Microfibril Structure Masks Fibrillin-2 in Postnatal Tissues

Charbonneau, Noé L.; Jordan, C. Diana; Keene, Douglas R.; Lee-Arteaga, Sui; Dietz, Harry C.; Rifkin, Daniel B.; Ramirez, Francesco; Sakai, Lynn Y.

doi:10.1074/jbc.m109.087031

Cited by 47 publications

(53 citation statements)

References 28 publications

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“…However, distinct organ-specific functions appear to be determined by temporal and tissue-specific differences in gene expression rather than by distinct molecular interactions. For example, the early and specific expression of fibrillin-2 in the interdigital space (Charbonneau et al 2010) may explain the defect in limb patterning in FBN2-null mice, whereas the ubiquitous postnatal expression of FBN1, in contrast to FBN2, may explain defects in homeostasis found in FBN1-deficient mice. From the restricted localization and apparent transient temporal expression of fibrillin-3 in the TF-specialized perifollicular stroma, we predict that fibrillin-3 may be responsible for the regulation of BMPs and/or TGF-b in these TFs.…”

Section: Discussionmentioning

confidence: 99%

Fibrillins in Adult Human Ovary and Polycystic Ovary Syndrome: Is Fibrillin-3 Affected in PCOS?

Jordan

Bohling

Charbonneau

et al. 2010

J Histochem Cytochem.

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(LYS) S U M M A R Y Polycystic ovary syndrome (PCOS) is a common endocrinopathy in women of reproductive age. Although genetic linkage analyses have demonstrated a susceptibility locus for PCOS mapping to the fibrillin-3 gene, the presence of fibrillin proteins in normal and polycystic ovaries has not been characterized. This study compared and contrasted fibrillin-1, -2, and -3 localization in normal and polycystic ovaries. Immunohistochemical stainings of ovaries from 21 controls and 9 patients with PCOS were performed. Fibrillin-1 was ubiquitous in ovarian connective tissue. Fibrillin-2 localized around antral follicles and in areas of folliculolysis. Fibrillin-3 was present in a restricted distribution within the specialized perifollicular stroma of follicles in morphological transition from primordial to primary type [transitional follicles (TFs)]. Fibrillin-1 and -2 stainings of PCOS ovaries were similar to those of the controls. However, in eight of the nine PCOS ovaries, there was a decrease in the number of TFs associated with fibrillin-3, including no staining in five PCOS samples; decreased number of fibrillin-3-associated TFs/mm 2 was confirmed by quantitative analysis. Our findings support a role for fibrillin-3 in the pathogenesis of PCOS and suggest fibrillin-3 may function in primordial to primary follicle transition. We propose that loss of fibrillin-3 during folliculogenesis may be an important factor in PCOS pathogenesis. (J Histochem Cytochem 58:903-915, 2010)

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Section: Discussionmentioning

confidence: 99%

Fibrillins in Adult Human Ovary and Polycystic Ovary Syndrome: Is Fibrillin-3 Affected in PCOS?

Jordan

Bohling

Charbonneau

et al. 2010

J Histochem Cytochem.

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“…Fibrillin-2 may form the inner core of many fibrillin-1 containing microfibrils (Ref. 21). Although rarely detected in adult skin, fibrillin-2 expression can increase during wound healing and in sclerosis (Ref.…”

Section: Structural Molecules Elastinmentioning

confidence: 99%

Elastic fibres in health and disease

Baldwin

Simpson

Steer

et al. 2013

Expert Rev. Mol. Med.

243

158

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Elastic fibres are insoluble components of the extracellular matrix of dynamic connective tissues such as skin, arteries, lungs and ligaments. They are laid down during development, and comprise a cross-linked elastin core within a template of fibrillin-based microfibrils. Their function is to endow tissues with the property of elastic recoil, and they also regulate the bioavailability of transforming growth factor β. Severe heritable elastic fibre diseases are caused by mutations in elastic fibre components; for example, mutations in elastin cause supravalvular aortic stenosis and autosomal dominant cutis laxa, mutations in fibrillin-1 cause Marfan syndrome and Weill–Marchesani syndrome, and mutations in fibulins-4 and -5 cause autosomal recessive cutis laxa. Acquired elastic fibre defects include dermal elastosis, whereas inflammatory damage to fibres contributes to pathologies such as pulmonary emphysema and vascular disease. This review outlines the latest understanding of the composition and assembly of elastic fibres, and describes elastic fibre diseases and current therapeutic approaches.

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“…These antibodies have been characterized in detail elsewhere (Sakai et al, 1986;Charbonneau et al, 2003;Charbonneau et al, 2010).…”

Section: Experimental Procedures Proteins and Antibodiesmentioning

confidence: 99%

Fibrillin-3 expression in human development

et al. 2011

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Fibrillin proteins are the major components of extracellular microfibrils found in many connective tissues. Fibrillin-1 and fibrillin-2 are well studied and mutations in these proteins cause a number of fibrillinopathies including Marfan syndrome and congenital contractural arachnodactyly, respectively. Fibrillin-3 was more recently discovered and is much less well characterized. Fibrillin-1 is expressed throughout life, whereas fibrillin-2 and -3 are thought to be primarily present during development. Here, we report detailed fibrillin-3 expression patterns in early human development.A polyclonal antiserum against a C-terminal recombinant half of human fibrillin-3 was produced in rabbit. Anti-fibrillin-3 antibodies were affinity-purified and antibodies cross-reacting with the other fibrillins were removed by absorption resulting in specific anti-fibrillin-3 antibodies. Immunohistochemical analyses with these purified antibodies demonstrate that fibrillin-3 is temporally expressed in numerous tissues relatively evenly from the 6 th to the 12 th gestational week. Fibrillin-3 was found spatially expressed in perichondrium, perineurium, perimysium, skin, developing bronchi, glomeruli, pancreas, kidney, heart and testis and at the prospective basement membranes in developing epithelia and endothelia. Double immunohistochemical analyses showed that all fibrillins are globally expressed in the same organs, with a number of differences on the tissue level in cartilage, perichondrium and developing bronchi. These results suggest that fibrillin-3, compared to the other fibrillins, fulfills both overlapping and distinct functions in human development.

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Microfibril Structure Masks Fibrillin-2 in Postnatal Tissues

Cited by 47 publications

References 28 publications

Fibrillins in Adult Human Ovary and Polycystic Ovary Syndrome: Is Fibrillin-3 Affected in PCOS?

Fibrillins in Adult Human Ovary and Polycystic Ovary Syndrome: Is Fibrillin-3 Affected in PCOS?

Elastic fibres in health and disease

Fibrillin-3 expression in human development

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