Microfibril-Associated Glycoprotein-1 (MAGP-1) and Other Non-Fibrillin Macromolecules Which May Possess a Functional Association with the 10 nm Microfibrils

Gibson, Mark

doi:10.1007/978-1-4419-9013-6_14

Cited by 6 publications

(11 citation statements)

References 94 publications

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“…86 Although there is no evidence of a direct interaction between fibrillin and lysyl oxidase to date, it is plausible that interactions with fibrillin or other microfibrillar components might be important for elastogenesis. 70 Interestingly, ADAMTS10, 87 an extracellular matrix protease, is mutated in the autosomal recessive form of Weill-Marchesani syndrome (WMS). 88 The dominant form of WMS is caused by mutations in fibrillin-1, suggesting, perhaps, a potential interaction between ADAMTS10 and fibrillin-1.…”

Section: Microfibril-associated Proteinsmentioning

confidence: 99%

The molecular genetics of Marfan syndrome and related disorders

Robinson

Arteaga‐Solis

Baldock

et al. 2006

Journal of Medical Genetics

381

275

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Marfan syndrome (MFS), a relatively common autosomal dominant hereditary disorder of connective tissue with prominent manifestations in the skeletal, ocular, and cardiovascular systems, is caused by mutations in the gene for fibrillin-1 (FBN1). The leading cause of premature death in untreated individuals with MFS is acute aortic dissection, which often follows a period of progressive dilatation of the ascending aorta. Recent research on the molecular physiology of fibrillin and the pathophysiology of MFS and related disorders has changed our understanding of this disorder by demonstrating changes in growth factor signalling and in matrix-cell interactions. The purpose of this review is to provide a comprehensive overview of recent advances in the molecular biology of fibrillin and fibrillin-rich microfibrils. Mutations in FBN1 and other genes found in MFS and related disorders will be discussed, and novel concepts concerning the complex and multiple mechanisms of the pathogenesis of MFS will be explained.

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Section: Microfibril-associated Proteinsmentioning

confidence: 99%

The molecular genetics of Marfan syndrome and related disorders

Robinson

Arteaga‐Solis

Baldock

et al. 2006

Journal of Medical Genetics

381

275

View full text Add to dashboard Cite

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“…MAGP-1 was the first protein in this family to be characterized followed shortly thereafter by MAGP-2 [20]. Three other proteins, AMP [21], MFAP3 [22], and MAGP-36 [23], based on their small size and localization to microfibrils, were grouped together with the MAGPs as members of the MicroFibril-Associated Protein (MFAP) family.…”

Section: Magp Protein and Mfap Gene Family Nomenclaturementioning

confidence: 99%

“…Readers interested in an in-depth discussion of microfibril structure and the role of microfibrils in growth factor signaling should consult reviews by Cleary and Gibson [2], Sengle and Sakai [82, 83], and Ramirez et al [72, 84]. Reviews focused on the MAGPs, and other microfibrillar proteins can be found in [10, 20, 85, 86].…”

Section: Conclusion and Further Readingmentioning

confidence: 99%

Microfibril-associated glycoproteins MAGP-1 and MAGP-2 in disease

2018

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Microfibril-associated glycoproteins 1 and 2 (MAGP-1, MAGP-2) are protein components of extracellular matrix microfibrils. These proteins interact with fibrillin, the core component of microfibrils, and impart unique biological properties that influence microfibril function in vertebrates. MAGPs bind active forms of TGFβ and BMPs and are capable of modulating Notch signaling. Mutations in MAGP-1 or MAGP-2 have been linked to thoracic aneurysms and metabolic disease in humans. MAGP-2 has also been shown to be an important biomarker in several human cancers. Mice lacking MAGP-1 or MAGP-2 have defects in multiple organ systems, which reflects the widespread distribution of microfibrils in vertebrate tissues. This review summarizes our current understanding of the function of the MAGPs and their relationship to human disease.

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“…Finally, these microfibrillar components enable interactions with the surrounding ECM. MAGP-1 has been shown to interact with decorin, dermatan sulfate groups of proteoglycans, and collagen VI [90], and fibulins have been shown to impact elastin deposition and crosslinking by binding both LOX and tropoelastin [91]. Additionally, the microfibril scaffold has also been shown to sequester TGF-β and regulate its bioavailability and activity [92–94].…”

Section: Distribution Synthesis and Biological Roles Of The Elasticmentioning

confidence: 99%

“…For example, it is known that fibrillin-2 is found primarily in embryonic tissue, but fibrillin-1 is found primarily in adult tissue [58]. In addition, LTBP-1 has been found to associate with microfibrils in tendon and vascular tissues but is present in limited amounts in other tissues (e.g., skeletal muscle and lung) [90]. Tropoelastin precursors are laid down on microfibrillar pre-scaffolds to form amorphous deposits that grow radially and axially to form mature fibers.…”

Section: Considerations For Growing Tissue-type-specific Elastic Matrmentioning

confidence: 99%

Advances in biomimetic regeneration of elastic matrix structures

Balakrishnan

Bashur

Ramamurthi

2012

Drug Deliv. and Transl. Res.

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Elastin is a vital component of the extracellular matrix, providing soft connective tissues with the property of elastic recoil following deformation and regulating the cellular response via biomechanical transduction to maintain tissue homeostasis. The limited ability of most adult cells to synthesize elastin precursors and assemble them into mature crosslinked structures has hindered the development of functional tissue-engineered constructs that exhibit the structure and biomechanics of normal native elastic tissues in the body. In diseased tissues, the chronic overexpression of proteolytic enzymes can cause significant matrix degradation, to further limit the accumulation and quality (e.g., fiber formation) of newly deposited elastic matrix. This review provides an overview of the role and importance of elastin and elastic matrix in soft tissues, the challenges to elastic matrix generation in vitro and to regenerative elastic matrix repair in vivo, current biomolecular strategies to enhance elastin deposition and matrix assembly, and the need to concurrently inhibit proteolytic matrix disruption for improving the quantity and quality of elastogenesis. The review further presents biomaterial-based options using scaffolds and nanocarriers for spatio-temporal control over the presentation and release of these biomolecules, to enable biomimetic assembly of clinically relevant native elastic matrix-like superstructures. Finally, this review provides an overview of recent advances and prospects for the application of these strategies to regenerating tissue-type specific elastic matrix structures and superstructures.

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Microfibril-Associated Glycoprotein-1 (MAGP-1) and Other Non-Fibrillin Macromolecules Which May Possess a Functional Association with the 10 nm Microfibrils

Cited by 6 publications

References 94 publications

The molecular genetics of Marfan syndrome and related disorders

The molecular genetics of Marfan syndrome and related disorders

Microfibril-associated glycoproteins MAGP-1 and MAGP-2 in disease

Advances in biomimetic regeneration of elastic matrix structures

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