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W2035615036 abstract "A homologue of human protein kinase C (PKC)-related kinase-2, PRK2, which had previously escaped identification in normal mammalian tissues, was isolated from rat liver as the protease-activated kinase (PAK) originally named PAK-2. The 130-kDa cytosolic enzyme was purified to homogeneity and shown by tryptic peptide and reverse transcriptase- polymerase chain reaction (RT-PCR)-amplified rat cDNA sequence analyses to be structurally related to the 116-kDa rat hepatic PAK-1/protein kinase N (PKN) and, even more closely (95% sequence identity) to the 130-kDa human PKC-related kinase, PRK2. Rat myeloma RNA was used as the RT-PCR template because of its relative abundance in PAK-2/PRK2 mRNA compared with liver and other rat tissues. The catalytic properties of PAK-2/PRK2 in many respects resembled those of hepatic PAK-1/PKN, but were distinguished by more favorable kinetics with several peptide substrates, and greater sensitivity to PKC pseudosubstrate and polybasic amino acid inhibitors. PAK-2/PRK2 was also activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids and unsaturated fatty acids. Cardiolipin activation was most evident with autophosphorylation and histone H2B phosphorylation, but only marginally evident with the favored ribosomal S6-(229–239) peptide substrate for the protease-activated kinase activity. It was concluded that PAK-2 is the rat homologue of human PRK2, with biochemical properties distinct from although overlapping those of the PAK-1/PKN/PRK1 isoform. A homologue of human protein kinase C (PKC)-related kinase-2, PRK2, which had previously escaped identification in normal mammalian tissues, was isolated from rat liver as the protease-activated kinase (PAK) originally named PAK-2. The 130-kDa cytosolic enzyme was purified to homogeneity and shown by tryptic peptide and reverse transcriptase- polymerase chain reaction (RT-PCR)-amplified rat cDNA sequence analyses to be structurally related to the 116-kDa rat hepatic PAK-1/protein kinase N (PKN) and, even more closely (95% sequence identity) to the 130-kDa human PKC-related kinase, PRK2. Rat myeloma RNA was used as the RT-PCR template because of its relative abundance in PAK-2/PRK2 mRNA compared with liver and other rat tissues. The catalytic properties of PAK-2/PRK2 in many respects resembled those of hepatic PAK-1/PKN, but were distinguished by more favorable kinetics with several peptide substrates, and greater sensitivity to PKC pseudosubstrate and polybasic amino acid inhibitors. PAK-2/PRK2 was also activated by lipids, particularly cardiolipin and to a lesser extent by other acidic phospholipids and unsaturated fatty acids. Cardiolipin activation was most evident with autophosphorylation and histone H2B phosphorylation, but only marginally evident with the favored ribosomal S6-(229–239) peptide substrate for the protease-activated kinase activity. It was concluded that PAK-2 is the rat homologue of human PRK2, with biochemical properties distinct from although overlapping those of the PAK-1/PKN/PRK1 isoform. INTRODUCTIONLipid-regulated protein kinases, best characterized by the protein kinase Cs (PKCs) 1The abbreviations used are: PKCprotein kinase CPAKprotease-activated protein kinasePRKprotein kinase C-related kinasePKNprotein kinase NHPLChigh performance liquid chromatographyPAGEpolyacrylamide gel electrophoresisS6-(229–239)synthetic peptide analogue of ribosomal protein S6, residues 229-239 (Ala-Lys-Arg-Arg-Arg-Leu-Ser-Ser-Leu-Arg-Ala)PKC-α-(19–31)pseudosubstrate inhibitor peptide (Arg-Phe-Ala-Arg-Lys-Gly-Ala-Leu-Arg-Gln-Lys-Asn-Val)GS-(1–12)synthetic peptide analogue based on skeletal muscle glycogen synthase sequence, residues 1-12, Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys-LysEGFR-(650–658)synthetic peptide analogue of epidermal growth factor receptor (Val-Arg-Lys-Arg-Thr-Leu-Arg-Arg-Leu)CLcardiolipinPCRpolymerase chain reactionRTreverse transcriptasePMSFphenylmethylsulfonyl fluoride. (1Nishizuka Y Science. 