Basement membrane localization of Frem3 is independent of the Fras1/Frem1/Frem2 protein complex within the sublamina densa

Petrou, Petros; Pavlakis, Evangelos; Dalezios, Yannis; Chalepakis, Georges

doi:10.1016/j.matbio.2007.05.008

Cited by 32 publications

(64 citation statements)

References 18 publications

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“…The mouse head blebs phenotype is caused by mutations in Frem1 (Smyth et al, 2004), a related mesenchymally expressed, secreted, BM localized protein lacking the vWF and Furin domains and associated with an N-terminal lectin motif. Frem1 engages integrins av and a8 through an N-terminal RGD domain (Kiyozumi et al, 2005), and localizes to the fibrillar structures in the sub lamina densa but is also detected in the lamina lucida (Petrou et al, 2007b). Interestingly, mutations in humans FREM1 do not cause a ''classic'' Fraser Syndrome-like phenotype, despite the overt similarity with the other blebs mice.…”

Section: Fraser Syndromementioning

confidence: 98%

“…Further insights into the role of Fras1 have been provided by the cloning of the other blebs mutants. The myelencephalic blebs mutation affects Frem2, an epidermally expressed transmembrane protein containing CSPG and Calxb domains, whose ectodomain is also cleaved and which localizes to the sub lamina densa (Petrou et al, 2007b). A small proportion of FS mutations are found in FREM2, but they are missense as opposed to the primarily truncating mutations in FRAS1 (Jadeja et al, 2005).…”

Section: Fraser Syndromementioning

confidence: 99%

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Basement membranes in development and disease

Wiradjaja

DiTommaso

Smyth

2010

Birth Defects Research Pt C

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Basement membranes (BMs) are specializations of the extracellular matrix that act as key mediators of development and disease. Their sheet like protein matrices typically serve to separate epithelial or endothelial cell layers from underlying mesenchymal tissues, providing both a biophysical support to overlying tissue as well as a hub to promote and regulate cell-cell and cell-protein interactions. In the latter context, the BM is increasingly being recognized as a mediator of growth factor interactions during development. In this review, we discuss recent findings regarding the structure of the BM and its roles in mediating the normal development of the embryo, and we examine congenital diseases affecting the BM which impact embryonic development and health in later life.

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Section: Fraser Syndromementioning

confidence: 98%

Section: Fraser Syndromementioning

confidence: 99%

Basement membranes in development and disease

Wiradjaja

DiTommaso

Smyth

2010

Birth Defects Research Pt C

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“…Elegant biochemical studies have subsequently shown that Frem1, Frem2, and Fras1 form a ternary complex in vitro and that this complex is most probably required for normal epidermal adhesion in utero (Kiyozumi et al, 2006). It is unclear whether Frem3 is involved in this complex, but the gene's divergent expression and the normal localization of the protein in mice carrying mutations in the other three proteins suggest that it acts in an independent manner (Chiotaki et al, 2007;Petrou et al, 2007b). One way in which we can study the nature of the relationships between these genes and the pathology resulting from their loss is by comparing gene expression in mammals with other vertebrates.…”

Section: Introductionmentioning

confidence: 99%

Expression of the fras1/frem gene family during zebrafish development and fin morphogenesis

Gautier

Naranjo-Golborne

Taylor

et al. 2008

Developmental Dynamics

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Mouse studies have highlighted the requirement of the extracellular matrix Fras and Frem proteins for embryonic epidermal adhesion. Mutations of the genes encoding some of these proteins underlie the blebs mouse mutants, whereas mutations in human FRAS1 and FREM2 cause Fraser syndrome, a congenital disorder characterized by embryonic blistering and renal defects. We have cloned the zebrafish homologues of these genes and characterized their evolutionary diversification and expression during development. The fish gene complement includes fras1, frem1a, frem1b, frem2a, frem2b, and frem3, which display complex overlapping and complementary expression patterns in developing tissues including the pharyngeal arches, hypochord, musculature, and otic vesicle. Expression during fin development delineates distinct populations of epidermal cells which have previously only been described at a morphological level. We detect relatively little gene expression in epidermis or pronephros, suggesting that the essential role of these proteins in mediating their development in humans and mice is recently evolved. Developmental Dynamics 237:3295-3304, 2008.

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“…Fras1/Frem and collagen VII colocalize in the basement membrane of adult mouse tail skin Recent ultrastructural immunohistochemical experiments have shown that Fras1/Frem proteins are located in the sublamina densa of embryonic epithelial basement membranes (Petrou et al 2007b). The major structural hallmarks of the sublamina densa are the so-called anchoring Wbrils and anchoring plaques which are mainly composed of collagen VII (Tidman and Eady 1985;Keene et al 1987).…”

Section: Resultsmentioning

confidence: 99%

“…Furthermore, utilization of transmission electron microscopy to investigate the exact location of these proteins, revealed their colocalization in the sublamina densa of various embryonic epithelial basement membranes (Kiyozumi et al 2006;Petrou et al 2007b). Interestingly, individual Fras1/Frem proteins were detected as large clusters of immunogold often extending from the sublamina densa as far as the connective tissue cells (Dalezios et al 2007;Petrou et al 2007b).…”

Section: Introductionmentioning

confidence: 99%

Differential localization profile of Fras1/Frem proteins in epithelial basement membranes of newborn and adult mice

Pavlakis

Makrygiannis

Chiotaki

et al. 2008

Histochem Cell Biol

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The Fras1/Frem gene family encodes for structurally similar proteins of the extracellular matrix, functionally correlated with embryonic dermal-epidermal adhesion as deduced from the appearance of sub-epidermal blisters in mouse mutants compromising the function of Fras1, Frem1 and Frem2 proteins. Mutations in the human counterparts FRAS1 and FREM2 have been detected in patients suffering from Fraser syndrome. So far, Fras1/Frem proteins have been shown to be strictly colocalized in the sublamina densa of mouse epithelial basement membranes during development. Here, we focused on the characterization of the localization pattern of the aforementioned proteins, in various parts of the adult mouse skin as well as a range of organs and tissues. Frem3 was present in a broad range of epithelial basement membranes where Fras1, Frem1 and Frem2 were missing. The localization profile of Frem3 coincided with that of collagen VII in all skin basement membranes but differed in that Frem3 was additionally found in the basement membrane of several internal epithelia, where collagen VII was absent. Fras1 and Frem2 were colocalized with Frem3 in the basement membrane of certain skin parts, underlying the thin-layer, of rapidly proliferating keratinocytes, whereas Frem1 was detected only in the basement membrane of the tail. The localization pattern of Fras1 and Frem2 was indistinguishable, while both proteins along with Frem3 could be detected even in the absence of Frem1.

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Basement membrane localization of Frem3 is independent of the Fras1/Frem1/Frem2 protein complex within the sublamina densa

Cited by 32 publications

References 18 publications

Basement membranes in development and disease

Basement membranes in development and disease

Expression of the fras1/frem gene family during zebrafish development and fin morphogenesis

Differential localization profile of Fras1/Frem proteins in epithelial basement membranes of newborn and adult mice

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