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Article ; Online: Fibronectin isoforms in skeletal development and associated disorders.

Dinesh, Neha E H / Campeau, Philippe M / Reinhardt, Dieter P

American journal of physiology. Cell physiology

2022 Volume 323, Issue 2, Page(s) C536–C549

Abstract: The extracellular matrix is an intricate and essential network of proteins and nonproteinaceous components that provide a conducive microenvironment for cells to regulate cell function, differentiation, and survival. Fibronectin is one key component in ... ...

Abstract	The extracellular matrix is an intricate and essential network of proteins and nonproteinaceous components that provide a conducive microenvironment for cells to regulate cell function, differentiation, and survival. Fibronectin is one key component in the extracellular matrix that participates in determining cell fate and function crucial for normal vertebrate development. Fibronectin undergoes time-dependent expression patterns during stem cell differentiation, providing a unique stem cell niche. Mutations in fibronectin have been recently identified to cause a rare form of skeletal dysplasia with scoliosis and abnormal growth plates. Even though fibronectin has been extensively analyzed in developmental processes, the functional role and importance of this protein and its various isoforms in skeletal development remain less understood. This review attempts to provide a concise and critical overview of the role of fibronectin isoforms in cartilage and bone physiology and associated pathologies. This will facilitate a better understanding of the possible mechanisms through which fibronectin exerts its regulatory role on cellular differentiation during skeletal development. The review discusses the consequences of mutations in fibronectin leading to corner fracture type spondylometaphyseal dysplasia and presents a new outlook toward matrix-mediated molecular pathways in relation to therapeutic and clinical relevance.
MeSH term(s)	Cell Differentiation/genetics ; Extracellular Matrix/genetics ; Extracellular Matrix/metabolism ; Fibronectins/genetics ; Fibronectins/metabolism ; Humans ; Osteochondrodysplasias/genetics ; Osteochondrodysplasias/metabolism ; Protein Isoforms/genetics ; Protein Isoforms/metabolism
Chemical Substances	Fibronectins ; Protein Isoforms
Language	English
Publishing date	2022-06-27
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00226.2022
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Article: Fibrillin-1 and fibrillin-1-derived asprosin in adipose tissue function and metabolic disorders.

Muthu, Muthu L / Reinhardt, Dieter P

Journal of cell communication and signaling

2020 Volume 14, Issue 2, Page(s) 159–173

Abstract: The extracellular matrix microenvironment of adipose tissue is of critical importance for the differentiation, remodeling and function of adipocytes. Fibrillin-1 is one of the main components of microfibrils and a key player in this process. Furin ... ...

Abstract	The extracellular matrix microenvironment of adipose tissue is of critical importance for the differentiation, remodeling and function of adipocytes. Fibrillin-1 is one of the main components of microfibrils and a key player in this process. Furin processing of profibrillin-1 results in mature fibrillin-1 and releases the C-terminal propeptide as a circulating hunger hormone, asprosin. Mutations in the fibrillin-1 gene lead to adipose tissue dysfunction and causes Marfan syndrome, marfanoid progeroid lipodystrophy syndrome, and neonatal progeroid syndrome. Increased TGF-β signaling, altered mechanical properties and impaired adipogenesis are potential causes of adipose tissue dysfunction, mediated through deficient microfibrils. Circulating asprosin on the other hand is secreted primarily by white adipose tissue under fasting conditions and in obesity. It increases hepatic glucose production and drives insulin secretion and appetite stimulation through inter-organ cross talk. This review discusses the metabolic consequences of fibrillin-1 and fibrillin-1-derived asprosin in pathological conditions. Understanding the dynamic role of fibrillin-1 in the adipose tissue milieu and of circulating asprosin in the body can provide novel mechanistic insights into how fibrillin-1 may contribute to metabolic syndrome. This could lead to new management regimens of patients with metabolic disease.
Language	English
Publishing date	2020-04-12
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2299380-0
ISSN	1873-961X ; 1873-9601
ISSN (online)	1873-961X
ISSN	1873-9601
DOI	10.1007/s12079-020-00566-3
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Article ; Online: High-Fat Diet Has a Protective Sex-Dependent Effect on Aortic Aneurysm Severity in a Marfan Syndrome Mouse Model.