1992; 258: 607-614Google Scholar, 2Nishizuka Y FASEB J. 1995; 9: 484-496Google Scholar, 3Newton A. J. Biol. Chem. 1995; 270: 28495-28498Google Scholar), also include the recently discovered family variously named the liver PAK 2The often used abbreviation PAK to describe protease-activated kinase (e.g. see Refs. 4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, and 19Tahara S.M. Traugh J.A. J. Biol. Chem. 1981; 256: 11558-11564Google Scholar) should not be confused with the recent use of the same abbreviation to describe p21 protein-activated kinases (e.g. see Manser et al (29Manser E. Leung T. Sallhuddin H. Zhao Z.-S. Lim L. Nature. 1994; 367: 40-46Google Scholar)). (4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), PKN (6Mukai H. Ono Y. Biochem. Biophys. Res. Commun. 1994; 199: 897-904Google Scholar, 7Mukai H. Kitagawa M. Shibata H. Takanaga H. Mori K. Shimakawa M. Miyahara M. Hirao K. Ono Y. Biochem. Biophys. Res. Commun. 1995; 204: 348-356Google Scholar, 8Kitagawa M. Mukai H. Shibata H. Ono Y. Biochem. J. 1995; 310: 657-664Google Scholar), and the PKC-related kinases (PRKs) (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar, 10Palmer R.H. Parker P.J. Biochem. J. 1995; 309: 315-320Google Scholar, 11Palmer R.H. Dekker L.D. Woscholski R. Le Good A.J. Gigg R. Parker P.J. J. Biol. Chem. 1995; 270: 22412-22416Google Scholar). While several PKN/PRK isoforms have been detected by cDNA/PCR analyses (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar), direct mRNA analyses have detected only the ubiquitously expressed PKN/PRK1 in human and rat tissues (6Mukai H. Ono Y. Biochem. Biophys. Res. Commun. 1994; 199: 897-904Google Scholar, 9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar), PRK-3 in human myeloma and a few rat tissues (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar), and PRK2 only in human myeloma cell lines (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar). PKN/PRK1-type isoforms have been isolated and structurally characterized, originally as the naturally occurring liver protease-activated kinase, PAK-1 (4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), and, subsequently as the cDNA-derived recombinant proteins (6Mukai H. Ono Y. Biochem. Biophys. Res. Commun. 1994; 199: 897-904Google Scholar, 9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar, 12Peng B. Morrice N.A. Groenen L. Wettenhall R.E.H. J. Biol. Chem. 1996; 271: 32233-32240Google Scholar). Isoforms of this type share several biochemical characteristics with the PKCs, particularly their general substrate preferences and activatability by proteases, phospholipids and unsaturated fatty acids (4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, 7Mukai H. Kitagawa M. Shibata H. Takanaga H. Mori K. Shimakawa M. Miyahara M. Hirao K. Ono Y. Biochem. Biophys. Res. Commun. 1995; 204: 348-356Google Scholar, 8Kitagawa M. Mukai H. Shibata H. Ono Y. Biochem. J. 1995; 310: 657-664Google Scholar, 10Palmer R.H. Parker P.J. Biochem. J. 1995; 309: 315-320Google Scholar, 11Palmer R.H. Dekker L.D. Woscholski R. Le Good A.J. Gigg R. Parker P.J. J. Biol. Chem. 1995; 270: 22412-22416Google Scholar, 13Morrice N.A. Fecondo J. Wettenhall R.E.H. FEBS Lett. 1994; 351: 171-175Google Scholar), but are distinguished from the PKCs by their phospholipid specificity (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, 13Morrice N.A. Fecondo J. Wettenhall R.E.H. FEBS Lett. 1994; 351: 171-175Google Scholar), inhibitor sensitivity (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), substrate kinetics (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), and activatability by the RhoA GTP-binding protein (14Amano M. Mukai H. Ono Y. Chihara K. Matsui T. Hamajima Y. Okawa K. Iwamatsu A. Kaibuchi K. Science. 