Archenteron formation induced by ascorbate and α-ketoglutarate in sea urchin embryos kept in SO2−4-free artificial seawater

Mizoguchi, Hazime; Yasumasu, Ikuo

doi:10.1016/0012-1606(82)90245-7

Cited by 15 publications

(7 citation statements)

References 20 publications

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“…20). Many studies have demonstrated a correlation between spicule formation and collagen synthesis (6,7,(17)(18)(19)(20)(21)23).…”

Section: Discussionmentioning

confidence: 99%

“…According to the classical definition, collagen is a hot acid-extractable protein that contains hydroxyproline and hydroxylysine residues (1,12,27). Exposure of embryos to ''C-proline results in its incorporation into hot acid-extractable proteins that contain 14C-hydroxyproline residues (6,7,(17)(18)(19)(20)(21)23). The percentage ratio of 14C-hydroxyproline residues to 14C-proline residues is about 4% at most in sea urchin embryos ( 6, 7, 17-21,23), which is rnarkedly lower than in other organisms (2,3).…”

Section: Introductionmentioning

confidence: 99%

“…Despite all these lines of circumstantial evidence, no hydroxyproline residues have yet been found in sea urchin embryos, probably because of the low hydroxylation ratio (6,7,(17)(18)(19)(20)(21)23). However, recently proteins that cross-reacted with antibodies raised against mammalian collagens were found on the cell surface of sea urchin embryos in the blastula and pluteus stages (30).…”

Section: Introductionmentioning

confidence: 99%

“…In sea urchin embryos, collagen-like proteins are reported to be synthesized after the blastula stage (6, 7,[17][18][19][20][21]23). According to the classical definition, collagen is a hot acid-extractable protein that contains hydroxyproline and hydroxylysine residues (1,12,27).…”

Section: Introductionmentioning

confidence: 99%

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Synthesis of Collagen‐Like Proteins in Embryonic Organs of the Sea Urchin, Hemicentrotus pulcherrimus

1989

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In sea urchin embryos exposed to ''C-proline at 20°C for 3 hr at the gastrula, prism or pluteus stage, 14C-radioactivity was found in hot acid-extractable proteins, in which more than 4% of the radioactivity was detectable in hydroxyproline residues. In these embryos, 14C-radioactivity in collagen-like proteins was found in the archenteron, spicule and embryo-wall cells. The rate of synthesis of collagen-like proteins was highest in the archenteron in the mid-gastrula stage, in the embryo-wall cells in the prism stage and in the spicule in the pluteus stage. The rate of synthesis decreased in the archenteron and increased in ernbryo-wall cells in the period between the mid-and late-gastrula stages, when the rate of synthesis in the spicule was quite low. Thereafter, the rate decreased slightly in the embryo-wall cells, was maintained in archenteron and increased markedly in the spicule. The rates of synthesis of collagen-like proteins are high in these embryonic organs at stages at which development and growth respectively, occur in embryos. Therefore, synthesis of collagen-like proteins probably supports morphogenesis in these embryonic organs.

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“…20). Many studies have demonstrated a correlation between spicule formation and collagen synthesis (6,7,(17)(18)(19)(20)(21)23).…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Synthesis of Collagen‐Like Proteins in Embryonic Organs of the Sea Urchin, Hemicentrotus pulcherrimus

1989

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“…In embryos kept in SOg--free sea water, the rate of hydroxylation of proline residues in collagen is very low and gastrulation does not occur. However, in additions of ascorbate and a-ketoglutarate stimulate the hydroxylation of proline residues in collagen, and an archenteron, even though small, is formed in embryos kept in SOi--free sea water (1). Normal embryos at the swimming blastula stage developed into abnormal embryos with a large exogut when the hydroxylation of proline residues in collagen is stimulated by ascorbate and a-ketoglutarate (3).…”

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confidence: 99%

Effect of α,α′‐dipyridyl on Exogut Formation in Vegetalized Embryos of the Sea Urchin

Mizoguchi¹,

Yasumasu²

1983

Dev Growth Differ

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In presumptive vegetalized embryos, obtained by 3-hr treatment with chloramphenicol at the 16-32 cell stage, the rates of [14Clproline incorporation into the collagen fraction and production of the [14C]hydroxyproline residues increased during development between 16 hr (equivalent to mesenchyme blastula stage) and 40 hr (the early pluteus stage) after fertilization at 20°C. In presumptive vegetalized embryos, the radioactivity of [14C]hydroxyproline residues was higher at the mesenchyme blastula stage (16 hr after fertilization), but lower at the post-gastrula stage than in normal embryos. In normal embryos at the post-gastrula stage, [''C]hydroxyproline residues were mainly found in isolated spicules, and the amounts of [14C]hydroxyproline residues in other parts were much lower than in vegetalized embryos, which had few, if any, spicules. a, a'-Dipyridyl, an inhibitor of prolyl hydroxylase, inhibited the hydroxylation of [14C]proline residues in presumptive vegetalized and normal embryos, and blocked the formation of the archenteron and exogut.Previously, we reported that archenteron formation occurs in embryos in SOi--free sea water on addition of ascorbate and/or a-ketoglutarate (l), which are known to be activators of prolyl hydroxylase (2). In embryos kept in SOg--free sea water, the rate of hydroxylation of proline residues in collagen is very low and gastrulation does not occur. However, in additions of ascorbate and a-ketoglutarate stimulate the hydroxylation of proline residues in collagen, and an archenteron, even though small, is formed in embryos kept in SOi--free sea water (1). Normal embryos at the swimming blastula stage developed into abnormal embryos with a large exogut when the hydroxylation of proline residues in collagen is stimulated by ascorbate and a-ketoglutarate (3). In these embryos in the presence of ascorbate and aketoglutarate, as well as in normal blastulae, a, a '-dipyridyl, an inhibitor of prolyl hydroxylase (4), inhibits formation of the archenteron and hydroxylation of proline residues in collagen (1, 3). These observations (1, 3) suggest that archenteron formation is supported, in a part at least, by collagen synthesis.In vegetalized embryos, it is known that a large exogut is produced (5). Provided that archenteron formation is supported by the synthesis of collagen, the rate of its synthesis during archenteron formation in presumptive vegetalized embryos should be higher than in normal embryos. Preliminary work from our laboratory showed that the rate of hydroxylation of proline residues in collagen is higher in presumptive vegetalized embryos than in normal embryos during the blastula stage (3).In the present study, we measured the change in rate of hydroxylation of proline residues in collagen during development of presumptive vegetalized embryos. The effects of,&, a '-57

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Migration of Sea Urchin Primary Mesenchyme Cells

Solursh

1986

The Cellular Basis of Morphogenesis

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Archenteron formation induced by ascorbate and α-ketoglutarate in sea urchin embryos kept in SO2−4-free artificial seawater

Cited by 15 publications

References 20 publications

Synthesis of Collagen‐Like Proteins in Embryonic Organs of the Sea Urchin, Hemicentrotus pulcherrimus

Synthesis of Collagen‐Like Proteins in Embryonic Organs of the Sea Urchin, Hemicentrotus pulcherrimus

Effect of α,α′‐dipyridyl on Exogut Formation in Vegetalized Embryos of the Sea Urchin

Migration of Sea Urchin Primary Mesenchyme Cells

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