. The Biological bulletin. Biology; Zoology; Marine biology. 216 D. MIKI ET Figure 4. In situ hybridization of the Mgfp-2 gene transcripts in the foot of Mytilus galloprovincialis. Hybridization was performed using the digoxigenin-labeled antisense-probe (A) and sense-probe (B) RNAs. Bar = 1 mm. nous core of the threads and the polyphenolic protein protecting it are secreted by the collagen gland and the accessory gland, respectively (Brown, 1952; Pujol, 1967; Vitellaro-Zuccarello, 1980, 1981). The distal plaque ma- trix of byssal threads consists of Mefp-2 (Rzepecki et al., 1992). The pl
. The Biological bulletin. Biology; Zoology; Marine biology. 216 D. MIKI ET Figure 4. In situ hybridization of the Mgfp-2 gene transcripts in the foot of Mytilus galloprovincialis. Hybridization was performed using the digoxigenin-labeled antisense-probe (A) and sense-probe (B) RNAs. Bar = 1 mm. nous core of the threads and the polyphenolic protein protecting it are secreted by the collagen gland and the accessory gland, respectively (Brown, 1952; Pujol, 1967; Vitellaro-Zuccarello, 1980, 1981). The distal plaque ma- trix of byssal threads consists of Mefp-2 (Rzepecki et al., 1992). The plaque matrix is formed by secretion from the phenol gland at the distal depression (Rzepecki et al., 1992), and Mefp-2 is detectable only in extracted foot tip (Waite, 1992). By comparing the location of the proteins and the sites of accumulation of the mRNA for the proteins, we con- clude that the expression sites are located around the veny tral groove in an arrangement appropriate for byssus for" mation (Fig. 5). Since Mgfp-2 was detected exclusively in the phenol gland in the previous study (Rzepecki et al., 1992), the phenol-gland-specific expression of Mgfp-2 gene was expected (Fig. 4). However, the very low level expres- sion of Mgfp-1 in the phenol gland was unexpected (Fig. 3) because it has been reported that an antibody to Mefp- 1 binds strongly to the phenol gland as well as to the accessory glands (Benedict and Waite, 1986) and that the phenol gland is an apparent site of Mefp-1 storage (Waite, 1983; Benedict and Waite, 1986). Furthermore, Mefp-1 has been isolated from dissected phenol glands as well as from the accessory gland (Waite, 1983, 1992). We thus interpret our results to suggest that the Mgfp-1 gene is transcribed in the accessory gland and the translated pro- tein is delivered to and stored in the phenol gland. We also postulate that Mgfp-1 and Mgfp-2 are synthesized as raw materials in the accessory and phenol glands, respec- tively, and that Mgfp-1
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