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Related Concept Videos

Mutations01:39

Mutations

Overview
Mutations01:35

Mutations

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...
Point and Frameshift Mutations01:30

Point and Frameshift Mutations

Point mutations are genetic alterations involving the change of a single nucleotide base pair in DNA. Depending on how the alteration affects protein synthesis, they can lead to various consequences.Point mutations fall into the following types:Silent mutations occur when a nucleotide change does not alter the amino acid sequence due to the redundancy of the genetic code. For instance, changing ACC to ACA still encodes threonine, leaving the protein function unaffected. This occurs because...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Phase II Reactions: Sulfation and Conjugation with α-Amino Acids01:19

Phase II Reactions: Sulfation and Conjugation with α-Amino Acids

Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme activation, sulfur...

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Related Experiment Video

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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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Function modification of SR-PSOX by point mutations of basic amino acids.

Weiwei Liu1, Lan Yin, Chunxia Chen

  • 1Department of Immunology, Tongji University School of Medicine, 1239 Siping Road, Shanghai, 200092, China.

Lipids in Health and Disease
|April 16, 2011
PubMed
Summary

Identifying key amino acids in SR-PSOX reveals how it drives atherosclerosis. Mutations in specific residues enhance modified low-density lipoprotein (LDL) uptake and bacterial binding, potentially contributing to disease development.

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Area of Science:

  • Cardiovascular Biology
  • Molecular Medicine
  • Immunology

Background:

  • Atherosclerosis (AS) involves macrophage foam cell formation via modified low-density lipoprotein (LDL) uptake mediated by scavenger receptors (SR).
  • SR-PSOX acts as both an SR for atherogenic lipoprotein/bacterial uptake and a chemokine for immune cell adhesion, playing a crucial role in AS pathogenesis.
  • Understanding SR-PSOX's function is key to developing AS therapies.

Purpose of the Study:

  • To identify critical basic amino acids within the chemokine domain of SR-PSOX responsible for its atherogenic functions.
  • To investigate how mutations in these amino acids affect SR-PSOX's scavenger and chemokine activities.
  • To elucidate the role of specific SR-PSOX residues in modified LDL and bacterial uptake and cell adhesion.

Main Methods:

  • Established a cell model for studying SR-PSOX functions.
  • Generated site-directed mutants of human SR-PSOX by replacing key basic amino acids (R62, R78, H80, R82, H85, K105, K119, H123) in the chemokine domain with alanine.
  • Assessed functional changes in oxLDL uptake, bacterial phagocytosis, and cell adhesion for each mutant.

Main Results:

  • Mutants H80A, H85A, and K105A exhibited significantly enhanced uptake of oxidized LDL (oxLDL) and bacterial phagocytosis compared to wild-type SR-PSOX.
  • Mutagenesis of these specific basic amino acids markedly reduced SR-PSOX-mediated cell adhesion.
  • All basic amino acids in the non-conservative region of the chemokine domain were found to be important for SR-PSOX's cell adhesion properties.

Conclusions:

  • Basic amino acid residues in the SR-PSOX chemokine domain are critical for its biological functions.
  • Mutations at H80, H85, and K105 enhance SR-PSOX binding to oxLDL and bacteria, suggesting a role in atherogenesis.
  • Targeting these basic amino acids offers a potential therapeutic strategy for mitigating atherosclerosis progression.