Histochemically demonstrable phosphotyrosine protein phsophatase in the rat hippocampal formation

Yoshioka, Takafumi; Tanaka, Osamu; Otani, Hiroki; Shinohara, Haruo

doi:10.1016/0006-8993(91)90877-x

Cited by 7 publications

(4 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…PTPase 1 is strongly expressed in the hippocampus [16], a region of the brain known to be important ha long-term potentiation and memory. In-situ staining fur PTPase activity ha the brain using o-phoxpho-L-t3~a~ine as a substrate [56] confirmed that the hippocampus is a region of the brain rich in PTPases.…”

Section: L Mulecular Mele~ Ef the Ptpusesmentioning

confidence: 84%

A thousand and two protein tyrosine phosphatases

Pot¹,

Dixon²

1992

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

123

View full text Add to dashboard Cite

Section: L Mulecular Mele~ Ef the Ptpusesmentioning

confidence: 84%

A thousand and two protein tyrosine phosphatases

Pot¹,

Dixon²

1992

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

123

View full text Add to dashboard Cite

“…Changes in [Ca2+ ] have been reported to affect the activities of both tyrosine kinases (Migliaccio et al ., 1984;Huckle et al ., 1992) and protein tyrosine phosphatases (Singh, 1990;Mei and Huganir, 1991 ;Ostergaard and Trowbridge, 1991) . The dependency of the sustained decrease in tyrosine phosphorylation of PSD-GP180 on the presence of extracellular Ca 2+ ions suggests that increases in [Ca2 ']; resulting from the ischemic-like event may modulate the activities of tyrosine kinases or protein tyrosine phosphatases that are associated with the PSD (Cudmore and Gurd, 1991 ;Yoshioka et al, 1991) and that act on PSD-GP 180 .…”

Section: Discussionmentioning

confidence: 99%

Tyrosine Phosphorylation in a Model of Ischemia Using the Rat Hippocampal Slice: Specific, Long‐Term Decrease in the Tyrosine Phosphorylation of the Postsynaptic Glycoprotein PSD‐GP180

Au¹,

Gurd²

1995

Journal of Neurochemistry

View full text Add to dashboard Cite

The effects of the exposure of hippocampal slices to brief periods of ischemic‐like conditions on the tyrosine phosphorylation of proteins and glycoproteins were investigated. Freshly prepared hippocampal slices contained a range of tyrosine‐phosphorylated proteins and two prominent tyrosine‐phosphorylated glycoproteins of apparent Mr 110,000 (GP110) and 180,000, which we have previously shown to correspond to the postsynaptic density (PSD)‐associated glycoprotein PSD‐GP180. When hippocampal slices were incubated in oxygenated Krebs‐Ringer buffer containing 10 mM glucose (KRB), there was a transient increase in the tyrosine phosphorylation of a protein of Mr 42,000 (p42) and a pronounced increase in the tyrosine phosphorylation of GP110. After these initial changes, the tyrosine phosphorylation of all proteins remained constant for at least 60 min. In vitro “ischemia” was achieved by transferring slices that had been preincubated for 60 min in KRB to KRB that had been equilibrated with N2 instead of O2 and that did not contain glucose. Tyrosine‐phosphorylated GP110 and PSD‐GP180 could no longer be detected after 10 min of exposure of the slices to ischemic‐like conditions. GP110 was rapidly rephosphorylated on tyrosine after transfer of slices back to oxygenated, glucose‐containing buffer. In contrast, short periods of ischemia (5 or 10 min) resulted in the long‐term loss of phosphotyrosine [Tyr(P)]‐PSD‐GP180 so that it was not detected even after 60 min of reincubation in oxygenated KRB. The sustained decrease in tyrosine phosphorylation of PSD‐GP180 after ischemia was Ca2+ dependent, the levels of Tyr(P)‐PSD‐GP180 slowly increasing to preischemic values if Ca2+ was omitted from the incubation media. Reoxygenation of ischemic slices also resulted in the Ca2+‐dependent, transient tyrosine phosphorylation of p42. The major PSD‐associated, tyrosine‐phosphorylated glycoprotein of molecular mass 180 kDa has recently been identified as the NR2B subunit of the NMDA receptor. The results suggest that changes in tyrosine phosphorylation after an ischemic insult may modulate the NMDA receptor or signal transduction pathways in the postsynaptic cell and are consistent with a role for tyrosine phosphorylation in the sequence of events leading to neuronal cell damage and death.

show abstract

“…Several other proteins predominantly localized in the perikarya or dendrites of neurons have been identified and include microtubuleassociated protein 2 (Huber and Matus, 1984), erythrocyte spectrin (Lazarides and Nelson, 1983), brain 4. Ilike protein (Goodman et al, 1984), erythrocyte ankyrin-like proteins (Kordeli and Bennett, 1991), glycoproteins bearing the PAC 1 epitope (Willmott et al,199 1) , Ca2'/calmodulin-dependent protein kinase I I (Fukunaga et al, 1988), calmodulin and the heat-labile calmodulin-binding protein CaM-BP,, (Wood et al, 1980), the y-subspecies of protein kinase C (Kose et al, 1990), and phosphotyrosine protein phosphatase activity (Yoshioka et al, 1991). Thus, the F5 protein represents an additional marker distinguishing dendrites from axons.…”

Section: Discussionmentioning

confidence: 99%

Subcellular localization of the F5 protein to the neuronal membrane‐associated cytoskeleton

Arai

Cohen

1994

J of Neuroscience Research

View full text Add to dashboard Cite

F5 was identified originally as an interleukin-2-regulated gene in the murine helper T-lymphocyte clone L2. Subsequent studies demonstrated high levels of F5 mRNA and protein in mature neurons in adult mouse central and peripheral nervous systems. The F5 protein was present in dendrites and perikarya but not in axons. In the present studies, the intracellular localization of the F5 protein in adult mouse brain was determined by subcellular fractionation and Western blotting. Although the deduced F5 sequence predicts a soluble protein, virtually no F5 immunoreactivity was found in the cytosol. The F5 protein was restricted to the P2 crude mitochondrial and P3 crude microsomal particulate fractions. Within the P2 fraction, F5 protein was enriched in the P2B synaptosomal subfraction. The results of temperature-dependent phase separation with Triton X-114 and alkaline extraction with sodium carbonate of the P2 and P3 fractions were consistent with the F5 protein being an extrinsic membrane-associated protein. Although essentially all of the F5 protein in the P3 fraction was membrane-associated, a substantial proportion of P2-associated F5 protein and nearly all of the synaptosomal F5 protein was detergent-insoluble. Direct isolation and subfractionation of brain cytoskeleton confirmed colocalization of F5 immunoreactivity with the membrane-associated cytoskeleton and postsynaptic densities. These studies suggest that the F5 protein, which has a large number of potential phosphorylation sites, plays a role in membrane-cytoskeletal interactions and in dynamic aspects of synaptic structure or function.

show abstract

Histochemically demonstrable phosphotyrosine protein phsophatase in the rat hippocampal formation

Cited by 7 publications

References 18 publications

A thousand and two protein tyrosine phosphatases

A thousand and two protein tyrosine phosphatases

Tyrosine Phosphorylation in a Model of Ischemia Using the Rat Hippocampal Slice: Specific, Long‐Term Decrease in the Tyrosine Phosphorylation of the Postsynaptic Glycoprotein PSD‐GP180

Subcellular localization of the F5 protein to the neuronal membrane‐associated cytoskeleton

Contact Info

Product

Resources

About