Lau, Cori / Muthu, Muthu L / Siddiqui, Iram Fatima / Li, Ling / Reinhardt, Dieter P

The Canadian journal of cardiology

2023 Volume 39, Issue 11, Page(s) 1553–1567

Abstract: Background: Marfan syndrome (MFS) is a genetic disorder caused by mutations in fibrillin-1 and is characterized by thoracic aortic aneurysms and other complications. Previous studies revealed sexual dimorphisms in formation of aortic aneurysm in ... ...

Abstract	Background: Marfan syndrome (MFS) is a genetic disorder caused by mutations in fibrillin-1 and is characterized by thoracic aortic aneurysms and other complications. Previous studies revealed sexual dimorphisms in formation of aortic aneurysm in patients with MFS. The current study aimed to investigate the combined role of a high-fat diet (HFD) and biological sex in aortic disease using the mgR/mgR MFS mouse model. Methods: Male and female mgR/mgR mice, as well as wild-type (WT) littermate mice, were fed a control diet (CD [10% fat]) or HFD (60% fat) from 4 to 12 weeks of age. Key aortic disease parameters analyzed included the diameter of the aortic wall; elastic fibre fragmentation; proteoglycan content; mRNA levels of Mmp12, Col1a1, Col3a1, and Fbn1; and fibrillin-1 deposition in the aortic wall. Results: HFD-fed female mgR/mgR mice had significantly reduced aortic diameters (35%), elastic fibre fragmentation (56%), pathologically enhanced proteoglycans (45%), and expression of Mmp12 (64%), Col1a1 (41%), and Col3a1 (43%) compared with male mgR/mgR mice on HFD. Fibrillin-1 deposition and Fbn1 mRNA levels were unaffected. The data reveal a protective effect of HFD in female mice. In contrast, CD did not exert any protective effects. Conclusions: This study demonstrates a specific sexual dimorphism in MFS mice, with HFD exerting an explicit protective effect on severity of aortic disease in female mice. These preclinical data may be useful for developing nutritional recommendations for individuals with MFS in the longer term.
MeSH term(s)	Humans ; Mice ; Male ; Female ; Animals ; Fibrillin-1/genetics ; Marfan Syndrome/complications ; Marfan Syndrome/genetics ; Diet, High-Fat/adverse effects ; Matrix Metalloproteinase 12 ; Aortic Aneurysm/genetics ; Aortic Aneurysm/prevention & control ; Aortic Aneurysm, Thoracic/etiology ; Aortic Aneurysm, Thoracic/genetics ; Aortic Diseases/complications ; RNA, Messenger ; Disease Models, Animal
Chemical Substances	Fibrillin-1 ; Matrix Metalloproteinase 12 (EC 3.4.24.65) ; RNA, Messenger
Language	English
Publishing date	2023-07-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	632813-1
ISSN	1916-7075 ; 0828-282X
ISSN (online)	1916-7075
ISSN	0828-282X
DOI	10.1016/j.cjca.2023.07.020
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Article ; Online: Male Marfan mice are predisposed to high-fat diet-induced obesity, diabetes, and fatty liver.

Tiedemann, Kerstin / Muthu, Muthu L / Reinhardt, Dieter P / Komarova, Svetlana V

American journal of physiology. Cell physiology

2022 Volume 323, Issue 2, Page(s) C354–C366

Abstract: Gene mutations in the extracellular matrix protein fibrillin-1 cause connective tissue disorders including Marfan syndrome (MFS) with clinical symptoms in the cardiovascular, skeletal, and ocular systems. Patients with MFS also exhibit alterations in ... ...

