Defining the Roles of Collagen and Collagen‐Like Proteins Within the Proteome

Baronas-Lowell, Diane; Lauer‐Fields, Janelle L.; Fields, Gregg B.

doi:10.1081/jlc-120023245

Cited by 13 publications

(11 citation statements)

References 155 publications

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“…In this study, the injured tissues showed increased CLP levels compared to the naive. This suggests that collagen is biosynthesized to recover the injured tissues because most collagens assist in anchoring cells to the extracellular matrix and some function in cellular regulation (Baronas-Lowell et al, 2003). Moreover, CoQ10-treated tissues showed significantly increased CLP levels, compared to the control.…”

Section: Effect Of Coq10 On Collagen-like Polymer (Clp) Level In Skinmentioning

confidence: 96%

Effect of coenzyme Q10 on cutaneous healing in skin-incised mice

et al. 2009

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Coenzyme Q10 (CoQ10) is a biosynthesized quinone with 10 isoprene side chains in humans. To investigate the anti-inflammatory and wound healing effect of CoQ10, we performed in vivo and in vitro experiments. In vivo studies, there were 3 groups; Naive (without skin incision), Control (with skin incision) and CoQ10 (100 mg/kg treatment with skin incision). Collagen-like polymer (CLP) level of CoQ10 group was increased significantly compared to the control group (p<0.05). Also, CoQ10 group showed significant inhibition on myeloperoxidase (MPO) and PLA(2) level compared to the control group (p<0.05). These data show that CoQ10 may have an anti-inflammatory and a wound healing effect. CoQ10 showed significant antioxidant activity in vivo on malondialdehyde (MDA) and superoxide dismutase (SOD) levels compared to the control group (p<0.05). Although CoQ10 did not show antioxidant activity in cell free system of DPPH radical scavenge, it had a potent antioxidant activity in cell culture system of both silica- and zymosan-induced reactive oxygen species generation using Raw 264.7 cells. This result may be associated with the conversion of CoQ10 to the reduced form (CoQ10H(2)) in the presence of some kinds of intracellular reducing agents. In conclusion, it is considered that CoQ10 appears to have a cutaneous healing effect in vivo, which may be related to the secondary action of CoQ10.

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Section: Effect Of Coq10 On Collagen-like Polymer (Clp) Level In Skinmentioning

confidence: 96%

Effect of coenzyme Q10 on cutaneous healing in skin-incised mice

et al. 2009

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“…The triple-helical structure of collagen renders it resistant to most proteases. In vertebrates, enzymes capable of cleaving the triple-helical structure include cathepsin K and collagenolytic matrix metalloproteinase (MMP) 2 family members. One or more of the interstitial collagens (types I-III) are hydrolyzed within their triple-helical domain by MMP-1, MMP-2, MMP-8, MMP-13, MMP-18, MT1-MMP (MMP- 14), and MT2-MMP (MMP-15) (4,5).…”

mentioning

confidence: 99%

“…Current studies identify at least 25 different collagen types, each with a specific role in the extracellular matrix (1,2). The hydrolysis of collagen (collagenolysis) is one of the committed steps in extracellular matrix turnover (3).…”

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confidence: 99%

The Roles of Substrate Thermal Stability and P2 and P1′ Subsite Identity on Matrix Metalloproteinase Triple-helical Peptidase Activity and Collagen Specificity

