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Metamorphic Changes in Glycolipids and Myelin Proteins and 2′,3′-Cyclic Nucleotide 3′-Phosphohydrolase in Bullfrog and Axolotl Brains (1993)

Tamai, Yoichi ; Kojima, Hisako ; Saito, Shintaro ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Journal of neurochemistry 60 (1993), S. 0

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ISSN: 1471-4159

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: Abstract: The metamorphic changes in levels of glycolipids and myelin proteins and 2′,3′-cyclic nucleotide 3′-phosphohydrolase (CNP) in the brains of bullfrog tadpoles, adult frogs, and axolotls were investigated, with particular emphasis on myelin maturation. The concentrations of cerebroside. sulfatide, and galactosyldiacylglycerol gradually increased from the onset of prometamorphosis throughout the active metamorphic period and then greatly increased after metamorphosis was completed. The ratio of glucocerebroside to galactocerebroside increased greatly in the prometamorphic period and then rapidly decreased to the frog level during the climax period. The fatty acid compositions of cerebroside and sulfatide showed a developmental change, with 24:1 being more predominant in the later metamorphic stage. The proportion of hydroxy fatty acids increased up to the onset of the prometamorphic stage and thereafter remained constant at ∼ 50% of the total. The CNP activity remained unchanged throughout metamorphosis at 60% that in frog myelin and increased in the adult frog. The composition of tadpole myelin proteins remained constant during metamorphosis, with large basic protein being the most abundant, and in the frog, proteolipid protein and large basic protein were present in comparable amounts. The two adult forms of axolotl, i.e., the neotenous and metamorphosed forms, exhibited almost identical myelin constituents, and CNP activity in the neotenous form amounted to one-fifth that in the bullfrog. These results indicate that active biosynthesis of myelin marker components occurs as metamorphosis proceeds, but more pronounced changes of myelin components occur after metamorphosis is completed.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1471-4159.1993.tb13412.x

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Effects of hydrolase inhibitors on fertilization of sea urchins: I. Protease inhibitors (1979)

Hoshi, Motonori ; Moriya, Tsuneo ; Aoyagi, Takaaki ; [et al.]

New York, NY : Wiley-Blackwell

Gamete Research 2 (1979), S. 107-119

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ISSN: 0148-7280

Keywords: lysin ; protease inhibitor ; sea urchin ; vitelline coat ; fertilization ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology

Notes: To search the spermatozoa of sea urchins for their lysins, the eggs were inseminated in the presence of various protease inhibitors. Among them, two chymotrypsin-specific inhibitors, chymostatin and N-tosyl-L-phenylalanyl-chloro-methane, as well as p-nitrophenyl p′-guanidinobenzoate, inhibit fertilization of the sea urchins, Hemicentrotus pulcherrimus and Strongylocentrotus intermedius.A chymotrypsin-like protease is presumed to be a lysin of the sea urchins, since the inhibition of fertilization by chymostatin is remarkably diminished if the eggs are pretreated with trypsin or chymotrypsin to break the vitelline coat before insemination, and since N-tosyl-L-phenylalanyl-chloromethane, and p-nitrophenyl p′-guanidinobenzoate, as well as chymostatin, inhibit the fertilization.In all the sea urchins so far studied, elevation of fertilization envelopes is inhibited by leupeptin, antipain, soybean trypsin inhibitor, and p-nitrophenyl p′-guanidinobenzoate, all of which are potent trypsin inhibitors.Synthetic inhibitors have cytotoxic side effects on the eggs, but the microbial and plant inhibitors have no such effects.

Additional Material: 6 Ill.