Proteomics Center publications (MU)The items in this collection are the scholarly output of the faculty, staff, and students of the Proteomics Center.https://hdl.handle.net/10355/32372024-03-19T01:48:37Z2024-03-19T01:48:37ZAccumulation of glial fibrillary acidic protein and histone H4 in brain storage bodies of Tibetan terriers with hereditary neuronal ceroid lipofuscinosisKatz, Martin L.Sanders, Douglas N., 1973-Mooney, Brian P.Johnson, Gary S.https://hdl.handle.net/10355/32462020-06-23T19:47:21Z2007-01-01T00:00:00ZAccumulation of glial fibrillary acidic protein and histone H4 in brain storage bodies of Tibetan terriers with hereditary neuronal ceroid lipofuscinosis
Katz, Martin L.; Sanders, Douglas N., 1973-; Mooney, Brian P.; Johnson, Gary S.
The neuronal ceroid lipofuscinoses (NCLs) are inherited neurodegenerative diseases characterized by massive accumulation of autofluorescent storage bodies in neurons and other cells. A late-onset form of NCL occurs in Tibetan terrier dogs. Gel electrophoretic analyses of isolated storage body proteins from brains of affected dogs indicated that a protein of approximately 50 kDa was consistently prominent and a 16 kDa component was present in some brain storage body preparations. Mass spectral analysis identified the 50 kDa protein as glial fibrillary acidic protein (GFAP), isoform 2. GFAP identification was supported by immunoblot and immunohistochemical analyses. Histone H4 was the major protein in the 16 kDa component. Specific accumulation of GFAP and histone H4 in storage bodies has not been previously reported for any of the NCLs. Tibetan terrier NCL may be the canine correlate of one of the human adult-onset NCLs for which the genetic bases and storage body compositions have not yet been determined.
2007-01-01T00:00:00ZAnti-chaperone [eszett]A3/A1102-117 peptide interacting sites in human aB-crystallinRao, GuruprasadSanthoshkumar, PutturSharma, K. Krishnahttps://hdl.handle.net/10355/32432020-06-23T19:47:21Z2008-01-01T00:00:00ZAnti-chaperone [eszett]A3/A1102-117 peptide interacting sites in human aB-crystallin
Rao, Guruprasad; Santhoshkumar, Puttur; Sharma, K. Krishna
Purpose: Our previous work identified 23 low molecular weight (<3.5 kDa) crystallin peptides in the urea-soluble fractions of normal young, normal aged, and aged cataract human lenses. We found that one of these crystallin fragments, [beta]A3/ A1102-117 peptide (SDAYHIERLMSFRPIC), that are present in aged and cataract lens, increased the scattering of light by [beta]- and [gamma]-crystallins and alcohol dehydrogenase (ADH) and also reduced the chaperone-like activity of [alpha][beta]-crystallin. The present study was performed to identify the interacting sites of the [beta]A3/A1102-117 peptide in [alpha]B-crystallin. Methods: [beta]A3/A1102-117 peptide was first derivatized with sulfo-succinimidyl-2-[6-(biotinamido)-2-{pazidobenzamido}- hexanoamido] ethyl-1-3 dithio propionate (sulfo-SBED), a photoactivable, heterotrifunctional biotincontaining cross-linker. The biotin-derivatized peptide was then incubated with [alpha]B-crystallin at 37 [degrees]C for 2 h to allow complex formation followed by photolysis to facilitate the transfer of the biotin label from the peptide to [alpha]B-crystallin. Label transfer was confirmed by western blot, and the labeled [alpha]B-crystallin was digested with trypsin. Tryptic peptides from [alpha]B-crystallin carrying the biotin label were purified by avidin affinity chromatography, and [beta]A3/A1102-117 peptide interacting sites in [alpha]B-crystallin were identified by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF MS) and nanospray quadrupole time-of-flight mass spectrometry (QqTOF MS/MS). Results: We found that the [beta]A3/A1102-117 peptide interacted with [alpha]B-crystallin regions 70LEKDR74, 83HFSPEELKVK92, 91VKVLGDVIEVHGK103, 93VLGDVIEVHGKHEER107, and 121KYR123, which are part of the [alpha]-crystallin domain, and were previously shown to be part of the functional chaperone site in [alpha]B-crystallin. The [beta]A3/A1102-117 peptide also interacted with regions at the COOH-terminal extension of [alpha]B-crystallin, 150KQVSGPER157, 164EEKPAVTAAPK174, and 164EEKPAVTAAPKK175. When two of the hydrophobic residues of [beta]A3/A1102-117 peptide were replaced with hydrophilic residues, the resulting substituted peptide, SDADHGERLMSFRPIC, did not show the anti-chaperone property. Conclusions: This study confirmed the interactions between a low molecular weight peptide derived from [beta]A3/A1- crystallin found in aged and cataract lenses and [alpha]B-crystallin. The binding of [beta]A3/A1102-117 peptide to the chaperone site and the COOH-terminal extension of [alpha]B-crystallin may explain its anti-chaperone property.
