The cuticle proteins of Drosophila melanogaster: Stage specificity

Chihara, Charles S.; Silvert, Donald J.; Fristrom, James W.

doi:10.1016/0012-1606(82)90326-8

Cited by 99 publications

(27 citation statements)

References 16 publications

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“…The Ceratitis set of pupal cuticle proteins is completely different from the larval one (Boccaccio and Quesada-Allu6, 1989a), in agreement with results from other flies (Chihara et al, 1982;Skelly and Howells, 1987). The main Ceratitis PCP-PCG-100-is glycosylated, and its carbohydrate chains seem to have a quite unusual composition, being a high mannose oligosaccharide that contains fucose (Boccaccio and Quesada, unpublished results).…”

Section: Discussionsupporting

confidence: 73%

Synthesis and deposition of PCG‐100, the main pupal cuticle glycoprotein of the medfly Ceratitis capitata

Boccaccio

Quesada-Allué

1994

Arch Insect Biochem Physiol

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W e have studied the developmental expression of the main pupal cuticle glycoprotein, PCG-100, in the Medfly Ceratitis capitata. A polyclonal antiserum was raised against this protein. Western blotting analysis showed that this glycoprotein is integument-and stage-specific. N o PCC-1 00 or immunologically related polypeptides were detected in other tissues or instars. As studied by microinjection of[35S]rnethionine in individual flies, in vivo synthesis and deposition of PCG-100 begins approximately 48 h after the onset of pupariation, shortly after the time of head eversion. Synthesis is maximal at 54-64 h, decreases at 72 h, and practically ceases in fully shaped 4-day-old pupae. The time required for PCG-100 deposition into the cuticle was found to be less than 1 0 min after its synthesis. This is the first time such in vivo analysis has been performed.

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Section: Discussionsupporting

confidence: 73%

Synthesis and deposition of PCG‐100, the main pupal cuticle glycoprotein of the medfly Ceratitis capitata

Boccaccio

Quesada-Allué

1994

Arch Insect Biochem Physiol

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“…We have no knowledge of the function of the conserved region(s), but assume that the sequence conservation is a requirement for deposition of the proteins within a highly ordered procuticular structural matrix. Immunological evidence also indicates evolutionary conservatism among cuticle proteins: antibody made against third-instar Drosophila LCPs cross-reacts with the first-and second-instar LCPs, the S-PCPs (but not the H-PCPs), and with the ACPs of Drosophila [9]. The Drosophila antibody also cross-reacts with cuticle proteins from Lucilia, Manduca, and Antheraea [Silvert and Fristrom, unpublished; personal communications from L. Riddiford, and S. Sridhara].…”

Section: Introductionmentioning

confidence: 91%

Ecdysone regulation of cuticle protein gene expression inDrosophila

Fristrom

Alexander

Brown

et al. 1986

Arch. Insect Biochem. Physiol.

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The deposition and apolysis of insect cuticles have long been known to be regulated by ecdysone. Unsclerotized, chitin-containing procuticles contain evolutionarily conserved, hydrophobic proteins that are soluble in solutions of denaturing agents. The pupal procuticle of Drosophila is deposited by larval and imaginal epidermis starting 9 h after puparium formation when the ecdysone titer is low. Initially, a set of low molecular weight proteins (less than 25,000 daltons; low molecular weight pupal cuticle proteins = S-PCPs) is synthesized. However, about the time of pupation, synthesis of S-PCPs ceases, and high molecular weight proteins (greater than 50,000 daltons; HPCPs) are synthesized. In vitro experiments indicate that the initial formation of the procuticle with synthesis of the S-PCPs requires a pulse of hormone followed by withdrawal (6 h with 20-hydroxyecdysone, 1 pg/ml). The switch from synthesis of S-PCPs to H-PCPs is facilitated by a second, short pulse of 20-hydroxyecdysone (0.1 pglml, 3 h). Ultrastructural localization demonstrates that the S-PCPs are located only in the external lamellae of the procuticle, while the H-PCPs are present only in internal lamellae. Developmental analyses with cloned genes indicate that cuticle protein genes are expressed during only one stage of Drosophila development. Some of the genes encoding S-PCPs are limited in their expression to larval (posterior) or imaginal (anterior) epidermis. Preliminary molecular analyses of the larval and pupal cuticle protein genes indicate that they are organized in different ways. For example, four larval genes exist in a cluster with divergent transcription, and one PCP gene, PCP-CART, is located within an intron of a "housekeeping" gene.

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“…The cuticle is mainly composed of chitin, a polymer of N-acetylglucosamine (GlcNAc), and cuticle proteins, which are structural proteins binding to chitin and/or other proteins. The composition of cuticle proteins varies with the mechanical properties of the cuticle (Chihara et al, 1982;Cox and Willis, 1985;Andersen and Hojrup, 1987;Nakato et al, 1990). Therefore, it is believed that cuticle proteins have important roles in the expression of cuticle mechanical properties.…”

Section: Introductionmentioning

confidence: 99%