Canada Spends Logo

Explore our Budget 2026 analysis

Grant: Operating Grant: Fall 2008 Priority Announcement (IMHA)

University of Manitoba

$100,000.00

Agrin-an integrated approach to analyze the structure-function relationship of a key organizer in the neuromuscular junction

FY 2008-09

Summary
Agrin is a proteinn that plays a key role in neuromuscular junction (NMJ) development. It is best known for its induction of the acetylcholine receptor (AChR) clustering at the muscle cell and the induction and maintenance of the postsynaptic apparatus. Agrin is an extracellular matrix protein, which is composed of more than 22 separate domains, undergoing a number of modifications during its maturation and which is target for alternative mRNA splicing at three sites. Agrin mediates cell adhesion via its N-terminal domain (NtA) and induces the aggregation of acetylcholine receptor (AchR) on the postsynaptic membranes of muscle cells via its C-terminal domains (LG1-3). Disorders involving agrin lead, in Western countries, to much suffering, and also expensive therapeutic costs associated with diseases such as muscular dystrophy. Disruption of the linkage between agrin and the basement membrane in the muscular dystrophy (MDC1A) can cause extensive muscle degeneration and impairment of nerve conduction. To improve this situation, basic as well as applied research in the many-layered aspects of extracellular matrices is necessary. The goal of this program is to study the structure, function and regulation of certain agrin domains in health and disease. To achieve this, a combination of structural and biophysical techniques together with biochemical-functional analysis will be performed. Structural information on target proteins in atomic detail obtained from this work will directly contribute to the development of new applications in biomedicine, basic and applied research. Understanding of target proteins and their active sites will guide the structure-based design of diagnostic and therapeutic strategies for the associated disorders.
Program
Operating Grant: Fall 2008 Priority Announcement (IMHA)
Location
Manitoba, Canada
Recipient Type
Academia
Type
Grant
Source
CIHR Funding Decisions Database

As published

Id
179206
Name
Stetefeld Joerg
Region
Manitoba
Country
Canada
Orgtype
Institution Paid; Research Institution
Instname2
Musculoskeletal Health and Arthritis
Theme2
Biomedical
Prcname2
Biochemistry & Molecular Biology - A
Projecttitle
Agrin-an integrated approach to analyze the structure-function relationship of a key organizer in the neuromuscular junction
Programtype2
Operating Grants
Orgnameinp2
University of Manitoba
Cihramount2
$100,000
Cihrequipment2
$0
Programname2
Operating Grant: Fall 2008 Priority Announcement (IMHA)
Keyworddelim
Agrin; Agrin-Laminin Interaction; Agrin-Matrixin Interaction; Alternative Mrna Splicing; Biochemistry; Biophysics
Abstract
Agrin is a proteinn that plays a key role in neuromuscular junction (NMJ) development. It is best known for its induction of the acetylcholine receptor (AChR) clustering at the muscle cell and the induction and maintenance of the postsynaptic apparatus. Agrin is an extracellular matrix protein, which is composed of more than 22 separate domains, undergoing a number of modifications during its maturation and which is target for alternative mRNA splicing at three sites. Agrin mediates cell adhesion via its N-terminal domain (NtA) and induces the aggregation of acetylcholine receptor (AchR) on the postsynaptic membranes of muscle cells via its C-terminal domains (LG1-3). Disorders involving agrin lead, in Western countries, to much suffering, and also expensive therapeutic costs associated with diseases such as muscular dystrophy. Disruption of the linkage between agrin and the basement membrane in the muscular dystrophy (MDC1A) can cause extensive muscle degeneration and impairment of nerve conduction. To improve this situation, basic as well as applied research in the many-layered aspects of extracellular matrices is necessary. The goal of this program is to study the structure, function and regulation of certain agrin domains in health and disease. To achieve this, a combination of structural and biophysical techniques together with biochemical-functional analysis will be performed. Structural information on target proteins in atomic detail obtained from this work will directly contribute to the development of new applications in biomedicine, basic and applied research. Understanding of target proteins and their active sites will guide the structure-based design of diagnostic and therapeutic strategies for the associated disorders.
Competitiondate
200809
Approvedterm2
1 yr 0 mth
Pinamesdelim
Stetefeld, Joerg
Approvedterm
1 an 0 mois
Cihrcontribution2
~ $100,000~ $0~