The function of PS integrins during Drosophila embryogenesis

Leptin, Maria; Bogaert, Tim Van den; Lehmann, Ruth; Wilcox, Michael

doi:10.1016/0092-8674(89)90243-2

Cited by 245 publications

(169 citation statements)

References 31 publications

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“…In the fly, βPS-deficient muscle cells fail to connect to the 'tendon' matrix and in the worm βpat3-deficient muscle cells fail to attach to the 'cuticle' basement membrane [53][54][55]. As a result, these muscles detach from the ECM upon their first contraction and round up.…”

Section: Integrin Function In Invertebratesmentioning

confidence: 99%

Integrins in regulation of tissue development and function

Danen¹,

Sonnenberg²

2003

The Journal of Pathology

229

173

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Cell adhesion is indispensable for embryonic development and for proper tissue function. In metazoans, integrins are the major adhesion receptors that connect cells to components of the extracellular matrix. Integrins are implicated in assembly of extracellular matrices, cell adhesion and migration on extracellular matrices, and in vertebrates (in which the integrin family has expanded) they can also mediate cell-cell adhesion. Furthermore, integrinmediated adhesion can modulate many different signal transduction cascades and support cell survival, proliferation, and influence the expression of differentiation-related genes. In this review we briefly explain how integrins can affect so many different aspects of cell behavior and discuss evidence for roles of integrins in tissue development, function, and disease.

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Section: Integrin Function In Invertebratesmentioning

confidence: 99%

Integrins in regulation of tissue development and function

Danen¹,

Sonnenberg²

2003

The Journal of Pathology

229

173

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show abstract

“…Integrins are cell surface receptors that mediate a number of biological processes including development, inflammation, tumour metastasis and wound healing, (Hynes, 1992). In Drosophila , two β integrins, β PS (Leptin et al ., 1989) and βν (Yee & Hynes, 1993), have been identified. β PS, encoded by the X-linked myospheroid ( mys ) gene (MacKrell et al ., 1988), appears to be the major integrin β subunit in flies.…”

Section: Introductionmentioning

confidence: 99%

Delayed behavioural aging and altered mortality in Drosophilaβ integrin mutants

et al. 2003

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SummaryThe genetic basis for aging is being intensely investigated in a variety of model systems. Much of the focus in Drosophila has been on the molecular-genetic determinants of lifespan, whereas the molecular-genetic basis for age-related functional declines has been less vigorously explored. We evaluated behavioural aging and lifespan in flies harbouring loss-of-function mutations in myospheroid , the gene that encodes β β β β PS, a β β β β integrin. Integrins are adhesion molecules that regulate a number of cellular processes and developmental events. Their role in aging, however, has received limited attention. We report here that age-related declines in locomotor activity are ameliorated and that mean lifespan is increased in myospheroid mutants. The delayed functional senescence and altered mortality in myospheroid flies are independent of changes in body size, reproduction or stress resistance. Our data indicate that functional senescence and age-dependent mortality are influenced by β β β β integrins in Drosophila .

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“…At that time, one could identify about ten distinct cated in cell migration (Armant et al, 1986;Boucaut et al, 1984), transmembrane signalling events (Clark and Brugge, vertebrate integrins ; there are now 21 known (Schwartz, 1992). Integrins are a family of heterodimeric transmembrane proteins 1995; Ruoslahti and Pierschbacher, 1987), differentiation (Leptin et al, 1989), response to hormones and growth factors formed by the non-covalent association of one polypeptide of 15 structurally related A subunits with one polypeptide of 8 (Ignotz and Massagué, 1987). In addition, integrins have been implicated in the attachment of certain bacteria and viruses to structurally related β subunits (Hynes, 1992).…”

mentioning

confidence: 99%

A plant surface protein sharing structural properties with animal integrins

Faïk

Labouré

Gulino

et al. 1998

European Journal of Biochemistry

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Using a polyclonal antibody (P23) generated against the human platelet integrin AIIbβ3 and a FITCconjugate secondary antibody, fluorescence is observed at the surface of protoplasts isolated from Arabidopsis thaliana and Rubus fruticosus. Arabidopsis thaliana cells grown in suspension culture containing P23 and glycylarginylglycylaspartylserine (GRGDS), a synthetic peptide containing the RGD sequence found in many extracellular matrix adhesive proteins demonstrated aberrant cell wall/plasma membrane interactions and organization. When glycoproteins from these plants, purified on a concanavalin A Sepharose 4B, were subjected to SDS/PAGE and Western blotting, under reduced and non-reduced conditions, immunoblots probed with P23 revealed bands in both species. A shift in electrophoretic mobility is observed to different apparent molecular mass when no reducing agent is present. When purified by immunoaffinity chromatography on anti-AIIbβ3 Sepharose or Sepharose linked to the synthetic peptide D-Arg-Gly-Asp-Trp, the major antigenic components detected migrate at 30 kDa and 60 kDa in the first experiment and 60 kDa in the second one. Only the 60-kDa component is immunodetected with antibodies specific for either the β3 platelet chain or the AIIb polypeptide, suggesting the presence of two polypeptides co-migrating. To address more precisely the structure of this complex in plants, competition assays were performed. A significant inhibition is observed with CS3 a monoclonal antibody that interacts with the complexed form AIIbβ3 but not the dissociated subunits. Further structural similarities with the animal AIIbβ3 complex is demonstrated with Western blotting detection after plant glycoproteins immunoprecipitation with CS3 in absence or presence of 5 mM EDTA to dissociate the complex. We also present data on the characterization of a polyclonal antibody, named AcAt2, raised against Arabidopsis glycocoproteins purified by affinity chromatography on a D-RGDW column and eluted with the same peptide, that specifically interacts with the animal AIIbβ3 receptor.

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The function of PS integrins during Drosophila embryogenesis

Cited by 245 publications

References 31 publications

Integrins in regulation of tissue development and function

Integrins in regulation of tissue development and function

Delayed behavioural aging and altered mortality in Drosophilaβ integrin mutants

A plant surface protein sharing structural properties with animal integrins

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