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Rpa2  -  replication protein A2

Rattus norvegicus

Synonyms: RF-A protein 2, RP-A p32, Replication factor A protein 2, Replication protein A 32 kDa subunit
 
 
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High impact information on Rpa2

  • All PKC isoforms expressed in rat hepatocytes interacted in vitro with p32, but the binding dependence on PKC activators was different for each one [1].
  • Recombinant p32 was expressed as a glutathione S-transferase fusion protein, affinity-purified, and tested for an in vitro interaction with PKC using an overlay assay approach [1].
  • Our data also showed that phorbol ester treatment induces a transient translocation of p32 from the cytoplasm to the cell nucleus [1].
  • This third protein has been compared with a protein, p32/6.3, of very similar size and isoelectric point, which has been associated with lead-induced intranuclear inclusion bodies [2].
  • Reaction of rat brain and placenta microsomes with BrAc[125I]T3 resulted in the extensive labeling of a 32 kDa protein (p32) [3].
 

Anatomical context of Rpa2

  • A time course of phorbol ester treatment of cultured rat hepatocytes (C9 cells) showed that PKCtheta and p32 are constitutively associated in vivo, whereas PKCdelta activation is required for its association with p32 [1].
  • BrAc[125I]T3 labeling of embryonic chicken liver microsomes did not reveal p32 or another protein possibly related to ID-III [3].
  • SDS-PAGE of BrAc[125I]T3-labeled microsomes showed a prominent radioactive approximately 27 kDa protein (p27) in liver, kidney and thyroid, which was previously identified as ID-I, and a approximately 32 kDa protein (p32) in brain, in particular fetal brain, and placenta [4].
  • However, marked decrease in total phospholipids, phosphatidyl choline, phosphatidyl ethanolamine and phosphatidyl inositol in cauda epididymis and vas deferens was observed. p32 incorporation also showed similar changes in phospholipids [5].
 

Associations of Rpa2 with chemical compounds

  • Although 3,3',5'-triiodothyronine (rT3) is not a substrate for ID-III, p32 was readily labeled with BrAc[125I]rT3 [4].
  • Labeling of p32 in rat brain microsomes by BrAc[125I]rT3 was not affected by addition of 100 microM unlabeled thyroxine (T4) or T3, whereas deiodination of [125I]T3 by ID-III was inhibited by 91 and 96% in the presence of 1 microM T4 and T3, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)[4]
  • After treatment of microsomes with 0.05% deoxycholate or carbonate buffer (pH 11.5) p32 was still labeled by BrAc[125I]T3, indicating that p32 is a transmembrane protein [4].
  • Incubation of isolated hepatocytes with leupeptin induced time-dependent accumulation of p32 in the ML fraction from 30 to 90 min after the start of incubation [6].
  • Amino acids and 3-methyladenine, both of which specifically suppress macroautophagy, inhibited the accumulation of p32 as well as of p44 [6].
 

Analytical, diagnostic and therapeutic context of Rpa2

References

  1. p32 (gC1qBP) is a general protein kinase C (PKC)-binding protein; interaction and cellular localization of P32-PKC complexes in ray hepatocytes. Robles-Flores, M., Rendon-Huerta, E., Gonzalez-Aguilar, H., Mendoza-Hernandez, G., Islas, S., Mendoza, V., Ponce-Castaneda, M.V., Gonzalez-Mariscal, L., Lopez-Casillas, F. J. Biol. Chem. (2002) [Pubmed]
  2. The induction of stress-related proteins by lead. Shelton, K.R., Todd, J.M., Egle, P.M. J. Biol. Chem. (1986) [Pubmed]
  3. Reaction of the type III iodothyronine deiodinase with the affinity label N-bromoacetyl-triiodothyronine. Schoenmakers, C.H., Pigmans, I.G., Kaptein, E., Darras, V.M., Visser, T.J. FEBS Lett. (1993) [Pubmed]
  4. Investigation of type I and type III iodothyronine deiodinases in rat tissues using N-bromoacetyl-iodothyronine affinity labels. Schoenmakers, C.H., Pigmans, I.G., Visser, T.J. Mol. Cell. Endocrinol. (1995) [Pubmed]
  5. Phospholipid analysis in testis-epididymis complex after alpha-chlorohydrin administration. Kalla, N.R., Singh, B. Contraception. (1978) [Pubmed]
  6. Leupeptin-induced appearance of partial fragment of betaine homocysteine methyltransferase during autophagic maturation in rat hepatocytes. Furuya, N., Kanazawa, T., Fujimura, S., Ueno, T., Kominami, E., Kadowaki, M. J. Biochem. (2001) [Pubmed]
 
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