Midline fasciclin: ADrosophila fasciclin-I-related membrane protein localized to the CNS midline cells and trachea

Hu, Song; Sonnenfeld, Margaret; Stahl, Stephanie; Crews, Stephen T.

doi:10.1002/(sici)1097-4695(199804)35:1<77::aid-neu7>3.0.co;2-8

Cited by 39 publications

(34 citation statements)

References 44 publications

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“…In addition, mfas was expressed in the central nervous system (CNS; Fig. 4C, part III, parts g,h); previous analyses demonstrated that mfas is expressed on the midline neurons and glia in the embryo (Hu et al, 1998). At the level of resolution of our analysis, we are unable to detect expression differences between males and females in the CNS.…”

Section: Development 131 (9)contrasting

confidence: 58%

“…Of the 11 genes ultimately selected, 10 were significant for regulation by dsx according to one or both approaches. The exception was the male gene mfas, which Development 131 (9) Research article the forced-choice model found (though not with significance) more likely to be regulated by fru, and which is known to function in the central nervous system (Hu et al, 1998), as do the male-specific fru products. Having chosen a set of 11 genes, two female and nine male, we proceeded to determine their patterns of expression by in situ hybridization.…”

Section: Selecting Genes For Further Studymentioning

confidence: 95%

“…mfas encodes a protein containing fasciclin and β-Ig-H3 domains, which are thought to mediate cell adhesion (Hu et al, 1998). mfas transcript was detected in both sexes (although at higher levels in males than females) according to both microarray and RNA blot analyses, and was detected in the internal genitalia of both sexes.…”

Section: Development 131 (9)mentioning

confidence: 98%

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A genomic analysis ofDrosophilasomatic sexual differentiation and its regulation

et al. 2004

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2008components of sex-differential expression were determined, but regulation by the sex-determination hierarchy was not explored.Here, we identify genes that are expressed sex-differentially in somatic tissues of adults and regulated by the sex hierarchy. Using arrays that assay approximately one-third (4040) of Drosophila genes, we analyzed adults mutant for the regulatory genes transformer (tra), dsx and fru (Fig. 1). To select a small number of such genes for further study, we chose a conservative approach. Stringent statistical analysis of these data, combined with data from wild-type adults and adults that lack germline tissue (Arbeitman et al., 2002), identified 63 genes that are sex-differentially expressed in the adult soma and regulated by the somatic sex hierarchy. Additional selection criteria, and validation by RNA blot analysis, defined a set of 11 genes for further characterization. In situ hybridization revealed that sex-differential expression of all 11 genes is confined to the internal genitalia. Analysis of the regulation of these genes revealed that the sex hierarchy functions during development to specify their adult expression patterns, and that dsx probably functions in diverse ways to set their activities. Materials and methods Drosophila stocks Microarray experimentsMicroarray production, data acquisition and analysis were performed as described in (Arbeitman et al., 2002). Each hybridization was a comparison of one RNA sample to a reference sample that was comprised of RNA derived from whole animals representing all stages of the life-cycle. Normalization was calculated so that the average ratio of signals from the experimental and reference sample equalled one. Analyses were performed on log-transformed ratio values. In all cases, chromosomal males and females were sampled separately. The wild-type data set and tudor data set were described previously (Arbeitman et al., 2002); each time point was sampled in duplicate. The wild-type data set includes 0-to 24-hour-, 3-day-, 5-day-, 10-day-, 15-day-, 20-day-, 25-day-and 30-day-old adults. The tudor data set includes 0-to 24-hour-and 5-day-old adults. Microarray experiments on sex determination mutants tra 1 /Df(3L)stj7 (XX), fru 4-40 /fru p1 (XY) and Dsx D /dsx m+r15 (XX) were performed with four (tra and fru) or five (Dsx D ) replicates. Microarray experiments performed on dsx null mutants (dsx m+r15 /dsx d+r3 ) were sampled in duplicate.

