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  • Amino Acid Sequence
  • Phosphorylation
  • American Association for the Advancement of Science (AAAS)  (3,759)
  • Wiley-Blackwell  (19)
  • Protein Phosphorylation in Human Health  (1)
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  • 1
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    Chapter 8 Signalling DNA Damage (2021)
    InTechOpen | Protein Phosphorylation in Human Health | Protein Phosphorylation in Human Health
    Details
    Publication Date: 2024-04-04
    Description: During our lifetime, the genome is constantly being exposed to different types of damage caused either by exogenous sources (radiations and/or genotoxic compound) but also as byproducts of endogenous processes (reactive oxigen species during respiration, stalled forks during replication, eroded telomeres, etc). From a structural point of view, there are many types of DNA damage including single or double strand breaks, base modifications and losses or base-pair mismatches. The amount of lesions that we face is enormous with estimates suggesting that each of our 1013 cells has to deal with around 10.000 lesions per day [1]. While the majority of these events are properly resolved by specialized mechanisms, a deficient response to DNA damage, and particularly to DSB, harbors a serious threat to human health [2]. DSB can be formed [1] following an exposure to ionizing radiation (X- or γ-rays) or clastogenic drugs; [2] endogenously, during DNA replication, or [3], as a consequence of reactive oxygen species (ROS) generated during oxidative metabolism. In addition, programmed DSB are used as repair intermediates during V(D)J and Class-Switch recombination (CSR) in lymphocytes [3], or during meiotic recombination [4]. Because of this, immunodeficiency and/or sterility problems are frequently associated with DDR-related pathologies.
    Keywords: dna damage ; dna damage ; Apoptosis ; Ataxia telangiectasia and Rad3 related ; ATM serine/threonine kinase ; DNA repair ; DNA-PKcs ; Phosphorylation ; Protein ; Ubiquitin ; thema EDItEUR::P Mathematics and Science::PD Science: general issues
    Language: English
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  • 2
    Electronic Resource
    Electronic Resource
    Synthesis and processing of mammalian protamines and transition proteins (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 37 (1994), S. 255-263 
    Details
    ISSN: 1040-452X
    Keywords: Phosphorylation ; Chromatin condensation ; Testis ; DNA binding proteins ; Seminiferous tubules ; Sonication-resistant nuclei ; mP1 ; Pre-mP2 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Mouse and rat seminiferous tubule fragment cultures were used to examine synthesis and processing of mammalian protamines and transition proteins. The tubule fragments were incubated with [3H]-arginine, [3H]-histidine, [35S]-cysteine, or [32P]-PO4, and radiolabeled proteins were analyzed by acid/urea polyacrylamide gel electrophoresis and fluorography or autoradiography. Newly synthesized protamines were recovered from sonication-resistant nuclei (SRN) and could not be detected in cytoplasmic fractions, indicating that protamines are deposited into nuclei immediately after synthesis. Newly synthesized mouse protamine 1 (mP1) and the precursor to mouse protamine 2 (pre-mP2) migrated more slowly during electrophoresis than their predominant testicular forms, identified by staining with Coomassie blue R-250. Within 1 hour of synthesis, the electrophoretic mobilities of mP1 and pre-mP2 increased to match those of their predominant forms. These changes are consistent with initial charge-neutralizing modifications of the newly synthesized protamines, followed by removal of at least some of the modifying ligands, to unmask protamine basicity. Steady-state phosphorylation rates were high for rat protamine 1 (rP1) and were independent of phosphate content; both rP1 molecules of low and high phosphate content were rapidly phosphorylated. Pre-mP2-3, a major processing intermediate derived by proteolysis of pre-mP2, was also rapidly phosphorylated. Like the protamines, transition protein 2 (TP2) was rapidly phosphorylated and increased in electrophoretic mobility soon after synthesis. In contrast, transition protein 1 (TP1) was not phosphorylated and did not exhibit multiple electrophoretic forms. © 1994 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080370303
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  • 3
    Electronic Resource
    Electronic Resource
    Effect of 6-dimethylaminopurine on germinal vesicle breakdown of bovine oocytes (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 29 (1991), S. 379-384 
    Details
    ISSN: 1040-452X