Abstract	Gene mutations in the extracellular matrix protein fibrillin-1 cause connective tissue disorders including Marfan syndrome (MFS) with clinical symptoms in the cardiovascular, skeletal, and ocular systems. Patients with MFS also exhibit alterations in adipose tissues, which in some individuals leads to lipodystrophy, whereas in others to obesity. We have recently demonstrated that fibrillin-1 regulates adipose tissue homeostasis. Here, we examined how fibrillin-1 abnormality affects metabolic adaptation to different diets. We used two MFS mouse models: hypomorph Fbn1<sup>mgR/mgR</sup> mice and Fbn1<sup>C1041G/+</sup> mice with a fibrillin-1 missense mutation. When Fbn1<sup>mgR/mgR</sup> mice were fed with high-fat diet (HFD) for 12 wk, male mice were heavier than littermate controls (LCs), whereas female mice gained less weight compared with LCs. Female Fbn1<sup>C1041G/+</sup> mice on an HFD for 24 wk were similarly protected from weight gain. Male Fbn1<sup>C1041G/+</sup> mice on an HFD demonstrated higher insulin levels, insulin intolerance, circulating levels of cholesterol, and high-density lipoproteins. Moreover, male HFD-fed Fbn1<sup>C1041G/+</sup> mice showed a higher liver weight and a fatty liver phenotype, which was reduced to LC levels after orchiectomy. Phosphorylation of protein kinase-like endoplasmic reticulum kinase (PERK) and the expression of sterol regulatory element-binding protein 1 (Srebp1) in livers of HFD-fed male Fbn1<sup>C1041G/+</sup> mice were elevated. In conclusion, the data demonstrate that male mice of both the MFS models are susceptible to HFD-induced obesity and diabetes. Moreover, male Fbn1<sup>C1041G/+</sup> mice develop a fatty liver phenotype, likely mediated by a baseline increased endoplasmic reticulum stress. In contrast, female MFS mice were protected from the consequence of HFD.
MeSH term(s)	Animals ; Diabetes Mellitus ; Diet, High-Fat/adverse effects ; Fatty Liver/genetics ; Female ; Fibrillin-1/genetics ; Insulins/genetics ; Male ; Marfan Syndrome/diagnosis ; Marfan Syndrome/genetics ; Marfan Syndrome/metabolism ; Mice ; Mutation ; Obesity/genetics
Chemical Substances	Fbn1 protein, mouse ; Fibrillin-1 ; Insulins
Language	English
Publishing date	2022-06-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00062.2022
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Article ; Online: Biophysical Techniques to Analyze Elastic Tissue Extracellular Matrix Proteins Interacting with ADAMTS Proteins.

Nelea, Valentin / Reinhardt, Dieter P

Methods in molecular biology (Clifton, N.J.)

2019 Volume 2043, Page(s) 213–235

Abstract: Multidomain matrix-associated zinc extracellular proteases ADAMTS and ADAMTS-like proteins have important biological activities in cells and tissues. Beyond their traditional role in procollagen and von Willebrand factor processing and proteoglycan ... ...

Abstract	Multidomain matrix-associated zinc extracellular proteases ADAMTS and ADAMTS-like proteins have important biological activities in cells and tissues. Beyond their traditional role in procollagen and von Willebrand factor processing and proteoglycan cleavage, ADAMTS/ADAMTSL likely participate in or at least have some role in ECM assembly as some of these proteins bind ECM proteins including fibrillins, fibronectin, and LTBPs. In this chapter, we present four biophysical techniques largely used for the characterization, multimerization, and interaction of proteins: surface plasmon resonance spectroscopy, dynamic light scattering, atomic force microscopy, and circular dichroism spectroscopy.
MeSH term(s)	ADAMTS Proteins/metabolism ; Circular Dichroism ; Dynamic Light Scattering ; Elastic Tissue/metabolism ; Extracellular Matrix Proteins/metabolism ; Humans ; Microscopy, Atomic Force ; Surface Plasmon Resonance
Chemical Substances	Extracellular Matrix Proteins ; ADAMTS Proteins (EC 3.4.24.-)
Language	English
Publishing date	2019-08-28
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-9698-8_18
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Article ; Online: Microfibril-associated glycoprotein 4 forms octamers that mediate interactions with elastogenic proteins and cells.

