Distribution of bovine and rabbit lens α-crystallin products by MALDI imaging mass spectrometry

Molecular Vision

Volumn 14, Issue , 2008, Pages 171-179

  Grey, Angus C ^a   Schey, Kevin L ^a  

^a MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL; ALPHA CRYSTALLIN; PROTEIN SUBUNIT; XYLENE;

ANIMAL TISSUE; ARTICLE; CELL DIFFERENTIATION; CONTROLLED STUDY; COW; CRYOPRESERVATION; CRYSTALLIZATION; FROZEN SECTION; LENS; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR IMAGING; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DETERMINATION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; RABBIT; TISSUE PREPARATION;

ALPHA-CRYSTALLINS; ANIMALS; CATTLE; LENS, CRYSTALLINE; PEPTIDE FRAGMENTS; PHOSPHORYLATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; RABBITS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 38849146266     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article

References (40)

1. Bassnett S. The fate of the Golgi apparatus and the endoplasmic reticulum during lens fiber cell differentiation. Invest Ophthalmol Vis Sci 1995; 36:1793-803.
2. Bassnett S, Beebe DC. Coincident loss of mitochondria and nuclei during lens fiber cell differentiation. Dev Dyn 1992; 194:85-93.
3. Zampighi GA, Simon SA, Hall JE. The specialized junctions of the lens. Int Rev Cytol 1992; 136:185-225.
4. Wistow GJ, Piatigorsky J. Lens crystallins: The evolution and expression of proteins for a highly specialized tissue. Annu Rev Biochem 1988; 57:479-504.
5. Fagerholm PP, Philipson BT, Lindström B. Normal human lens - the distribution of protein. Exp Eye Res 1981; 33:615-20.
6. Donaldson PJ, Grey AC, Merriman-Smith BR, Sisley AM, Soeller C, Cannell MB, Jacobs MD. Functional imaging: new views on lens structure and function. Clin Exp Pharmacol Physiol 2004; 31:890-5.
7. Lin JS, Eckert R, Kistler J, Donaldson P. Spatial differences in gap junction gating in the lens are a consequence of connexin cleavage. Eur J Cell Biol 1998; 76:246-50.
8. Gonen T, Cheng Y, Kistler J, Walz T. Aquaporin-0 membrane junctions form upon proteolytic cleavage. J Mol Biol 2004; 342:133745.
9. Kamei A, Hamaguchi T, Matsuura N, Masuda K. Does post-translational modification influence chaperone-like activity of alpha-crystallin? I. Study on phosphorylation. Biol Pharm Bull 2001; 24:96-9.
10. Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 1992; 89:10449-53.
11. Aquilina JA, Benesch JL, Ding LL, Yaron O, Horwitz J, Robinson CV. Subunit exchange of polydisperse proteins: mass spectrometry reveals consequences of alphaA-crystallin truncation. J Biol Chem 2005; 280:14485-91.
12. Takemoto L, Emmons T, Horwitz J. The C-terminal region of alpha-crystallin: involvement in protection against heat-induced denaturation. Biochem J 1993; 294:435-8.
13. Takeuchi N, Ouchida A, Kamei A. C-terminal truncation of alpha-crystallin in hereditary cataractous rat lens. Biol Pharm Bull 2004; 27:308-14.
14. Aquilina JA, Benesch JL, Ding LL, Yaron O, Horwitz J, Robinson CV. Phosphorylation of alphaB-crystallin alters chaperone finiction through loss of dimeric substructure. J Biol Chem 2004; 279:28675-80.
15. Ecroyd H, Meehan S, Horwitz J, Aquilina JA, Benesch JL, Robinson CV, Macphee CE, Carver JA. Mimicking phosphorylation of αB-crystallin affects its chaperone activity. Biochem J 2007; 401:129-41.
16. Ito H, Kamei A, Iwamoto I, Inaguma Y, Nohara D, Kato K. Phosphorylation-induced change of the oligomerization state of alpha B-crystallin. J Biol Chem 2001; 276:5346-52.
17. Koteiche HA, McHaourab HS. Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in αB-crystallin. J Biol Chem 2003; 278:10361-7.