    Keywords: Oocyte maturation ; Phosphorylation ; 6-DMAP ; Cattle oocytes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The effect of 6-dimethylaminopurine (6-DMAP) on germinal vesicle breakdown (GVBD) and maturation in bovine oocytes was investigated in this study. This puromycin analog has been shown to be an inhibitor of phosphorylation. Whereas GVBD occurred in nearly all oocytes (96.8%; 120/124) in control medium, presence of 6-DMAP (2 mM) blocked this process almost completely, irrespective of the presence (98.3% GV, 349/355) or absence (97.1% GV, 165/170) of cumulus cells. When lower concentrations of 6-DMAP were used (100-500 μM), GVBD was observed in 87.9% of oocytes, but their maturation was arrested at late diakinesis-metaphase I stage. The inhibition of GVBD was fully reversible, but most of the metaphase II plates were abnormal (80%). To assess whether the action of 6-DMAP is different from the inhibitors of protein synthesis, metaphase II oocytes were exposed to either cycloheximide or 6-DMAP, respectively. Whereas in cycloheximide-supplemented medium approximately 80% of the oocytes were activated, parthenogenetic activation was much less frequent after incubation in 6-DMAP (14.5%). Fusion studies showed that, even if GVBD occurs in 6-DMAP supplemented medium, the level of the maturation-promoting factor (MPF) is decreased. These experiments may indicate the importance of phosphorylation for GVBD in cattle oocytes.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080290410
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  • 4
    Electronic Resource
    Electronic Resource
    Chromatin condensation and histone H1 kinase activity during growth and maturation of rabbit oocytes (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 37 (1994), S. 210-215 
    Details
    ISSN: 1040-452X
    Keywords: Meiosis ; Cell Cycle ; Phosphorylation ; p34cdc2 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Fully grown rabbit oocytes, isolated from preovulatory follicles, exhibit highly condensed bivalents within an intact germinal vesicle while a very low level of histone H1 kinase activity could be detected in their extracts. Chromatin condensation started in growing oocytes isolated from antral follicles presenting a diameter of 0.5 mm. This event was accompanied by a transient rise in histone H1 kinase activity which culminated in large antral follicles measuring 0.75 to 1 mm in diameter.However, the extent of histone H1 kinase activity observed in these growing oocytes remained far less important than that recorded in extracts prepared from in vitro cultured metaphase I and metaphase II oocytes. Moreover, this activity was insufficient to induce germinal vesicle breakdown which will only occur with an increasing efficiency, following in vitro culture of medium, large, and fully grown antral follicles. © 1994 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080370212
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  • 5
    Electronic Resource
    Electronic Resource
    Evidence for presence of hyaluronan binding protein on spermatozoa and its possible involvement in sperm function (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 38 (1994), S. 69-76 
    Details
    ISSN: 1040-452X
    Keywords: Hyaluronic acid binding protein ; Sperm motility ; Phosphorylation ; Epididymal maturation ; Fertilization ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Hyaluronic acid, a major component of the extracellular matrix, plays an important role in the regulation of different cellular processes, e.g., locomotion, cell-cell interaction during morphogenesis, and differentiation. Distribution of hyaluronic acid with respect to the role of sperm hyaluronidase in sperm penetration and gamete interaction is well established. In order to elucidate this mechanism, in our current study we have identified and demonstrated, for the first time, the presence of a 68-kDa cell surface hyaluronic acid binding glycoprotein (HABP) in spermatozoa of different species (rat, mice, bull, and human) by immunoblot analysis and indirect immunofluorescence using the polyclonal antibodies raised against purified HABP. Furthermore, we were able to demonstrate a differential distribution of 68-kDa HA binding protein on the sperm head, midpiece, and tail of different species. To identify its role in sperm function, we observed its declining pattern during epididymal maturation and also the inhibition of sperm-oolemmal adherence by pretreatment of the sperms with anti-HABP antibodies. We have further observed its in vivo phosphorylation in motile spermatozoa. All our data clearly indicate that sperm hyaluronan binding protein may have a specific role in sperm maturation, motility, and fertilization processes. © 1994 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080380112
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  • 6
    Electronic Resource
    Electronic Resource
    Protein and nuclear changes in pig eggs at fertilization (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 31 (1992), S. 287-296 
    Details
    ISSN: 1040-452X