Wozny, Michael R / Nelea, Valentin / Siddiqui, Iram Fatima S / Wanga, Shaynah / de Waard, Vivian / Strauss, Mike / Reinhardt, Dieter P

Nature communications

2024 Volume 15, Issue 1, Page(s) 4015

Abstract: Microfibril-associated glycoprotein 4 (MFAP4) is a 36-kDa extracellular matrix glycoprotein with critical roles in organ fibrosis, chronic obstructive pulmonary disease, and cardiovascular disorders, including aortic aneurysms. MFAP4 multimerises and ... ...

Abstract	Microfibril-associated glycoprotein 4 (MFAP4) is a 36-kDa extracellular matrix glycoprotein with critical roles in organ fibrosis, chronic obstructive pulmonary disease, and cardiovascular disorders, including aortic aneurysms. MFAP4 multimerises and interacts with elastogenic proteins, including fibrillin-1 and tropoelastin, and with cells via integrins. Structural details of MFAP4 and its potential interfaces for these interactions are unknown. Here, we present a cryo-electron microscopy structure of human MFAP4. In the presence of calcium, MFAP4 assembles as an octamer, where two sets of homodimers constitute the top and bottom halves of each octamer. Each homodimer is linked together by an intermolecular disulphide bond. A C34S missense mutation prevents disulphide-bond formation between monomers but does not prevent octamer assembly. The atomic model, built into the 3.55 Å cryo-EM map, suggests that salt-bridge interactions mediate homodimer assembly, while non-polar residues form the interface between octamer halves. In the absence of calcium, an MFAP4 octamer dissociates into two tetramers. Binding studies with fibrillin-1, tropoelastin, LTBP4, and small fibulins show that MFAP4 has multiple surfaces for protein-protein interactions, most of which depend upon MFAP4 octamer assembly. The C34S mutation does not affect these protein interactions or cell interactions. MFAP4 assemblies with fibrillin-1 abrogate MFAP4 interactions with cells.
MeSH term(s)	Humans ; Fibrillin-1/metabolism ; Fibrillin-1/genetics ; Fibrillin-1/chemistry ; Tropoelastin/metabolism ; Tropoelastin/chemistry ; Tropoelastin/genetics ; Cryoelectron Microscopy ; Extracellular Matrix Proteins/metabolism ; Extracellular Matrix Proteins/chemistry ; Extracellular Matrix Proteins/genetics ; Protein Multimerization ; Protein Binding ; Models, Molecular ; Calcium/metabolism ; Mutation, Missense ; Microfibrils/metabolism ; Microfibrils/chemistry ; Microfibrils/ultrastructure ; HEK293 Cells ; Carrier Proteins ; Glycoproteins ; Adipokines
Chemical Substances	Fibrillin-1 ; Tropoelastin ; MFAP4 protein, human ; Extracellular Matrix Proteins ; FBN1 protein, human ; Calcium (SY7Q814VUP) ; Carrier Proteins ; Glycoproteins ; Adipokines
Language	English
Publishing date	2024-05-13
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-48377-z
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Article ; Online: Microfibril-associated disorders: fibrillinopathies.

Reinhardt, Dieter P

Journal of glaucoma

2014 Volume 23, Issue 8 Suppl 1, Page(s) S34–5

MeSH term(s)	Exfoliation Syndrome/metabolism ; Extracellular Matrix Proteins/metabolism ; Fibrillins ; Humans ; Marfan Syndrome/metabolism ; Microfibrils/physiology ; Microfilament Proteins/metabolism ; Signal Transduction
Chemical Substances	Extracellular Matrix Proteins ; Fibrillins ; Microfilament Proteins
Language	English
Publishing date	2014-10-01
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	913494-3
ISSN	1536-481X ; 1057-0829
ISSN (online)	1536-481X
ISSN	1057-0829
DOI	10.1097/IJG.0000000000000114
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Zs.A 3795: Show issues

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Book ; Thesis: Untersuchung über die Mechanismen von Thyroxineinfluss auf die Knochengeometrie der Rattentibia

Reinhardt, Dieter

1980

Author's details	vorgelegt von Dieter Reinhardt
Language	English
Publishing country	Germany
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Heidelberg, Univ., Diss, 1980
HBZ-ID	HT013755099
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Article ; Online: Fibrillin-1 Regulates Arteriole Integrity in the Retina.

