Abstract
Fibrillin-1 is a large extracellular matrix glycoprotein which assembles to form 10-12 nm microfibrils in extracellular matrix. Mutations in the human fibrillin-1 gene (FBN-1) cause the connective tissue disease Marfan syndrome and related disorders, which are characterised by defects in the skeletal, cardiovascular and ocular systems of the body. Fibrillin-1 has a striking modular organisation which is dominated by multiple tandem repeats of the calcium binding epidermal growth factor-like (cbEGF) domain. This review focuses on recent studies which have investigated the structural and functional role of calcium binding to cbEGF domains in fibrillin-1 and 10-12 nm microfibrils.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Calcium / metabolism
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Calcium Chloride / chemistry
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Calcium-Binding Proteins / chemistry
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Calcium-Binding Proteins / metabolism*
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Egtazic Acid
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Epidermal Growth Factor / chemistry
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Epidermal Growth Factor / genetics
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Extracellular Matrix Proteins / chemistry
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Extracellular Matrix Proteins / metabolism*
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Fibrillin-1
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Fibrillins
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Fibroblasts
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Humans
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Marfan Syndrome / genetics
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Microfibrils / chemistry
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Microfibrils / metabolism*
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Microfilament Proteins / chemistry
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Microfilament Proteins / genetics
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Microfilament Proteins / metabolism*
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Mutation
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Tandem Repeat Sequences
Substances
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Calcium-Binding Proteins
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Extracellular Matrix Proteins
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FBN1 protein, human
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Fibrillin-1
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Fibrillins
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Microfilament Proteins
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Egtazic Acid
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Epidermal Growth Factor
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Calcium Chloride
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Calcium