18. Moroni M, Garland D. In vitro dephosphorylation of alpha-crystallin is dependent on the state of oligomerization. Biochim Biophys Acta 2001; 1546:282-90.
19. Colvis C, Garland D. Posttranslational modification of human αA-Crystallin: Correlation with electrophoretic migration. Arch Biochem Biophys 2002; 397:319-23.
20. Garland DL, Duglas-Tabor Y, Jimenez-Asensio J, Datiles MB, Magno B. The nucleus of the human lens: Demonstration of a highly characteristic protein pattern by two-dimensional electrophoresis and introduction of a new method of lens dissection. Exp Eye Res 1996; 62:285-91.
21. Han J, Schey KL. MALDI tissue imaging of ocular lens α-crystallin. Invest Ophthalmol Vis Sci 2006; 47:2990-6.
22. Chiesa R, Gawinowicz-Kolks MA, Kleiman NJ, Spector A. The phosphorylation sites of the B2 chain of bovine alpha-crystallin. Biochem Biophys Res Commun 1987; 144:1340-7.
23. Smith JB, Sun Y, Smith DL, Green B. Identifitation of post-translational modifications of bovine lens αB-crystallins by mass spectrometry. Protein Sci 1992; 1:601-8.
24. Smith JB, Thevenon-Emeric G, Smith DL, Green B. Elucidation of the primary structures of proteins by mass spectrometry. Anal Biochem 1991; 193:118-24.
25. Borchman D, Yappert MC, Afzal M. Lens lipids and maximum lifespan. Exp Eye Res 2004; 79:761-8.
26. Rujoi M, Estrada R, Yappert MC. In situ MALDI-TOF MS regional analysis of neutral phospholipids in lens tissue. Anal Chem 2004; 76:1657-63.
27. Voorter CEM, de Haard-Hoekman WA, van den Oetelaar PJ, Bloemendal H, de Jong WW. Spontaneous peptide bond cleavage in aging alpha-crystallin through a succinimide intermediate. J Biol Chem 1988; 263:19020-3.
28. Ueda Y, Fukiage C, Shih M, Shearer TR, David LL. Mass measurements of c-terminally truncated alpha-crystallins from two-dimensional gels identify 1p82 as a major endopeptidase in rat lens. Mol Cell Proteomics 2002; 1:357-65.
29. Sharma KK, Kumar RS, Kumar GS, Quinn PT. Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin. J Biol Chem 2000; 275:3767-71.
30. Chiesa R, Gawinowicz-Kolks MA, Spector A. The phosphorylation of the primary gene products of α-crystallin. J Biol Chem 1987; 262:1438-41.
31. Spector A, Chiesa R, Sredy J, Garner W. cAMP-dependent phosphorylation of bovine lens α-crystallin. Proc Natl Acad Sci USA 1985; 82:4712-6.
32. Voorter CEM, Mulders JWM, Bloemendal H, de Jong WW. Some aspects of the phosphorylation of α-crystallin A. Eur J Biochem 1986; 160:203-10.
33. Chiesa I, Spector A. The dephosphorylation of lens α-crystallin A chain. Biochem Biophys Res Commun 1989; 162:1494-501.
34. Ifeanyi F, Takemoto LJ. Specificity of alpha-crystallin binding to the lens membrane. Curr Eye Res 1990; 9:259-65.
35. Mulders JWM, Stokkermans J, Leunissen JAM, Benedetti EL, Bloemendal H, de Jong WW. Interaction of α-crystallin with lens plasma membranes: affinity for MP26. Eur J Biochem 1985; 152:721-8.
36. Bennardini F, Wrzosek A, Chiesi M. αB-crystallin in cardiac tissue. Association with actin and desmin filaments. Circ Res 1992; 71:288-94.
37. Carter JM, Hutcheson AM, Quinlan RA. In vitro studies on the assembly properties of the lens proteins CP49, CP115: co-assembly with α-crystallin but not vimentin. Exp Eye Res 1995; 60:181-92.
38. Gopalakrishnan S, Takemoto L. Binding of actin to lens α-crystallins. Curr Eye Res 1992; 11:929-33.
39. Nicholl ID, Quinlan RA. Chaperone activity of α-crystallins modulates intermediate filament assembly. EMBO J 1994; 13:945-53.
40. Wang K, Spector A. alpha-crystallin stabilizes actin filaments and prevents cytochalasin-induced depolymerization in a phosphorylation-dependent manner. Eur J Biochem 1996; 242:56-66.