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Related Concept Videos

Parkinson Disease ll: Pathophysiology01:24

Parkinson Disease ll: Pathophysiology

Parkinson disease (PD) is a progressive neurodegenerative disorder primarily affecting movement, with additional non-motor features. Its pathophysiology involves complex interactions among genetic susceptibility, environmental exposures, and cellular dysfunction, including dopaminergic neuron loss, protein aggregation, and mitochondrial impairment.Selective NeurodegenerationA key feature is the degeneration of dopaminergic neurons in the substantia nigra pars compacta, leading to reduced...
Parkinson Disease l: Introduction01:24

Parkinson Disease l: Introduction

Parkinson’s disease is a chronic, progressive neurodegenerative disorder that primarily affects movement. It is characterized by motor symptoms such as resting tremors, muscle rigidity, bradykinesia (slowness of movement), and postural instability. Patients may notice hand tremors at rest, stiffness during movement, or a shuffling gait. In addition to motor features, non-motor symptoms include sleep disturbances, mood and behavioral changes, constipation, and cognitive impairment, all of which...
Neural Regulation01:37

Neural Regulation

Digestion begins with a cephalic phase that prepares the digestive system to receive food. When our brain processes visual or olfactory information about food, it triggers impulses in the cranial nerves innervating the salivary glands and stomach to prepare for food.
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...
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...

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Related Experiment Video

Updated: Jun 26, 2026

Metabolic Labeling of Leucine Rich Repeat Kinases 1 and 2 with Radioactive Phosphate
11:31

Metabolic Labeling of Leucine Rich Repeat Kinases 1 and 2 with Radioactive Phosphate

Published on: September 18, 2013

LRRK2 and neurodegeneration.

Gabriel Santpere1, Isidre Ferrer

  • 1Institut de Neuropatologia, IDIBELL-Hospital Universitari de Bellvitge, Universitat de Barcelona, Hospitalet de LLobregat, CIBERNED, Barcelona, Spain.

Acta Neuropathologica
|January 15, 2009
PubMed
Summary

Mutations in the leucine-rich repeat kinase 2 gene (LRRK2) cause Parkinson's disease. This study found full-length LRRK2 is not a major component of Lewy bodies or tau inclusions, suggesting truncated forms may be involved.

Area of Science:

  • Neuroscience
  • Genetics
  • Pathology

Background:

  • Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene are linked to inherited and sporadic Parkinson's disease (PD).
  • The neuropathology of LRRK2 mutations can include dopaminergic neuron loss and variable protein inclusions, not always alpha-synucleinopathy.
  • The precise role of LRRK2 in neurodegeneration and its presence in pathological inclusions remain debated.

Purpose of the Study:

  • To investigate the presence and form of LRRK2 protein in Lewy bodies and tau inclusions associated with neurodegenerative diseases.
  • To clarify discrepancies in previous studies regarding LRRK2 immunoreactivity in Lewy body diseases (LBDs) and Alzheimer's disease (AD).
  • To determine if full-length LRRK2 or other forms are responsible for observed immunoreactivity.

Main Methods:

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Assaying the Kinase Activity of LRRK2 in vitro
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Assaying the Kinase Activity of LRRK2 in vitro

Published on: January 18, 2012

Human Peripheral Blood Neutrophil Isolation for Interrogating the Parkinson's Associated LRRK2 Kinase Pathway by Assessing Rab10 Phosphorylation
12:49

Human Peripheral Blood Neutrophil Isolation for Interrogating the Parkinson's Associated LRRK2 Kinase Pathway by Assessing Rab10 Phosphorylation

Published on: March 21, 2020

Related Experiment Videos

Last Updated: Jun 26, 2026

Metabolic Labeling of Leucine Rich Repeat Kinases 1 and 2 with Radioactive Phosphate
11:31

Metabolic Labeling of Leucine Rich Repeat Kinases 1 and 2 with Radioactive Phosphate

Published on: September 18, 2013

Assaying the Kinase Activity of LRRK2 in vitro
06:09

Assaying the Kinase Activity of LRRK2 in vitro

Published on: January 18, 2012

Human Peripheral Blood Neutrophil Isolation for Interrogating the Parkinson's Associated LRRK2 Kinase Pathway by Assessing Rab10 Phosphorylation
12:49

Human Peripheral Blood Neutrophil Isolation for Interrogating the Parkinson's Associated LRRK2 Kinase Pathway by Assessing Rab10 Phosphorylation

Published on: March 21, 2020

  • Utilized three distinct anti-LRRK2 antibodies (NB-300-268, NB-300-267, AP7099b) for immunohistochemical analysis.
  • Examined brain tissue from patients with LBDs and tauopathies, as well as cultured cells.
  • Analyzed the molecular weight bands recognized by antibodies to differentiate between full-length LRRK2 and potential degradation products or related proteins.

Main Results:

  • Antibody-dependent variations in LRRK2 detection were observed, particularly concerning low molecular weight bands.
  • Full-length LRRK2 was found not to be a major component of Lewy bodies in LBDs or hyper-phosphorylated tau inclusions in AD and tauopathies.
  • Low molecular weight bands were present in cultured cells, suggesting they are not solely post-mortem artifacts.

Conclusions:

  • The discrepancies in LRRK2 detection in pathological inclusions are largely due to antibody choice and interpretation of low molecular weight bands.
  • Truncated forms of LRRK2 or related transcripts, rather than full-length protein, may account for LRRK2 immunoreactivity in neuronal inclusions.
  • This finding has implications for understanding LRRK2's role in the pathogenesis of Parkinson's disease and other neurodegenerative disorders.