1996; 271: 648-650Google Scholar, 15Mukai H. Miyahara M. Sunakawa H. Shibata H. Toshimori M. Kitagawa M. Shimakawa M. Takanaga H. Ono Y. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 10195-10199Google Scholar). Human PRK1 and PRK2 share structurally very similar catalytic domains (87% identity), but relatively less similar N-terminal regulatory regions (48% identity; see Palmer and Parker (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar)), suggestive of different regulatory domain functions.The failure to detect PRK2 mRNA in normal human and rat tissues suggests either that expression is restricted to abnormal cells of the myeloma type (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar) or that low abundance or an intrinsic structural feature of the mRNA prevents its ready detection. Direct screening of rat liver extracts (cytosol) for PRK-like enzyme activities has identified a second protease-activated kinase (PAK-2) with biochemically similar, although nonidentical, properties to those of liver PAK-1/PKN (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, 16Wettenhall R.E.H. Gabrielli B. Morrice N.A. Bozinova L. Kemp B.E. Stapleton D. Peptide Res. 1991; 4: 159-170Google Scholar). This investigation concerns the purification and characterization of this enzyme, including an assessment of its relationship with the PRKs. INTRODUCTIONLipid-regulated protein kinases, best characterized by the protein kinase Cs (PKCs) 1The abbreviations used are: PKCprotein kinase CPAKprotease-activated protein kinasePRKprotein kinase C-related kinasePKNprotein kinase NHPLChigh performance liquid chromatographyPAGEpolyacrylamide gel electrophoresisS6-(229–239)synthetic peptide analogue of ribosomal protein S6, residues 229-239 (Ala-Lys-Arg-Arg-Arg-Leu-Ser-Ser-Leu-Arg-Ala)PKC-α-(19–31)pseudosubstrate inhibitor peptide (Arg-Phe-Ala-Arg-Lys-Gly-Ala-Leu-Arg-Gln-Lys-Asn-Val)GS-(1–12)synthetic peptide analogue based on skeletal muscle glycogen synthase sequence, residues 1-12, Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys-LysEGFR-(650–658)synthetic peptide analogue of epidermal growth factor receptor (Val-Arg-Lys-Arg-Thr-Leu-Arg-Arg-Leu)CLcardiolipinPCRpolymerase chain reactionRTreverse transcriptasePMSFphenylmethylsulfonyl fluoride. (1Nishizuka Y Science. 1992; 258: 607-614Google Scholar, 2Nishizuka Y FASEB J. 1995; 9: 484-496Google Scholar, 3Newton A. J. Biol. Chem. 1995; 270: 28495-28498Google Scholar), also include the recently discovered family variously named the liver PAK 2The often used abbreviation PAK to describe protease-activated kinase (e.g. see Refs. 4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, and 19Tahara S.M. Traugh J.A. J. Biol. Chem. 1981; 256: 11558-11564Google Scholar) should not be confused with the recent use of the same abbreviation to describe p21 protein-activated kinases (e.g. see Manser et al (29Manser E. Leung T. Sallhuddin H. Zhao Z.-S. Lim L. Nature. 1994; 367: 40-46Google Scholar)). (4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), PKN (6Mukai H. Ono Y. Biochem. Biophys. Res. Commun. 1994; 199: 897-904Google Scholar, 7Mukai H. Kitagawa M. Shibata H. Takanaga H. Mori K. Shimakawa M. Miyahara M. Hirao K. Ono Y. Biochem. Biophys. Res. Commun. 