The synthesis and activity of tyrosinase during development of the frog Rana pipiens

Benson, Stephen C.; Triplett, Edward L.

doi:10.1016/0012-1606(74)90129-8

Cited by 29 publications

(2 citation statements)

References 18 publications

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“…Development of tyrosinase has been investigated only in amphibian embryos, where it is first synthesized at the early neurula stage immediately following the embryonic induction of the neural plate by the underlying chordamesoderm (Benson and Triplett, 1974). Developmental change in phenoloxidase activity in amphioxus was also studied biochemically and histochemically.…”

Section: Presence Antibacterial Action and Development Of Phenoloxidmentioning

confidence: 99%

Origin and Evolution of Chordates

Satoh¹,

Yasui²

2001

Zoological Science

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Section: Presence Antibacterial Action and Development Of Phenoloxidmentioning

confidence: 99%

Origin and Evolution of Chordates

Satoh¹,

Yasui²

2001

Zoological Science

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“…A very feeble tyrosinase activity has been found by polyacrylamide disc gel electrophoresis during development, from the first cleavage till muscular response stages, but none by spectrophotometer in the extracts of melanosomes until developmental stage 19 (Miranda et al, 1982). During Rana pipiens development the tyrosinase enzymatic activity gradually increase from the neural plate stage till stage 19 (heart beat) (Benson and Triplett, 1974, Gaulton and Triplett, 1983a, Gaulton and Triplett, 1983b).…”

Section: Introductionmentioning

confidence: 99%

Transcriptional analysis of tyrosinase gene expression during Bufo bufo development

Cesare

Bonfigli

Miranda

et al. 2019

Saudi Journal of Biological Sciences

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Tyrosinase (EC.1.14.18.1.) is a widespread enzyme, in the phylogenetic scale, that produces melanin, from bacteria to man, by using as substrates monophenols, o-diphenols and molecular oxygen. In this work we have confirmed and demonstrated that during Bufo bufo development tyrosinase activity and gene expression first occur at developmental stages 17–18 (tail bud-muscular response) as detected by a spectrophotometric assay and qRT-PCR. As expected, also during B. bufo development tyrosinase gene is expressed after the late gastrula (stage 12), differently from Rana pipiens development when tyrosinase mRNA appears at the neural plate stage and enzyme activity at stage 20 (gill circulation). We have cloned and sequenced the B. bufo tyrosinase cDNA in order to prepare B. bufo tyrosinase cDNA specific primers (forward and reverse). Tyrosinase mRNA cloning has been performed by using degenerate primers prepared according to the anuran tyrosinase gene sequence coding for the copper binding sites. The expressions of tyrosinase gene and enzymatic activity during B. bufo development support that until the developmental stage 17, embryo melanin is of maternal origin and at this stage can start embryo melanin synthesis. A correlation exists between tyrosinase expression and O2 consumption during B. bufo development.

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The effect of temperature on tyrosinase activity in Himalayan mouse skin

Kidson

Fabian

1981

J. Exp. Zool.

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The tyrosinase activity of Himalayan mouse skin homogenates was measured over a range of temperatures using two sensitive radiometric assay--namely, (1) the measurement of 14C-tyrosine incorporation into melanin, and (2) the measurement of 3HOH released as a by-product of 3H-tyrosine hydroxylation. Results show that Himalayan tyrosinase is maximally active at temperatures well below normal body temperature (15 degree C to 25 degree C). These results are in support of Danneel's visual observations ('41) that "ferment" activity of Himalayan rabbit skin is absent at temperatures above 25 degree C. Further results suggest the presence of a tyrosinase inhibitor in Himalayan mouse skin. First, removal of a low molecular weight fraction from Himalayan skin homogenates resulted in an increase in tyrosinase activity. Second, recombination of the low molecular weight fraction to the homogenate from which it was originally separated resulted in a decrease in tyrosinase activity when assayed at 37 degree C, but no decrease when assayed at 25 degree C. It is proposed that at the normal body temperature of 37 degree C, tyrosinase from Himalayan skin is strongly bound to an inhibitor. At lower body temperatures, the affinity of the enzyme for the inhibitor decreases, thus allowing the synthesis of melanin to increase. This change in affinity of the enzyme for the inhibitor could be regulated by temperature-induced conformational changes in either the enzyme or the inhibitor or both.

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The synthesis and activity of tyrosinase during development of the frog Rana pipiens

Cited by 29 publications

References 18 publications

Origin and Evolution of Chordates

Origin and Evolution of Chordates

Transcriptional analysis of tyrosinase gene expression during Bufo bufo development

The effect of temperature on tyrosinase activity in Himalayan mouse skin

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