    Keywords: Phosphorylation ; Protein synthesis ; Pronuclei ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The nuclear restructuring that occurs between insemination and full pronuclear formation in pig eggs is accompanied by posttranslational changes to specific egg proteins. Sperm penetration begins in vitro at 3 hr postinsemination (hpi). By 5 hr, decondensing sperm heads and anaphase II plates are observed in 50% of eggs, and, by 8 hpi, both male and female pronuclei have formed. Three consistent changes to the pattern of newly synthesised proteins are triggered in this period; they affect the 46K, 25K, and 22K polypeptides. Changes are also triggered in the 180-200K polypeptides and in the 14K polypeptides, but these are highly variable. The same changes in the prefertilization pattern were observed when prelabelled eggs were used and new protein synthesis was suppressed. The first and most abrupt change involves the apparent catabolic elimination of a group of 46K unphosphorylated polypeptides (pl 7.3-6.4), whose synthesis was greatest before germinal vesicle breakdown but declined slowly in the final phase of maturation, then declined precipitously after activation. Ageing (beyond maturation) also leads to the disappearance of these polypeptides. The progressive disappearance of a set of 25K polypeptides and the concomitant appearance of a dominant 22K polypeptide is the most characteristic fertilization-induced modification to porcine egg proteins. These modifications begin within 1 hr of sperm penetration or activation, are specific to the pig, and involve heavily phosphorylated polypeptides (25K, pl 6.7-6.0) whose synthesis is begun in the early metaphase I stage. Dual ([35S] and [32P]) labelling, protein blocking experiments, and use of alkaline phosphatase suggest that dephosphorylation selectively affects these 25K polypeptides and is mainly or wholly responsible for converting them (completely within 6 hr) to a single, new (22K, pl 7.6) species that is positively charged. The 25K/22K polypeptide modification has a close temporal relationship with the formation of the male and female pronuclei.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080310410
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  • 7
    Electronic Resource
    Electronic Resource
    IGF binding proteins and their functions (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 35 (1993), S. 368-375 
    Details
    ISSN: 1040-452X
    Keywords: Growth regulation ; Growth factor ; Mitogenesis ; Proteolysis ; Phosphorylation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The insulin-like growth factor (IGF) binding proteins (IGFBPs) have several functions, including transporting the IGFs in the circulation, mediating IGF transport out of the vascular compartment, localizing the IGFs to specific cell types, and modulating both IGF binding to receptors and growth-promoting actions. The functions of IGFBPs appear to be altered by posttranslational modifications. IGFBP-3, -4, -5, and -6 have been shown to be glycosylated. Likewise all the IGFBPs have a complex disulfide bond structure that is required for maintenance of normal IGF binding. IGFBP-2, -3, -4, and -5 are proteolytically cleaved, and specific proteases have been characterized for IGFBP-3, -4, and -5. Interestingly, attachment of IGF-I or II to IGFBP-4 results in enhancement of proteolysis, whereas attachment of either growth factor to IGFBP-5 results in inhibition of proteolytic cleavage. Cleavage of IGFBP-3 results in the appearance of a 31 kDa fragment that is 50-fold reduced in its affinity for the IGF-I or IGF-II. In spite of the reduction in its affinity, this fragment is capable of potentiating the effect of IGF-I on cell growth responses; therefore, proteolysis may be a specific mechanism that alters IGFBP modulation of IGF actions. Other processes that result in a reduction in IGF binding protein affinity are associated with potentiation of cellular responses to IGF-I and -II. Specifically, the binding of IGFBP-3 to cell surfaces is associated with its ability to enhance IGF action and with a ten- to 12-fold reduction in its affinity for IGF-I and IGF-II. Likewise, binding of IGFBP-5 to extracellular matrix (ECM) results in an eightfold reduction in its affinity and a 60% increase in cell growth in response to IGF-I. Another post-translational modification that modifies IGFBP activity is phosphorylation. IGFBP-1, -2, -3, and -5 have been shown to be phosphorylated. Phosphorylation of IGFBP-1 results in a sixfold enhancement in its affinity for IGF-I and -II. Following this enhancement of IGFBP-1 affinity, this binding protein loses its capacity to potentiate IGF-I growth-promoting activity. Future studies using site-directed mutagenesis to modify these proteins should enable us to determine the effect of these posttranslational modifications on the ability of IGFBPs to modulate IGF biologic activity. © 1993 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080350409
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  • 8
    Electronic Resource
    Electronic Resource
    Developmentally regulated testicular galactolipid sulfotransferase inhibitor is a phosphoinositol glycerolipid and insulin-mimetic (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 37 (1994), S. 462-466 
    Details
    ISSN: 1040-452X