1995; 204: 348-356Google Scholar, 8Kitagawa M. Mukai H. Shibata H. Ono Y. Biochem. J. 1995; 310: 657-664Google Scholar), and the PKC-related kinases (PRKs) (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar, 10Palmer R.H. Parker P.J. Biochem. J. 1995; 309: 315-320Google Scholar, 11Palmer R.H. Dekker L.D. Woscholski R. Le Good A.J. Gigg R. Parker P.J. J. Biol. Chem. 1995; 270: 22412-22416Google Scholar). While several PKN/PRK isoforms have been detected by cDNA/PCR analyses (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar), direct mRNA analyses have detected only the ubiquitously expressed PKN/PRK1 in human and rat tissues (6Mukai H. Ono Y. Biochem. Biophys. Res. Commun. 1994; 199: 897-904Google Scholar, 9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar), PRK-3 in human myeloma and a few rat tissues (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar), and PRK2 only in human myeloma cell lines (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar). PKN/PRK1-type isoforms have been isolated and structurally characterized, originally as the naturally occurring liver protease-activated kinase, PAK-1 (4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), and, subsequently as the cDNA-derived recombinant proteins (6Mukai H. Ono Y. Biochem. Biophys. Res. Commun. 1994; 199: 897-904Google Scholar, 9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar, 12Peng B. Morrice N.A. Groenen L. Wettenhall R.E.H. J. Biol. Chem. 1996; 271: 32233-32240Google Scholar). Isoforms of this type share several biochemical characteristics with the PKCs, particularly their general substrate preferences and activatability by proteases, phospholipids and unsaturated fatty acids (4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, 7Mukai H. Kitagawa M. Shibata H. Takanaga H. Mori K. Shimakawa M. Miyahara M. Hirao K. Ono Y. Biochem. Biophys. Res. Commun. 1995; 204: 348-356Google Scholar, 8Kitagawa M. Mukai H. Shibata H. Ono Y. Biochem. J. 1995; 310: 657-664Google Scholar, 10Palmer R.H. Parker P.J. Biochem. J. 1995; 309: 315-320Google Scholar, 11Palmer R.H. Dekker L.D. Woscholski R. Le Good A.J. Gigg R. Parker P.J. J. Biol. Chem. 1995; 270: 22412-22416Google Scholar, 13Morrice N.A. Fecondo J. Wettenhall R.E.H. FEBS Lett. 1994; 351: 171-175Google Scholar), but are distinguished from the PKCs by their phospholipid specificity (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, 13Morrice N.A. Fecondo J. Wettenhall R.E.H. FEBS Lett. 1994; 351: 171-175Google Scholar), inhibitor sensitivity (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), substrate kinetics (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), and activatability by the RhoA GTP-binding protein (14Amano M. Mukai H. Ono Y. Chihara K. Matsui T. Hamajima Y. Okawa K. Iwamatsu A. Kaibuchi K. Science. 1996; 271: 648-650Google Scholar, 15Mukai H. Miyahara M. Sunakawa H. Shibata H. Toshimori M. Kitagawa M. Shimakawa M. Takanaga H. Ono Y. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 10195-10199Google Scholar). Human PRK1 and PRK2 share structurally very similar catalytic domains (87% identity), but relatively less similar N-terminal regulatory regions (48% identity; see Palmer and Parker (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar)), suggestive of different regulatory domain functions.The failure to detect PRK2 mRNA in normal human and rat tissues suggests either that expression is restricted to abnormal cells of the myeloma type (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar) or that low abundance or an intrinsic structural feature of the mRNA prevents its ready detection. Direct screening of rat liver extracts (cytosol) for PRK-like enzyme activities has identified a second protease-activated kinase (PAK-2) with biochemically similar, although nonidentical, properties to those of liver PAK-1/PKN (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, 16Wettenhall