2006
DOI: 10.1016/j.modgep.2006.01.007
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Tenectin, a novel extracellular matrix protein expressed during Drosophila melanogaster embryonic development

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Cited by 14 publications
(22 citation statements)
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“…2B) [27,29]. In tnc mutants, the hindgut tube diameter remains narrow, while overexpression of Tnc leads to diametric overexpansion in a dose-dependent fashion (Fig.…”
Section: A Non-chitinous Matrix Drives Diameter Expansion Of the Drosmentioning
confidence: 93%
“…2B) [27,29]. In tnc mutants, the hindgut tube diameter remains narrow, while overexpression of Tnc leads to diametric overexpansion in a dose-dependent fashion (Fig.…”
Section: A Non-chitinous Matrix Drives Diameter Expansion Of the Drosmentioning
confidence: 93%
“…After washing in PBS, the imaginal discs and the larval brains were incubated overnight at 4–8°C with primary antibodies diluted in PBS containing 5% normal goat serum, 0.1% Triton X-100, and 0.02% sodium azide. Primary antibodies were mouse anti-elav (1:1000; Developmental Studies Hybridoma Center, University Iowa) and anti-tenectin (1:4000; Fraichard et al, 2006). Detection of the different primary antibodies was carried out using alkaline phosphatase anti-rabbit (1:50, Sigma), AlexaFluor594 anti-mouse (1:200, Molecular Probes), and AlexaFluor488 anti-rabbit (1:50, Molecular Probes).…”
Section: Methodsmentioning
confidence: 99%
“…To analyze the role of tenebrin in development, we identified its homolog, tenectin , in Drosophila melanogaster and described its embryonic expression patterns (Fraichard et al, 2006). In this report we used tenectin dsRNA to generate tenectin mutants and find phenotypes in the adult wing and male genitalia.…”
Section: Introductionmentioning
confidence: 99%
“…These molecules include Thrombospondin (Tsp) (Adams et al, 2003), M-spondin (Mspo; a homologue of F-spondin/VSGP/Spon1) (Umemiya et al, 1997), Papilin (Ppn; an alternatively spliced, conserved, prominent constituent of BMs with thrombospondin type-1 domains and homologies to the carboxyterminal of ADAMTS group metalloproteases) (Campbell et al, 1987; Kramerova et al, 2003; Fessler et al, 2004), Multiplexin (Mp; a homologue of collagens XV and XVIII with an endostatin domain) (Meyer and Moussian, 2009; Momota et al, 2011), Faulty attraction (Frac; a protein rich in EGF-like and calcium-binding EGF domains, related to the Fibrillin and Fibulin protein families) (Miller et al, 2011), Tiggrin (Tig; containing unique N- and C-terminal domains and a central stretch of sixteen contiguous ~75 amino acid repeats, essentially modified through mucin-type O -glycosylation) (Fogerty et al, 1994; Bunch et al, 1998; Zhang et al, 2011), Tenectin (Tnc; containing a signal peptide, a RGD tripeptide, and a c-type von Willebrand Factor domain) (Fraichard et al, 2006), Glutactin (Glt; containing a catalytically inactive acetylcholine esterase domain) (Olson et al, 1990), Peroxidasin (Pxn, containing leucin rich and immuno globulin repeats, and a functional peroxidase domain) (Nelson et al, 1994), and MDP-1 (Macrophage-derived proteoglycan-1; potentially synonymous to Papilin) (Hortsch et al, 1998). Indications of a potential Drosophila Fibronectin (Gratecos et al, 1988) have not been confirmed by subsequent studies or genome annotations.…”
Section: Ecm Molecules In Drosophilamentioning
confidence: 99%