    Keywords: Sulfogalactoglycerolipid ; Insulin-like growth factor 1 ; Spermatogenesis ; Phosphorylation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The synthesis of sulfogalactosyl-glycerolipid (SGG) is a differentiation marker in spermatogenesis restricted to the zygotene and early pachytene spermatocytes. The galactolipid sulfotransferase responsible for the synthesis of SGG is regulated by a phosphorylation mechanism. The activity of this enzyme is reduced in cells later in spermatogenesis by a low molecular weight inhibitor, which can be extracted in organic solvents and purified by reverse phase high pressure liquid chromatography (HPLC). This purified inhibitor is a potent postreceptor insulin-mimetic, which stimulates adipocyte lipogenesis more effectively than does insulin. Phosphoinositol (PI) glycolipids have been proposed as second messengers of the insulin phosphorylation cascade. These species contain a nonacetylated glucosamine, which renders them liable to cleavage by deamidation. The activity of the sulfotransferase inhibitor was lost following nitrous acid deamidation and was labile to PI specific phospholipase C digestion. Insulin and insulin-like growth factor I were found to inhibit germ cell synthesis of SGG in vitro to some degree but had no direct effect on the testicular galacto-lipid sulfotransferase assay. These results indicate that the sulfotransferase inhibitor is a glycosyl phosphoinositide similar to the lipid species, which mediate insulin signal transduction and suggest that germ cell SGG biosynthesis may be regulated by a receptor-mediated phosphorylation pathway. © 1994 Wiley-Liss, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080370414
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  • 9
    Electronic Resource
    Electronic Resource
    Inhibition of protein synthesis affects histone H1 kinase, but not chromosome condensation activity, during the first meiotic division of pig oocytes (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 41 (1995), S. 63-69 
    Details
    ISSN: 1040-452X
    Keywords: Oocyte maturation ; Phosphorylation ; P34cdc2 ; Cyclin B ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The influence of protein synthesis on the regulation of the first meiotic division was studied in pig oocytes. We show that histone H1 kinase activity gradually increases during in vitro culture of pig oocytes, reaching maximum in metaphase I stage after 24 hr of culture. However, in the presence of the protein synthesis inhibitor cycloheximide, histone H1 kinase is not activated during the whole culture period, and after 24 hr it is approximately at the same level as in prophase-stage oocytes. The gradual increase in phosphorylation of six proteins of molecular weights 39, 48, 53, 66, 96, and 120 kDa, observed during the first 24 hr of culture, was not detected when cycloheximide was added to the culture medium. Similarly, the decrease in phosphorylation of a 90-kDa protein was not seen in cycloheximide-treated oocytes. On the other hand, the levels of both MPF components, p34cdc2 and cyclin B, which were found to be nearly constant during the first meiotic division, were not influenced by cycloheximide treatment as revealed by Western blotting. The process of germinal vesicle breakdown (GVBD) was totally blocked by cycloheximide. The condensation of chromatin, however, was not influenced, suggesting that GVBD and chromosome condensation could be regulated independently. The different degrees of MPF activation involved in these processes, as well as the nature of the protein(s) which must be synthesized for triggering GVBD, are discussed. © 1995 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080410110
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  • 10
    Electronic Resource
    Electronic Resource
    Synthesis and Metabolism of the myo-Inositol Pentakisphosphates (1997)
    Weinheim : Wiley-Blackwell
    Liebigs Annalen 1997 (1997), S. 1861-1869 
    Details
    ISSN: 0947-3440
    Keywords: Inositol polyphosphates ; Phosphorylation ; Camphanates ; Inositol polyphosphate phosphatases ; Inositol polyphosphate kinases ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: All six isomeric myo-inositol pentakisphosphates (InsP5), consisting of the two meso compounds myo-inositol 1,3,4,5,6-pentakisphosphate [Ins(1,3,4,5,6)P5] (18) and myo-inositol 1,2,3,4,6-pentakisphosphate [Ins(1,2,3,4,6)P5] (22) and two pairs of enantiomers myo-inositol 1,2,4,5,6-pentakisphosphate [Ins(1,2,4,5,6)P5] (15) myo-inositol 2,3,4,5,6-pentakisphosphate [Ins(2,3,4,5,6)P5] (ent-15) and myo-inositol 1,2,3,5,6-pentakisphosphate [Ins(1,2,3,5,6)P5] (20) myo-inositol 1,2,3,4,5-pentakisphosphate [Ins(1,2,3,4,5)P5] (ent-20), respectively, were synthesized. These compounds have been found in tissue, and although not resolved as pure enantiomers, their primary metabolism in a cytosolic extract from fetal calf thymus was therefore investigated by analytical HPLC. Four isomers were dephosphorylated to singly defined inositol tetrakisphosphates, while Ins(1,2,4,5,6)P5 was phosphorylated to myo-inositol hexakisphosphate (InsP6). Interestingly, Ins(2,3,4,5,6)P5 was the only isomer which was not metabolized. These data demonstrate that chemically synthesized, enantiomerically pure inositol pentakisphosphate isomers are valuable tools for the unravelling of the metabolic pathways of InsP5 turnover in living cells.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jlac.199719970909
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