2008-01-01T00:00:00ZCell wall proteome in the maize primary root elongation zone. II. Region-specific changes in water soluble and lightly ionically bound proteins under water deficitZhu, JinmingAlvarez, SophieMarsh, Ellen L.LeNoble, Mary E.Cho, In-jeong, 1970-Sivaguru, MayandiChen, SixueNguyen, Henry T.Wu, YajunSchachtman, Daniel P.Sharp, Bob (Robert E.)https://hdl.handle.net/10355/32502020-06-23T19:47:19Z2007-01-01T00:00:00ZCell wall proteome in the maize primary root elongation zone. II. Region-specific changes in water soluble and lightly ionically bound proteins under water deficit
Zhu, Jinming; Alvarez, Sophie; Marsh, Ellen L.; LeNoble, Mary E.; Cho, In-jeong, 1970-; Sivaguru, Mayandi; Chen, Sixue; Nguyen, Henry T.; Wu, Yajun; Schachtman, Daniel P.; Sharp, Bob (Robert E.)
Previous work on the adaptation of maize (Zea mays) primary roots to water deficit showed that cell elongation is maintained preferentially toward the apex, and that this response involves modification of cell wall extension properties. To gain a comprehensive understanding of how cell wall protein (CWP) composition changes in association with the differential growth responses to water deficit in different regions of the elongation zone, a proteomics approach was used to examine water soluble and loosely ionically bound CWPs. The results revealed major and predominantly region-specific changes in protein profiles between well-watered and water-stressed roots. In total, 152 water deficit-responsive proteins were identified and categorized into five groups based on their potential function in the cell wall: reactive oxygen species (ROS) metabolism, defense and detoxification, hydrolases, carbohydrate metabolism, and other/unknown. The results indicate that stress-induced changes in CWPs involve multiple processes that are likely to regulate the response of cell elongation. In particular, the changes in protein abundance related to ROS metabolism predicted an increase in apoplastic ROS production in the apical region of the elongation zone of water-stressed roots. This was verified by quantification of hydrogen peroxide content in extracted apoplastic fluid and by in situ imaging of apoplastic ROS levels. This response could contribute directly to the enhancement of wall loosening in this region. This large-scale proteomic analysis provides novel insights into the complexity of mechanisms that regulate root growth under water deficit conditions and highlights the spatial differences in CWP composition in the root elongation zone.
2007-01-01T00:00:00ZComposition, vigor, and proteome of mature soybean seeds developed under high temperatureRen, C.Bilyeu, Kristin D.Beuselink, P. R.https://hdl.handle.net/10355/32382020-06-23T19:47:20Z1999-01-01T00:00:00ZComposition, vigor, and proteome of mature soybean seeds developed under high temperature
Ren, C.; Bilyeu, Kristin D.; Beuselink, P. R.
The effects of high temperature treatment on soybean [Glycine max (L.) Merr.] seed composition, vigor, and proteome were investigated using mature dry seeds harvested from plants grown in environment-controlled chambers. High day/night temperatures (37/30[degrees]C) from stages R5 through R8 altered ratios of individual fatty acids to total fatty acid compared to the control (27/18[degrees]C). Concentration of sugars decreased, but total protein and phytic acid concentration were unchanged. High temperature resulted in a greater proportion of abnormal seeds, but normal-appearing seed exhibited reduced germination and vigor. Proteomic analysis detected 20 protein identities whose accumulations were changed by the high temperature. Fourteen spots were identified as seven subunits of seed storage proteins. The remaining six proteins were identified as those responding to abiotic stresses or having a function in respiration: (i) sucrose binding protein, (ii) Class III acidic endochitinase, (iii) heat shock protein (HSP22), (iv) late embryo abundant protein, (v) Bowman-Birk proteinase inhibitor, and (vi) formate dehydrogenase. High temperature during seed development changed soybean seed composition and decreased seed vigor, but also changed seed protein expression profiles.
1999-01-01T00:00:00Z