R.E.H. Gabrielli B. Morrice N.A. Bozinova L. Kemp B.E. Stapleton D. Peptide Res. 1991; 4: 159-170Google Scholar). This investigation concerns the purification and characterization of this enzyme, including an assessment of its relationship with the PRKs. Lipid-regulated protein kinases, best characterized by the protein kinase Cs (PKCs) 1The abbreviations used are: PKCprotein kinase CPAKprotease-activated protein kinasePRKprotein kinase C-related kinasePKNprotein kinase NHPLChigh performance liquid chromatographyPAGEpolyacrylamide gel electrophoresisS6-(229–239)synthetic peptide analogue of ribosomal protein S6, residues 229-239 (Ala-Lys-Arg-Arg-Arg-Leu-Ser-Ser-Leu-Arg-Ala)PKC-α-(19–31)pseudosubstrate inhibitor peptide (Arg-Phe-Ala-Arg-Lys-Gly-Ala-Leu-Arg-Gln-Lys-Asn-Val)GS-(1–12)synthetic peptide analogue based on skeletal muscle glycogen synthase sequence, residues 1-12, Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys-LysEGFR-(650–658)synthetic peptide analogue of epidermal growth factor receptor (Val-Arg-Lys-Arg-Thr-Leu-Arg-Arg-Leu)CLcardiolipinPCRpolymerase chain reactionRTreverse transcriptasePMSFphenylmethylsulfonyl fluoride. (1Nishizuka Y Science. 1992; 258: 607-614Google Scholar, 2Nishizuka Y FASEB J. 1995; 9: 484-496Google Scholar, 3Newton A. J. Biol. Chem. 1995; 270: 28495-28498Google Scholar), also include the recently discovered family variously named the liver PAK 2The often used abbreviation PAK to describe protease-activated kinase (e.g. see Refs. 4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, and 19Tahara S.M. Traugh J.A. J. Biol. Chem. 1981; 256: 11558-11564Google Scholar) should not be confused with the recent use of the same abbreviation to describe p21 protein-activated kinases (e.g. see Manser et al (29Manser E. Leung T. Sallhuddin H. Zhao Z.-S. Lim L. Nature. 1994; 367: 40-46Google Scholar)). (4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), PKN (6Mukai H. Ono Y. Biochem. Biophys. Res. Commun. 1994; 199: 897-904Google Scholar, 7Mukai H. Kitagawa M. Shibata H. Takanaga H. Mori K. Shimakawa M. Miyahara M. Hirao K. Ono Y. Biochem. Biophys. Res. Commun. 1995; 204: 348-356Google Scholar, 8Kitagawa M. Mukai H. Shibata H. Ono Y. Biochem. J. 1995; 310: 657-664Google Scholar), and the PKC-related kinases (PRKs) (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar, 10Palmer R.H. Parker P.J. Biochem. J. 1995; 309: 315-320Google Scholar, 11Palmer R.H. Dekker L.D. Woscholski R. Le Good A.J. Gigg R. Parker P.J. J. Biol. Chem. 1995; 270: 22412-22416Google Scholar). While several PKN/PRK isoforms have been detected by cDNA/PCR analyses (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar), direct mRNA analyses have detected only the ubiquitously expressed PKN/PRK1 in human and rat tissues (6Mukai H. Ono Y. Biochem. Biophys. Res. Commun. 1994; 199: 897-904Google Scholar, 9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar), PRK-3 in human myeloma and a few rat tissues (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar), and PRK2 only in human myeloma cell lines (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar). PKN/PRK1-type isoforms have been isolated and structurally characterized, originally as the naturally occurring liver protease-activated kinase, PAK-1 (4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), and, subsequently as the cDNA-derived recombinant proteins (6Mukai H. Ono Y. Biochem. Biophys. Res. Commun. 