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Genetic analysis of chromosomal region 97D2-9 of Drosophila melanogaster (1993)

Knibb, Wayne R. ; Tearle, Richard G. ; Elizur, Abigail ; [et al.]

Springer

Molecular genetics and genomics 239 (1993), S. 109-114

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ISSN: 1617-4623

Keywords: Drosophila ; melanogaster ; rough ; 97D

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The rough homeobox gene of D. melanogaster is required for the correct patterning of the developing eye. The locus maps to cytological location 97D2-5, a region which has not been extensively characterised. As part of our genetic and molecular characterization of rough we carried out an EMS mutagenesis to generate mutants that map to the surrounding region, 97D2-9 which is deleted in Df(3R)ro-XB3. We have generated 1 visible and 13 lethal mutations which, together with the previously described Toll and ms(3)K10 loci, and other unpublished lethals, define nine complementation groups — four lethal, three semi-lethal, one visible and one male-sterile. In addition to rough, one other locus within this region, 1(3)97De, was shown to be required for formation of the normal pattern of photoreceptor cells in the compound eye.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00281608

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Antibodies specific for gp40 inhibit cell-cell adhesion by cross-linking the protein on the surface of Dictyostelium purpureum (1993)

Springer, Wayne R. ; Haywood-Reid, Patricia L.

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 53 (1993), S. 85-97

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ISSN: 0730-2312

Keywords: cellular slime mold ; cytoskeleton ; rounding ; filopodia ; glycocalyx ; flow cytometry ; immunogold ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: We have previously suggested a role for gp40 in cell-cell adhesion in Dictyostelium purpureum from the fact that antibodies specific for this protein inhibited adhesion in an in vitro assay [Springer: Dev Biol 133:447-455, 1989]. To further confirm this role mutants lacking the protein were isolated and characterized. To our surprise, the mutants had normal adhesive properties both in vitro and in situ. These results lead us to the conclusion that gp40 is not necessary for the cell-cell adhesions observed and may not be a molecule which directly participates in these adhesions. When studied further, we found that adhesion-inhibitory antibodies were only effective as divalent IgG. Monovalent Fab fragments of the same antibodies could not inhibit adhesion. The inhibitory antibodies also caused the cells to remain rounded and incapable of attaching to plastic surfaces. We conclude that when divalent antibodies specific for gp40 cross-link this protein on the cell surface a cytoskeletal change prevents them from attaching to substratum as well as to other cells, thereby inhibiting cell-cell adhesion. We suggest that an alternative mechanism for inhibition of cell-cell adhesion by divalent antibodies exists and should be considered before proposing a direct role for a protein in adhesion.

Additional Material: 5 Ill.