High impact information on Cg25C

• Here, we show that the pre-invasive polar cells undergo an unusual and asymmetrical apical capping with major basement membrane proteins, including the two Drosophila Collagen IV alpha chains, Laminin A and Perlecan [1].
• Loss of svp function resulted in the loss of Adh transcript and a reduction of DCg1 expression specifically in the fat body [2].
• We discuss the possibility that gp125 is generated through the action of a hormonally controlled serine protease in a process that is necessary for disc morphogenesis [3].
• An apical surface glycoprotein, designated gp125 for its apparent molecular weight of 125,000, appears in Ca2(+)-free, ionic detergent extracts of imaginal discs of Drosophila melanogaster in response to the steroid hormone, 20-hydroxyecdysone (20-HE) [3].
• We have examined directly the expression of one collagen gene (DCg1) during Drosophila melanogaster embryogenesis by means of in situ hybridization [4].

Anatomical context of Cg25C

• In the absence of hemocytes migrating adjacent to the developing VNC, the extracellular matrix components Collagen IV, Viking and Peroxidasin are not deposited around this tissue [5].
• Type IV collagen, a major structural component of basement membrane, has been characterized only in vertebrates [6].
• The genes Adh (alcohol dehydrogenase) and DCg1 (type IV collagen) code for gene products involved in fat-cell metabolism and therefore serve as terminal fat-cell differentiation markers [2].
• The results clearly demonstrate that DCg1 is maternally expressed by follicle cells and that the collagen type IV chain produced is stockpiled in the growing oocyte [7].

Analytical, diagnostic and therapeutic context of Cg25C

• By means of immunocytochemistry with a battery of specific antibodies, we describe the expression of the collagen IV chain produced by the gene DCg1 during the two phases of Drosophila neurogenesis [8].

References