Purification and characterization of rabbit liver calmodulin-dependent glycogen synthase kinase.

Payne, M E; Schworer, Charles M.; Soderling, Thomas R.

doi:10.1016/s0021-9258(18)32934-x

Cited by 150 publications

(18 citation statements)

References 40 publications

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“…The amino acid sequences surrounding phosphorylation sites of several substrates for CaM-kinase II have been determined. Examination of the available amino acid sequences reveals that an arginine three residues N-terminal of the phosphorylated serine or threonine is common to all the sequences, and is missing from sequences phosphorylated by other protein kinases, but not CaM-kinase II [16]. This comparison was most striking with the purified 20 kDa myosin light chains from smooth, skeletal and cardiac muscle, which are all good substrates for myosin light chain kinase.…”

Section: Substratesmentioning

confidence: 99%

“…Studies from a number of laboratories have demonstrated that isoenzymes of CaM-kinase II are also present in most mammalian tissues examined. Indeed, the kinase has been highly purified from mammalian brain [7,[10][11][12][13][14], liver [8,15,16], skeletal muscle [17], heart [18], pancreas [19], retina [20], lung [21], parathyroid [22], mammary gland [23] and intestinal brush border [24], as well as neural tissues of Aplysia [25], electric eel [26], squid [27] and Drosophila [28]. The isoenzymes are characterized by a large native molecular mass (300-700 kDa), subunits in the range 50-62 kDa, and similar or identical catalytic properties against several protein substrates (references listed above and [29]).…”

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

“…This comparison was most striking with the purified 20 kDa myosin light chains from smooth, skeletal and cardiac muscle, which are all good substrates for myosin light chain kinase. The smooth muscle light chain is also a relatively good substrate for CaM-kinase II, whereas cardiac and skeletal muscle light chains are not phosphorylated [16]. Although there is great sequence homology around the phosphorylation site for myosin light chain kinase, only the smooth muscle light chain has an arginine three residues N-terminal of the serine.…”

Section: Substratesmentioning

confidence: 99%

“…Studies in vitro have primarily used skeletal muscle glycogen synthase, since it is more thoroughly characterized (reviewed in [88,89]). CaM-kinase II catalyses the phosphorylation of muscle glycogen synthase primarily at site 2, with limited phosphorylation at site lb [16,17,90], resulting in partial inactivation of the enzyme [8,15,16]. Two other calcium-dependent protein kinases can also phosphorylate glycogen synthase in vitro, namely phosphorylase kinase (site 2) [91,92] and protein kinase C (sites 1 a and 2) [93].…”

Section: Substratesmentioning

confidence: 99%

“…Following SDS/polyacrylamide-gel electrophoresis, proteins were renatured, and an '25I-labelled calmodulin overlay was performed as described [166]. The arrow indicates the subunits of CaM-kinase II (51/53 kDa) [15,16]. from the kinase, exposing a new autophosphorylation site.…”

Section: Regulation By Ca2+/calmodulin and Autophosphorylationmentioning

confidence: 99%

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Expression of 5-aminolaevulinate synthase and cytochrome P-450 mRNAs in chicken embryo hepatocytes in vivo and in culture. Effect of porphyrinogenic drugs and haem

Colbran

Schworer

Hashimoto

et al. 1989

Biochemical Journal

281

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kinase activity is cytoplasmic in rat kidney (100 %), liver (94 0%) and heart (82 0%). whereas in cerebrum and testis most is particulate (88 % and 840%, respectively) [36].Immunological techniques have been used to demonstrate that in rat brain the subcellular distribution of the kinase, as well as its subunit composition, are under developmental control. The forebrain of 5-day postnatal rats contains approx. 800% cytoplasmic CaM-kinase II, with ax (50 kDa) and /3(60 kDa) subunits in a molar ratio of about 1:4 [37]. Between days 5 and 20 there is a 10fold increase in CaM-kinase II, with 80 % of the kinase now being particulate, and a 7: 1 ratio of a and , subunits [37]. The level of mRNA for the oc-subunit in forebrain also increases approx. 10-fold between postnatal days 1 and 21 [31]. In adult rat brain, the highest levels of CaMkinase II are found in the telencephalon regions (hippocampus, lateral septum, cortex, neostriatum, amygdaloid), with much lower activity in the cerebellum, diencephalon, mesencephalon, pons and medulla [9,38]. The ratio of subunits also varies between the different regions, with a and , subunits present in a 4: 1 ratio in rat forebrain and in a 1:4 ratio in cerebellum [12,39]. The variation in ratio of subunit polypeptides in these regions is paralleled by different ratios of the specific mRNA Vol. 258Abbreviations used: CaM-kinase II, Ca2+/calmodulin-dependent protein kinase II; cAMP-kinase, cyclic AMP-dependent protein kinase; protein kinase C, Ca2+/phospholipid-dependent protein kinase.* To whom correspondence and reprint requests should be addressed.Brain microtubule-associated proteins: MAP-2 and T. Microtubules are known to consist of tubulin and several microtubule-associated proteins or MAPs, some of which have been studied extensively. One of these, MAP-2, contains about 22 phosphorylation sites, 13 that are cyclic AMP-dependent and at least 8 that are cyclic AMP-independent [59]. MAP-2 is readily phosphorylated Vol. 258