1994; 199: 897-904Google Scholar, 9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar, 12Peng B. Morrice N.A. Groenen L. Wettenhall R.E.H. J. Biol. Chem. 1996; 271: 32233-32240Google Scholar). Isoforms of this type share several biochemical characteristics with the PKCs, particularly their general substrate preferences and activatability by proteases, phospholipids and unsaturated fatty acids (4Gabrielli B. Wettenhall R.E.H. Kemp B.E. Quinn M. Bozinova L. FEBS Lett. 1984; 175: 219-226Google Scholar, 5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, 7Mukai H. Kitagawa M. Shibata H. Takanaga H. Mori K. Shimakawa M. Miyahara M. Hirao K. Ono Y. Biochem. Biophys. Res. Commun. 1995; 204: 348-356Google Scholar, 8Kitagawa M. Mukai H. Shibata H. Ono Y. Biochem. J. 1995; 310: 657-664Google Scholar, 10Palmer R.H. Parker P.J. Biochem. J. 1995; 309: 315-320Google Scholar, 11Palmer R.H. Dekker L.D. Woscholski R. Le Good A.J. Gigg R. Parker P.J. J. Biol. Chem. 1995; 270: 22412-22416Google Scholar, 13Morrice N.A. Fecondo J. Wettenhall R.E.H. FEBS Lett. 1994; 351: 171-175Google Scholar), but are distinguished from the PKCs by their phospholipid specificity (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, 13Morrice N.A. Fecondo J. Wettenhall R.E.H. FEBS Lett. 1994; 351: 171-175Google Scholar), inhibitor sensitivity (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), substrate kinetics (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar), and activatability by the RhoA GTP-binding protein (14Amano M. Mukai H. Ono Y. Chihara K. Matsui T. Hamajima Y. Okawa K. Iwamatsu A. Kaibuchi K. Science. 1996; 271: 648-650Google Scholar, 15Mukai H. Miyahara M. Sunakawa H. Shibata H. Toshimori M. Kitagawa M. Shimakawa M. Takanaga H. Ono Y. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 10195-10199Google Scholar). Human PRK1 and PRK2 share structurally very similar catalytic domains (87% identity), but relatively less similar N-terminal regulatory regions (48% identity; see Palmer and Parker (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar)), suggestive of different regulatory domain functions. protein kinase C protease-activated protein kinase protein kinase C-related kinase protein kinase N high performance liquid chromatography polyacrylamide gel electrophoresis synthetic peptide analogue of ribosomal protein S6, residues 229-239 (Ala-Lys-Arg-Arg-Arg-Leu-Ser-Ser-Leu-Arg-Ala) pseudosubstrate inhibitor peptide (Arg-Phe-Ala-Arg-Lys-Gly-Ala-Leu-Arg-Gln-Lys-Asn-Val) synthetic peptide analogue based on skeletal muscle glycogen synthase sequence, residues 1-12, Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys-Lys synthetic peptide analogue of epidermal growth factor receptor (Val-Arg-Lys-Arg-Thr-Leu-Arg-Arg-Leu) cardiolipin polymerase chain reaction reverse transcriptase phenylmethylsulfonyl fluoride. The failure to detect PRK2 mRNA in normal human and rat tissues suggests either that expression is restricted to abnormal cells of the myeloma type (9Palmer R.H. Parker P.J. Eur. J. Biochem. 1995; 227: 344-351Google Scholar) or that low abundance or an intrinsic structural feature of the mRNA prevents its ready detection. Direct screening of rat liver extracts (cytosol) for PRK-like enzyme activities has identified a second protease-activated kinase (PAK-2) with biochemically similar, although nonidentical, properties to those of liver PAK-1/PKN (5Morrice N.A. Gabrielli B. Kemp B.E. Wettenhall R.E.H. J. Biol. Chem. 1994; 269: 20040-20046Google Scholar, 16Wettenhall R.E.H. Gabrielli B. Morrice N.A. Bozinova L. Kemp B.E. Stapleton D. Peptide Res. 1991; 4: 159-170Google Scholar). This investigation concerns the purification and characterization of this enzyme, including an assessment of its relationship with the PRKs. We thank Zlatan Trifunovic for technical assistance, Goslik Schepers for carrying out the automated DNA sequence analyses, Dr. Heung-Chin Cheng for critical reading of the manuscript, and Ann Best for typing the manuscript." @default.
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