Alonso, Florian / Li, Ling / Fremaux, Isabelle / Reinhardt, Dieter Peter / Génot, Elisabeth

Biomolecules

2022 Volume 12, Issue 10

Abstract: Fibrillin-1 is an extracellular matrix protein that assembles into microfibrils that provide critical functions in large blood vessels and other tissues. Mutations in the fibrillin-1 gene are associated with cardiovascular, ocular, and skeletal ... ...

Abstract	Fibrillin-1 is an extracellular matrix protein that assembles into microfibrils that provide critical functions in large blood vessels and other tissues. Mutations in the fibrillin-1 gene are associated with cardiovascular, ocular, and skeletal abnormalities in Marfan syndrome. Fibrillin-1 is a component of the wall of large arteries but has been poorly described in other vessels. We examined the microvasculature in the retina using wild type mice and two models of Marfan syndrome, Fbn1<sup>C1041G/+</sup> and Fbn1<sup>mgR/mgR</sup>. In the mouse retina, fibrillin-1 was detected around arterioles, in close contact with the basement membrane, where it colocalized with MAGP1. Both a mutation in fibrillin-1 or fibrillin-1 underexpression characteristically altered the microvasculature. In Fbn1<sup>C1041G/+</sup> and Fbn1<sup>mgR/mgR</sup> mice, arterioles were enlarged with reduced MAGP1 deposition and focal loss of smooth muscle cell coverage. Losartan, which prevents aortic enlargement in Fbn1<sup>C1041G/+</sup> mice, prevented smooth muscle cell loss and vessel leakiness when administrated in a preventive mode. Moreover, losartan also partially rescued the defects in a curative mode. Thus, fibrillin-1/MAGP1 performs essential functions in arteriolar integrity and mutant fibrillin-1-induced defects can be prevented or partially rescued pharmacologically. These new findings could have implications for people with Marfan syndrome.
MeSH term(s)	Mice ; Animals ; Fibrillin-1/genetics ; Marfan Syndrome/genetics ; Marfan Syndrome/complications ; Marfan Syndrome/metabolism ; Fibrillins ; Losartan ; Arterioles/metabolism ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Extracellular Matrix Proteins ; Retina/metabolism
Chemical Substances	Fibrillin-1 ; Fibrillins ; Losartan (JMS50MPO89) ; Microfilament Proteins ; Extracellular Matrix Proteins
Language	English
Publishing date	2022-09-20
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom12101330
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Article ; Online: Fibrillin-1 regulates white adipose tissue development, homeostasis, and function.

Muthu, Muthu L / Tiedemann, Kerstin / Fradette, Julie / Komarova, Svetlana / Reinhardt, Dieter P

Matrix biology : journal of the International Society for Matrix Biology

2022 Volume 110, Page(s) 106–128

Abstract: Fibrillin-1 is an extracellular glycoprotein present throughout the body. Mutations in fibrillin-1 cause a wide spectrum of type I fibrillinopathies, including Marfan syndrome characterized by clinical manifestations in adipose tissues, among others. ... ...

Abstract	Fibrillin-1 is an extracellular glycoprotein present throughout the body. Mutations in fibrillin-1 cause a wide spectrum of type I fibrillinopathies, including Marfan syndrome characterized by clinical manifestations in adipose tissues, among others. This study addresses the hypothesis that fibrillin-1 regulates adipocyte development and plays a vital role in adipose tissue homeostasis. We employed two mouse models - Fbn1
MeSH term(s)	Adipogenesis/genetics ; Adipose Tissue, White/metabolism ; Animals ; Female ; Fibrillin-1/genetics ; Fibrillin-1/metabolism ; Fibrillin-2 ; Fibrillins ; Homeostasis ; Male ; Marfan Syndrome/genetics ; Mice
Chemical Substances	Fbn1 protein, mouse ; Fibrillin-1 ; Fibrillin-2 ; Fibrillins
Language	English
Publishing date	2022-05-06
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1183793-7
ISSN	1569-1802 ; 0945-053X
ISSN (online)	1569-1802
ISSN	0945-053X
DOI	10.1016/j.matbio.2022.05.002
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