Minond

Lauer‐Fields

Čudić

et al. 2006

Journal of Biological Chemistry

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134

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The hydrolysis of collagen (collagenolysis) is one of the committed steps in extracellular matrix turnover. Within the matrix metalloproteinase (MMP) family distinct preferences for collagen types are seen. The substrate determinants that may guide these specificities are unknown. In this study, we have utilized 12 triple-helical substrates in combination with 10 MMPs to better define the contributions of substrate sequence and thermal stability toward triple helicase activity and collagen specificity. In general, MMP-13 was found to be distinct from MMP-8 and MT1-MMP(⌬279 -523), in that enhanced substrate thermal stability has only a modest effect on activity, regardless of sequence. This result correlates to the unique collagen specificity of MMP-13 compared with MMP-8 and MT1-MMP, in that MMP-13 hydrolyzes type II collagen efficiently, whereas MMP-8 and MT1-MMP are similar in their preference for type I collagen. In turn, MMP-1 was the least efficient of the collagenolytic MMPs at processing increasingly thermal stable triple helices and thus favors type III collagen, which has a relatively flexible cleavage site. Gelatinases (MMP-2 and MMP-9(⌬444 -707)) appear incapable of processing more stable helices and are thus mechanistically distinct from collagenolytic MMPs. The collagen specificity of MMPs appears to be based on a combination of substrate sequence and thermal stability. Analysis of the hydrolysis of triple-helical peptides by an MMP mutant indicated that Tyr 210 functions in triple helix binding and hydrolysis, but not in processing triple helices of increasing thermal stabilities. Further exploration of MMP active sites and exosites, in combination with substrate conformation, may prove valuable for additional dissection of collagenolysis and yield information useful in the design of more selective MMP inhibitors.Current studies identify at least 25 different collagen types, each with a specific role in the extracellular matrix (1, 2). The hydrolysis of collagen (collagenolysis) is one of the committed steps in extracellular matrix turnover (3). The triple-helical structure of collagen renders it resistant to most proteases. In vertebrates, enzymes capable of cleaving the triple-helical structure include cathepsin K and collagenolytic matrix metalloproteinase (MMP) 2 family members. One or more of the interstitial collagens (types I-III) are hydrolyzed within their triple-helical domain by MMP-1, MMP-2, MMP-8, MMP-13, MMP-18, MT1-MMP (MMP-14), and MT2-MMP (MMP-15) (4, 5). MMP-9 cleaves the triple helix of types V and XI collagen (6) but not of types I-III (7).Types I-III collagen are all fibrillar interstitial collagens, but differences in their sequences, glycosylation patterns, and tissue distribution have long been documented (1, 8 -10). For example, type I collagen has a low level of glycosylation and is found in skin, bone, cornea, and tendon, whereas type II collagen has much higher levels of glycosylation and is found in cartilage (1, 9). In a similar fashion to type I collagen, type III col...

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“…The pellet was washed with methyl tert-butyl ether and airdried. Four different peptides were synthesized: a. Gly-Phe-Hyp-Gly-Leu-Hyp-Gly-Ala-Lys-Gly-Glu-NH 2 (peptide 1); b. Gly-Phe-Hyp-Gly-Leu-Hyp-Gly-Ala-Hyl-Gly-Glu-NH 2 (peptide 2); c. Pro-Hyp-Gly-Arg-Lys-Gly-Ala-Lys-Gly-Lys-Arg-Gly-ProHyp-Gly-NH 2 (peptide 3) d. Ile-Lys-Gly-Ile-Lys-Gly-Ile-Lys-Gly-NH 2 (peptide 4).…”

Section: Synthesis Of Peptidesmentioning

confidence: 99%

“…Collagens play an important role in maintaining the integrity of various tissues and organs, and in regulating cellular behavior. [1][2][3] The characteristic structural feature of collagen is a triple helix of high mechanical strength.…”

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Development of a convenient peptide‐based assay for lysyl hydroxylase

Čudić¹,

Patel²,

Lauer‐Fields³

et al. 2008

Biopolymers

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Hydroxylysine (Hyl) is a posttranslationally modified amino acid found mainly in collagens, the most abundant protein in mammals. Lysyl hydroxylase (LH) catalyzes the hydroxylation of the C‐5 position of a Lys residue, resulting in the production of Hyl. Mechanistically, LH incorporates one oxygen atom into both Lys and 2‐oxoglutarate; the latter is decarboxylated to form succinate and CO2. To develop a convenient, RP‐HPLC based LH assay, we used Fmoc solid‐phase methodology to synthesize three different peptides designed as LH substrates and one peptide corresponding to an LH product. Peptides were characterized by RP‐HPLC, MALDI‐TOF mass spectrometry and CD spectroscopy. Separation of peptides was examined under a variety of RP‐HPLC conditions. The best results were achieved using peptide derivatization (1‐anthroylnitrile for organic phase and dansyl chloride for aqueous phase) prior to RP‐HPLC analysis. The products (di‐ and tetra‐substituted Lys‐ and Hyl‐containing peptides) were well resolved by RP‐HPLC. The resolution of each peak allows for quantification of peak areas, which in turn, when examined as a function of time, can be utilized for studying the kinetics of LH catalyzed reactions. Most significantly, the RP‐HPLC assay directly monitors the Hyl containing product. Prior LH assay methods are multi‐step, require radio‐labeled substrates, and/or measure depletion of 2‐oxoglutarate or formation of CO2. Since the LH reaction with 2‐oxoglutarate is uncoupled from Lys hydroxylation, the most accurate assay of LH activity should monitor the formation of Hyl. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90: 330–338, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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Defining the Roles of Collagen and Collagen‐Like Proteins Within the Proteome

Cited by 13 publications

References 155 publications

Effect of coenzyme Q10 on cutaneous healing in skin-incised mice

Effect of coenzyme Q10 on cutaneous healing in skin-incised mice

The Roles of Substrate Thermal Stability and P2 and P1′ Subsite Identity on Matrix Metalloproteinase Triple-helical Peptidase Activity and Collagen Specificity

Development of a convenient peptide‐based assay for lysyl hydroxylase

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