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Section: Substratesmentioning

confidence: 99%

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

Section: Substratesmentioning

confidence: 99%

Section: Substratesmentioning

confidence: 99%

Section: Regulation By Ca2+/calmodulin and Autophosphorylationmentioning

confidence: 99%

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Expression of 5-aminolaevulinate synthase and cytochrome P-450 mRNAs in chicken embryo hepatocytes in vivo and in culture. Effect of porphyrinogenic drugs and haem

Colbran

Schworer

Hashimoto

et al. 1989

Biochemical Journal

281

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Tyrosine Hydroxylase

Kaufman¹

1995

Advances in Enzymology - And Related Areas of Molecular Biology

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a b o r a t o r y of N e u r o c h e m i s t r y , N a t i o n a l I n s t i t u t e of M e n t a l H e a l t h , B e t h e s d a , Maryland the first step in the biosynthesis of norepinephrine and epinephrine involved the conversion of tyrosine to 3,4dihydroxyphenylalanine (dopa), followed by decarboxylation of the dopa to dopamine, which was then hydroxylated in the p position of the side chain and methylated on the amino group to form norepinephrine and epinephrine, respectively (Fig. 1). Although the evidence in favor of the pathway proposed by Blaschko continued to mount (5-8), and it is now widely accepted as the only quantitatively important one, the enzyme responsible for the ring hydroxylation SEYMOUR KAUFMAN droxylation of phenylalanine (17, 18), this product was also shown to be found during the TH-catalyzed conversion of tyrosine to dopa. (For a further discussion of this aspect of the reaction, see Section XI and Fig. 7.) Intracellular Localization and Regional DistributionAs already mentioned, TH is present in brain, adrenal medulla, and sympathetically innervated tissues. Its intracellular location in these tissues, however, has been the subject of controversy. Udenfriend and co-workers (12) reported that in guinea pig brain all of the activity, and in beef adrenal medulla, most of the activity, was particle bound. They further concluded that the hydroxylase found in the soluble fraction of adrenal medulla was originally present in particles from which it had been released by the homogenization process, a conclusion that was strengthened by the finding that about 90% of the activity was sedimentable after centrifugation for 1 h at 144,000 g. These findings appeared to support the proposal that all of the enzymes involved in catecholamine biosynthesis are localized within a catecholamine-containing granule (19).There is a growing body of evidence that contradicts the conclusion that TH is present intracellularly within a granule (20, 21). For the enzyme from both adrenal medulla and nerve tissue, it has been found that a major fraction of the activity is present in the highspeed supernatant fraction and that the distribution of hydroxylase activity is a function of the composition of the homogenization medium; homogenization in isotonic KC1 leads to more enzyme in the supernatant fraction than does homogenization in isotonic sucrose (21). At least part of the uncertainty about the intracellular localization of TH can be traced to the tendency of the enzyme from bovine adrenal medulla, and probably from other tissues as well, to aggregate and to adsorb to subcellular organelles (21).Although there is now a near consensus in favor of the view that the high molecular weight form of the enzyme in adrenal medulla is an artifact that is formed during cell disruption and that it is not in equilibrium with the native, nonaggregated form (22), that conclusion does not apply to brain where the enzyme appears to exist in two distinct forms, a soluble and a membrane-bound form. In fact, in the earliest studies...

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Organ‐specific distribution of the calcium sensor CaMKII in Locusta migratoria

Braak

Fährmann

2003

Arch Insect Biochem Physiol

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The Ca(2+)/calmodulin-dependent kinase CaMKII is a key signaling component in Ca(2+)-dependent physiological processes. The expression and function of CaMKII in insect brain is well documented but less investigated for other tissues of insects. The present study demonstrates that in the locust Locusta migratoria CaMKII is widely expressed in various tissues. Relatively high expression levels of CaMKII were found in the brain, upper part of the digestive tract (pharynx, esophagus), and the flight and leg muscles. The different expression patterns of CaMKII in various tissues, as well as different molecular masses of CaMKII between 48 and 60 kDa indicate a tissue-specific expression of CaMKII variants. The expression was monitored with a polyclonal anti-(rat)CaMKII antibody. About 60% of total CaMKII activity in flight muscle cells is associated to the myofibril-rich, particulate fraction suggesting an important role of CaMKII in sarcomeric function.

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Purification and characterization of rabbit liver calmodulin-dependent glycogen synthase kinase.

Cited by 150 publications

References 40 publications

Expression of 5-aminolaevulinate synthase and cytochrome P-450 mRNAs in chicken embryo hepatocytes in vivo and in culture. Effect of porphyrinogenic drugs and haem

Expression of 5-aminolaevulinate synthase and cytochrome P-450 mRNAs in chicken embryo hepatocytes in vivo and in culture. Effect of porphyrinogenic drugs and haem

Tyrosine Hydroxylase

Organ‐specific distribution of the calcium sensor CaMKII in Locusta migratoria

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