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Section: Development 131 (9)contrasting

confidence: 58%

Section: Selecting Genes For Further Studymentioning

confidence: 95%

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A genomic analysis ofDrosophilasomatic sexual differentiation and its regulation

et al. 2004

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“…Periostin has been regarded as a member of the Fasciclin I family, including ␤ig-h3 (Skonier et al, 1992), Algal-CAM (Huber and Sumper, 1994), and midline fasciclin (Hu et al, 1998), mimicking a function of Fasciclin I. Periodontal fibroblasts, major component cells in the periodontal ligament, are able to differentiate into multiple types of cells such as cementoblasts and osteoblasts and appear to play an essential role in response to mechanical forces of the tooth and in repair of a damaged matrix (Lekic and McCulloch, 1996). Although the periodontal fibroblasts have been well-known to have high alkaline phosphatase activity, the periodontal ligament is never calcified under normal conditions.…”

Section: Discussionmentioning

confidence: 99%

“…regarded as a member of the Fasciclin I family, which includes ␤ig-h3 (Skonier et al, 1992), Algal-CAM (Huber and Sumper, 1994), and midline fasciclin (Hu et al, 1998), mimicking a function of Fasciclin I.…”

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confidence: 99%

Immunohistochemical localization of periostin in tooth and its surrounding tissues in mouse mandibles during development

et al. 2004

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Previous reports have shown expression of immunoreactivity for periostin, originally identified as osteoblastspecific factor-2, in the periosteum and periodontal ligament. However, the developmental changes in its expression and the detailed immunolocalization have remained veiled. The present study was undertaken to examine the spatiotemporal expression of this protein in teeth and their associated tissues of mice during development at light and electron microscopic levels. In tooth germs at cap stage, periostin immunoreactivity was recognizable in the interface between inner enamel epithelium and preodontoblasts as well as in the mesenchymal tissues around cervical loop. Dental follicles around tooth germs at bell stage localized periostin immunopositivity in addition to the immunopositive areas observed in cap-staged tooth germs, although the functional significance of periostin has remained unclear in tooth development. Furthermore, periostin immunoreactivity was also found in the alveolar bone surface. In the incisors of both 7-and 21-day-old mice, immunoreaction for periostin was discernible in the lingual periodontal ligament and labial fibrous tissue adjacent to the papillary layer. After postnatal day 7, immunoreaction for periostin came to be restricted to the fibrous bundles in the periodontal ligament in accordance with the organization of the periodontal fibers, indicating its localization matched the morphogenesis of the periodontal ligament. Immunoelectron microscopic observation of the mature periodontal ligament verified the localization of periostin between the cytoplasmic processes of periodontal fibroblasts and cementoblasts and the adjacent collagen fibrils. Our findings suggest that periostin is involved at the sites of the cell-to-matrix interaction, serving as adhesive equipment for bearing mechanical forces, including occlusal force and tooth eruption.

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Structural characterizations of human periostin dimerization and cysteinylation

Liu

Zhang

et al. 2018

FEBS Letters

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Human periostin plays a multifaceted role in remodeling the extracellular matrix milieu by interacting with other proteins and itself in both a heterophilic and homophilic manner. However, the structural mechanism for its extensive interactions has remained elusive. Here, we report the crystal structures of human periostin (EMI-Fas1 ) and its Cys60Ala mutant. In combination with multi-angle light-scattering analysis and biochemical assays, the crystal structures reveal that periostin mainly exists as a dimer in solution and its homophilic interaction is mainly mediated by the EMI domain. Furthermore, Cys60 undergoes cysteinylation as confirmed by mass spectroscopy, and this site hardly affects the homophilic interaction. Also, the structures yield insights into how periostin forms heterophilic interactions with other proteins under physiological or pathological conditions.

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Midline fasciclin: ADrosophila fasciclin-I-related membrane protein localized to the CNS midline cells and trachea

Cited by 39 publications

References 44 publications

A genomic analysis ofDrosophilasomatic sexual differentiation and its regulation

A genomic analysis ofDrosophilasomatic sexual differentiation and its regulation

Immunohistochemical localization of periostin in tooth and its surrounding tissues in mouse mandibles during development

Structural characterizations of human periostin dimerization and cysteinylation

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