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Trial record 6 of 19 for:    Sod1 | Motor Neuron Disease

Analysis of Post-Translational Modifications of a Critical Protein Implicated in Amyotrophic Lateral Sclerosis (SOD1)

The safety and scientific validity of this study is the responsibility of the study sponsor and investigators. Listing a study does not mean it has been evaluated by the U.S. Federal Government. Read our disclaimer for details.
 
ClinicalTrials.gov Identifier: NCT02228915
Recruitment Status : Completed
First Posted : August 29, 2014
Last Update Posted : October 17, 2018
Sponsor:
Information provided by (Responsible Party):
University of North Carolina, Chapel Hill

Tracking Information
First Submitted Date August 27, 2014
First Posted Date August 29, 2014
Last Update Posted Date October 17, 2018
Actual Study Start Date August 2014
Actual Primary Completion Date October 14, 2018   (Final data collection date for primary outcome measure)
Current Primary Outcome Measures
 (submitted: August 28, 2014)
Post-translational modifications (PTMs) of Cu/Zn superoxide dismutase 1 [ Time Frame: 6 months ]
Original Primary Outcome Measures Same as current
Change History Complete list of historical versions of study NCT02228915 on ClinicalTrials.gov Archive Site
Current Secondary Outcome Measures Not Provided
Original Secondary Outcome Measures Not Provided
Current Other Pre-specified Outcome Measures Not Provided
Original Other Pre-specified Outcome Measures Not Provided
 
Descriptive Information
Brief Title Analysis of Post-Translational Modifications of a Critical Protein Implicated in Amyotrophic Lateral Sclerosis
Official Title Analysis of Post-Translational Modifications of a Critical Protein Implicated in Amyotrophic Lateral Sclerosis
Brief Summary The purpose of this research study is to discover and quantitate the differences in post-translational modifications found in the Cu, Zn superoxide dismutase (SOD1) of patients with amyotrophic lateral sclerosis (ALS) as compared to healthy individuals. SOD1 is a known genetic cause of ALS. With certain mutations, SOD1 gains a toxic function which leads to motor neuron death.
Detailed Description Amyotrophic Lateral Sclerosis (ALS) is a devastating neurodegenerative disease in which mutations in human Cu, Zn Superoxide Dismutase (SOD1) have been identified as a cause of familial ALS (FALS) cases.1-2 It has been shown that mutant SOD1 develops a novel toxic function through experiments demonstrating that many disease mutants maintain enzymatic activity, SOD1-null mice do not exhibit ALS symptoms, and co-expressed wild type protein does not rescue the disease-state.7-11 The majority of cases, however, are not caused directly by mutations of SOD1, instead being caused by a poorly understood interplay of several genes as well as environmental factors, which is often referred to as sporadic ALS (SALS).3 It has been found that FALS and SALS share similar pathology. 4-6 The hSOD1 protein aggregates characteristic of FALS have also been found in SALS patients, furthering the evidence that hSOD1 has an important role in the etiology of ALS in sporadic ALS patients.16-19 The exact mechanism of SOD1-associated toxicity has not yet been elucidated though many disease mutants have been shown to destabilize the SOD1 dimer. In this study we aim to compare the levels of SOD1 post-tra slational modifications in ALS patients to levels in healthy donors and to determine if there are distinct patterns of protein glutathionylation or phosphorylation. Our overall goal is to elucidate a direct mechanism of toxicity in SALS as well as identify potentially critical triggers
Study Type Observational
Study Design Observational Model: Cohort
Time Perspective: Prospective
Target Follow-Up Duration Not Provided
Biospecimen Retention:   Samples With DNA
Description:
A portion of this sample will be stored for future use in study of ALS and how the critical protien affects the disease progression long term. This sample will be stored de-identified; therefore will not be linked to any identifying informaton about the subject. Sample will be stored at the UNC biophysics and Biochemistry lab indefinitely
Sampling Method Probability Sample
Study Population SALS patients SOD1 associated FALS patients Healthy control
Condition ALS
Intervention Not Provided
Study Groups/Cohorts Not Provided
Publications * Not Provided

*   Includes publications given by the data provider as well as publications identified by ClinicalTrials.gov Identifier (NCT Number) in Medline.
 
Recruitment Information
Recruitment Status Completed
Actual Enrollment
 (submitted: October 16, 2018)
21
Original Estimated Enrollment
 (submitted: August 28, 2014)
30
Actual Study Completion Date October 16, 2018
Actual Primary Completion Date October 14, 2018   (Final data collection date for primary outcome measure)
Eligibility Criteria

Inclusion Criteria:

  • SALS patients
  • SOD1 associated FALS patients
  • Healthy control

Exclusion Criteria: none

Sex/Gender
Sexes Eligible for Study: All
Ages 18 Years to 99 Years   (Adult, Older Adult)
Accepts Healthy Volunteers Yes
Contacts Contact information is only displayed when the study is recruiting subjects
Listed Location Countries United States
Removed Location Countries  
 
Administrative Information
NCT Number NCT02228915
Other Study ID Numbers 14-1780
Has Data Monitoring Committee No
U.S. FDA-regulated Product Not Provided
IPD Sharing Statement
Plan to Share IPD: Undecided
Responsible Party University of North Carolina, Chapel Hill
Study Sponsor University of North Carolina, Chapel Hill
Collaborators Not Provided
Investigators
Principal Investigator: Chafic Karam, MD University of North Carolina, Chapel Hill
Principal Investigator: Nikolay V Dokholyan, PhD UNC
PRS Account University of North Carolina, Chapel Hill
Verification Date November 2017