Chromium(III)-Mediated Structural Modification of Glycoprotein: Impact of the Ligand and the Oxidants

Shrivastava, H. Yamini; Nair, Balachandran Unni

doi:10.1006/bbrc.2001.5258

Cited by 41 publications

(19 citation statements)

References 22 publications

(20 reference statements)

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“…Early studies in the area of metal-promoted peptide cleavage employed metal complexes in combination with oxidoreductive additives to achieve either oxidative (68)(69)(70)(71)(72)(73)(74)(75)(76)(77)(78)(79)(80)(81)(82) Metal complexes [e.g., a Cu(I) complex of 1,10-phenanthroline (phen) or and Fe(II) complex of ethylenediaminetetraacetato (edta, ligand)] conjugated to deoxyribonucleic acid (DNA) binding ligands oxidatively cleave nucleic acids in the presence of redox additives (84,85). The redox chemistry of those coordination complexes is related to the oxidative cleavage of polypeptide backbones of proteins.…”

Section: A Agents For Oxidative Cleavage Of Proteinsmentioning

confidence: 99%

Peptide‐ or Protein‐Cleaving Agents Based on Metal Complexes

Chei¹,

Suh²

2007

Progress in Inorganic Chemistry

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Section: A Agents For Oxidative Cleavage Of Proteinsmentioning

confidence: 99%

Peptide‐ or Protein‐Cleaving Agents Based on Metal Complexes

Chei¹,

Suh²

2007

Progress in Inorganic Chemistry

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“…Aquapentaamminechromium(III) nitrate {[Cr(NH 3 ) 5 (H 2 O)](NO 3 ) 3 NH 4 NO 3 } caused phosphorylation of bovine serum albumin in the presence of ATP, whereas other Cr(III) complexes with ligands such as bipyridine, phenanthroline, en, and [1,2-bis(salicylideneamino)ethane] (salen) did not [7]. Chromium(III) complexes of salen and EDTA induced non-specific cleavage of a 1 -acid glycoprotein in the presence of H 2 O 2 , whereas [Cr(en) 3 ] 3+ was inactive [8].…”

Section: Introductionmentioning

confidence: 99%

Ultrastructural damage in chromium picolinate-treated cells: a TEM study

2002

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Chromium picolinate (CrPic) is a human dietary supplement that provides a bioavailable form of chromium(III). Its mechanism of action is unknown, and a number of toxic endpoints have been attributed to its use. Understanding the cellular effects of CrPic is important for confirmation or dismissal of these potential toxic effects. The purpose of this work was to characterize morphological damage caused by CrPic, picolinic acid, and chromic chloride in Chinese hamster ovary AA8 cells. A 48-h exposure to 80 micro g/cm(2) CrPic (0.44 mg/mL CrPic) produced 45% survival by colony formation. Transmission electron microscopy (TEM) showed 83% of analyzed cells having swollen mitochondria with degraded cristae. Apoptosis was identified by nuclear convolution and fragmentation, and cytoplasmic blebbing. Apoptosis was quantified by fluorescence microscopy with acridine orange/ethidium bromide staining. At the 80 micro g/cm(2) dose of CrPic, 37% of the cells were apoptotic cells at 48 h. An equivalent dose of picolinate, 3 mM, was much more cytotoxic and thus there was an inadequate cell number for TEM analysis. However, a lower dose of 1.5 mM induced 49% cell survival, and damaged 86% of the mitochondria, with 51% of the cells undergoing apoptosis. A dose of 1 mM chromic chloride produced 71% cell survival, and damaged 86% of the mitochondria, with 22% of the cells undergoing apoptosis. The amount of apoptosis correlated with overall cell survival by colony formation, but not with the amount of mitochondrial damage. The coordination of Cr(III) by picolinate ligands may alter the cellular chemistry of Cr(III) to make chromium picolinate a toxic form of Cr(III).

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“…Metal ions and complexes are used to effect cleavage of the polypeptide backbone under nondenaturing conditions of temperature and pH [34][35][36]41,[44][45][46][47][48][49][50][51][52]. Because mild conditions can be employed, these reagents show great promise for use in the analysis of protein solution structure, in protein engineering (e.g., the generation of semi-synthetic proteins, the proteolytic cleavage of bioengineered fusion proteins), and in therapeutics.…”

mentioning

confidence: 99%

“…Redox active metal ions and/or complexes of Cu II [3,7,17,21,44], Cr III [45], Cr V [46], Fe III [1,2,[4][5][6]8,9,11,13,14,16,18,19,21,22,[24][25][26][27][28], Ni II [23], Rh III [11], and V V [10,12,15,20] have been used to promote the oxidative cleavage of peptide amide bonds in folded proteins under nondenaturing conditions. In the majority of cases (e.g., Cu II , Cr III , Cr V , Fe III , and V V ), cleavage is thought to arise from abstraction of peptide backbone α-carbon hydrogen atoms by hydroxyl radicals and other metal-generated, reactive oxygen species [45,[53][54][55][56].…”

mentioning

confidence: 99%

“…In the majority of cases (e.g., Cu II , Cr III , Cr V , Fe III , and V V ), cleavage is thought to arise from abstraction of peptide backbone α-carbon hydrogen atoms by hydroxyl radicals and other metal-generated, reactive oxygen species [45,[53][54][55][56]. Subsequent degradation of the NH-Cα and Cα-C(O) bonds yields multiple, fragmented peptide products [57,58] (Fig.…”

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confidence: 99%

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Major Advances in the Hydrolysis of Peptides and Proteins by Metal Ions and Complexes

Grant¹,

Kassai

2006

COC

116

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Metal ions and complexes that hydrolyze peptides and proteins have become increasingly important in recent years. These reagents have shown great promise for use in a variety of applications including protein sequencing and proteomics. When metal-assisted hydrolytic cleavage is accomplished under nondenaturing conditions of temperature and pH, their use can be extended to include the study of protein function and solution structure, the generation of semisynthetic proteins, the proteolytic cleavage of bioengineered fusion proteins, and therapeutics. Yet, because of the extreme stability of the peptide amide bond, hydrolytically active metals are limited in number and there is now great interest in the development of new, more efficient reagents. In this review, we provide a description of relevant, early work with metal ions and complexes that have been used to hydrolyze unactivated peptide amide bonds in peptides and proteins. More importantly, we present an overview of recent contributions that have been made toward the development of synthetic metalloproteases that catalyze hydrolysis under near physiological conditions of temperature and pH.Dedicated to Professor Koji Nakanishi on the occasion of his 80 th birthday.

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Chromium(III)-Mediated Structural Modification of Glycoprotein: Impact of the Ligand and the Oxidants

Cited by 41 publications

References 22 publications

Peptide‐ or Protein‐Cleaving Agents Based on Metal Complexes

Peptide‐ or Protein‐Cleaving Agents Based on Metal Complexes

Ultrastructural damage in chromium picolinate-treated cells: a TEM study

Major Advances in the Hydrolysis of Peptides and Proteins by Metal Ions and Complexes

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