal regulating protein alpha (SIRPa) is an essential signaling molecule that modulates inflammatory responses in macrophages. However, the regulation of SIRPs and its dynamic changes in macrophages under inflammatory stimulation in atherosclerosis remain uncertain. Objective The study aimed to identify the miRNAs that regulate SIRPa transcription and their roles in modulating phagocytosis, differentiation, and cholesterol efflux in macrophages.


Journal Details

This article was published in the following journal.

Name: Scandinavian journal of immunology
ISSN: 1365-3083
Pages: e12766


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Medical and Biotech [MESH] Definitions

A membrane glycoprotein and cell adhesion molecule expressed by LEUKOCYTES that contains multiple Ig-like domains. It is a ligand for LFA-1 (integrin alphaLbeta2) and integrin alpha-D/beta-2. Its interaction with LFA-1 may play a role in the PHAGOCYTOSIS of NEUTROPHILS by MACROPHAGES following APOPTOSIS.

T-cell differentiation antigens that serve as the receptors for the B7 antigen (ANTIGENS, CD80) which modulates T-cell lymphokine production.

A glycoprotein of MW 25 kDa containing internal disulfide bonds. It induces the survival, proliferation, and differentiation of neutrophilic granulocyte precursor cells and functionally activates mature blood neutrophils. Among the family of colony-stimulating factors, G-CSF is the most potent inducer of terminal differentiation to granulocytes and macrophages of leukemic myeloid cell lines.

Phenomenon of cell-mediated immunity measured by in vitro inhibition of the migration or phagocytosis of antigen-stimulated LEUKOCYTES or MACROPHAGES. Specific CELL MIGRATION ASSAYS have been developed to estimate levels of migration inhibitory factors, immune reactivity against tumor-associated antigens, and immunosuppressive effects of infectious microorganisms.

An abundant pulmonary surfactant-associated protein that binds to a variety of lung pathogens, resulting in their opsinization. It also stimulates MACROPHAGES to undergo PHAGOCYTOSIS of microorganisms. Surfactant protein A contains a N-terminal collagen-like domain and a C-terminal lectin domain that are characteristic of members of the collectin family of proteins.

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