Related Experiment Video

Updated: Aug 10, 2026

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting
10:51

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting

Published on: April 10, 2014

Structural features of human memapsin 2 (beta-secretase) and their biological and pathological implications

Lin Hong1, Xiangyuan He, Xiangping Huang

  • 1Protein Studies Program, Oklahoma Medical Research Foundation, University of Oklahoma Health Science Center, Oklahoma City, Oklahoma 73104, USA.

Acta Biochimica Et Biophysica Sinica
|December 14, 2004
PubMed

Insights

Memapsin 2, an enzyme crucial for Alzheimer's disease (AD) pathogenesis, cleaves beta-amyloid precursor protein. Understanding its structure is key for developing effective AD inhibitor drugs.

Area of Science:

  • Biochemistry
  • Neuroscience
  • Pharmacology

Background:

  • Memapsin 2 (beta-secretase) initiates beta-amyloid precursor protein (APP) cleavage, producing amyloid-beta (Abeta).
  • Abeta accumulation is a key factor in Alzheimer's disease (AD) pathogenesis.
  • Memapsin 2 is a primary target for developing AD inhibitor drugs.

Purpose of the Study:

  • To discuss the structural features of memapsin 2.
  • To explore the implications of these features in the protease's physiological and pathological roles.

Main Methods:

  • Structural analysis of catalytic/specificity apparatus.
  • Analysis of transmembrane domain.
  • Analysis of cytosolic domain.

Main Results:

  • Detailed discussion of memapsin 2's structural components.
  • Exploration of how structural features influence enzyme function.
  • Consideration of structural implications for AD pathogenesis.

Conclusions:

  • Structural insights into memapsin 2 are vital for understanding its role in Alzheimer's disease.
  • Targeting memapsin 2's structural features offers a promising therapeutic strategy for AD.

More Related Videos

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry09:31

Visualization of Amyloid β Deposits in the Human Brain with Matrix-assisted Laser Desorption/Ionization Imaging Mass Spectrometry

Published on: March 7, 2019

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase11:57

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Published on: June 24, 2025

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
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.
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...