What question did this study set out to answer?

To investigate whether membrane-bound brain proteoglycans possess intrinsic receptor-like protein tyrosine phosphatase (PTPase) enzymatic activity.

October 31, 1994FEBS LettersOpen Access

Multiple receptor‐like protein tyrosine phosphatases in the form of chondroitin sulfate proteoglycan

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To investigate whether membrane-bound brain proteoglycans possess intrinsic receptor-like protein tyrosine phosphatase (PTPase) enzymatic activity.
Extracted postnuclear membrane fractions from the brains of 8-day-old rats.
Purified membrane-bound proteoglycan fractions using DEAE ion-exchange chromatography and cesium chloride density gradient centrifugation.
Assessed PTPase activity and identified enzyme-bearing core proteins through renaturation experiments.
Purified brain proteoglycan fractions demonstrated high specific PTPase activities with characteristic PTPase enzymatic properties.
Renaturation assays established that chondroitin sulfate proteoglycans with 380-kDa and 170-kDa core proteins harbored the PTPase activity.
The 380-kDa proteoglycan was identified as RPTP beta/zeta carrying the HNK-1 carbohydrate epitope.

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Implication

Biochemical analysis reveals protein tyrosine phosphatase activity in rat brain chondroitin sulfate proteoglycans, highlighting receptor phosphatase functions in neural tissue.

Cite This Study

Maeda et al. (1994) studied this question.

synapsesocial.com/papers/6a0ad8ec334bc3615daca4d2 https://doi.org/10.1016/0014-5793(94)01093-5

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Implication

Biochemical analysis reveals protein tyrosine phosphatase activity in rat brain chondroitin sulfate proteoglycans, highlighting receptor phosphatase functions in neural tissue.

Multiple receptor‐like protein tyrosine phosphatases in the form of chondroitin sulfate proteoglycan

Key Points

Discussion

Implication

Cite This Study

Multiple receptor‐like protein tyrosine phosphatases in the form of chondroitin sulfate proteoglycan

Key Points

Discussion

Implication

Cite This Study

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