Racemization of aspartic acid in human proteins

Ritz‐Timme, Stefanie; Collins, Matthew J.

doi:10.1016/s0047-6374(01)00363-3

Cited by 169 publications

(141 citation statements)

References 111 publications

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“…Little quantitative data are available for the raft of changes that long-lived proteins undergo, although it is likely that age-dependent degradation of abundant proteins will result in measurable changes in the tissues of older people (Ritz-Timme and Collins 2002;Truscott 2010). Several sites in the human body, including lung (Shapiro et al 1991), heart (Powell et al 1992), brain (Shapira et al 1988), teeth (Helfman and Bada 1975), skin (Verzijl et al 2000), intervertebral discs (Ritz and Schutz 1993) and cartilage (Maroudas et al 1992) contain abundant proteins that are very long-lived, with half-lives measured in decades.…”

Section: Introductionmentioning

confidence: 99%

Racemisation and human cataract. d-Ser, d-Asp/Asn and d-Thr are higher in the lifelong proteins of cataract lenses than in age-matched normal lenses

Hooi

Truscott

2010

AGE

105

122

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Astract Several amino acids were found to undergo progressive age-dependent racemisation in the lifelong proteins of normal human lenses. The two most highly racemised were Ser and Asx. By age 70, 4.5% of all Ser residues had been racemised, along with >9% of Asx residues. Such a high level of inversion, equivalent to between 2 and 3 D -amino acids per polypeptide chain, is likely to induce significant denaturation of the crystallins in aged lenses. Thr, Glx and Phe underwent age-dependent racemisation to a smaller degree. In model experiments, D -amino acid content could be increased simply by exposing intact lenses to elevated temperature. In cataract lenses, the extent of racemisation of Ser, Asx and Thr residues was significantly greater than for agematched normal lenses. This was true, even for cataract lenses removed from patients at the earliest ages where age-related cataract is observed clinically. Racemisation of amino acids in crystallins may arise due to prolonged exposure of these proteins to ocular temperatures and increased levels of racemisation may play a significant role in the opacification of human lenses.

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Section: Introductionmentioning

confidence: 99%

Racemisation and human cataract. d-Ser, d-Asp/Asn and d-Thr are higher in the lifelong proteins of cataract lenses than in age-matched normal lenses

Hooi

Truscott

2010

AGE

105

122

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“…Thus, the ring structure can be transformed from L-aspartic acid into D-aspartic acid rapidly. In addition, formation of D-aspartic acids also involves asparagines (Asn) by deamidation process (McCudden & Kraus 2006;Ritz-Timme & Collins 2002). Additionally, the racemization rate of aspartic acid in peptide bond is due to reaction of succinimide intermediate formation (Geiger & Clarke 1987;Radkiewicz et al 1996).…”

Section: Aspartic Acid Racemizationmentioning

confidence: 99%

Aspartic Acid Racemization Method for Age Estimation in Human Tissues: A Review

Gumpangseth¹,

Mahakkanukrauh²

2017

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“…Thus, racemization of aspartic acid can be utilized for age indicator of individuals and also investigated protein aging. In addition, there was found that aspartic acid racemization process involve some pathological diseases Jousse et al 2004;Ritz-Timme & Collins 2002). Pathway of aspartic acid racemization occurs in proteins via a succinimide intermediated (succinyl residue or Asu) and the chiral center of succinimide can be easily racemized.…”

Section: Racemization Of Aspartic Acidmentioning

confidence: 99%

“…It make this structure can be converted from L-form of aspartic acid to D-form of aspartic acid (McCudden & Kraus 2006). Therefore, rate of racemization depends on the structure of amino acids within polypeptide that related to rapid accumulation of D-aspartic acids in proteins (Geiger & Clarke 1987;Radkiewicz et al 1996;Ritz-Timme & Collins 2002).…”

Section: Racemization Of Aspartic Acidmentioning

confidence: 99%

Age Estimation by Using Aspartic Acid Racemization from Purified Elastin of Aorta

Komutrattananont¹,

Mahakkanukrauh²

2017

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ABSTRAK ABSTRACTAge estimation is the one of biological profiles which plays an important role in identification in forensic field. The application of biochemical approach known 171 Age Estimation by Aspartic Acid Racemization Med & Health Dec 2017;12(2): 170-178 depend on the variation methods and skill of the specialist (Dobberstein et al. 2010). However, there are still high accuracy methods in age estimation which complicate the procedure more. One of these methods which has been accomplished in age estimation is amino acid racemization. AMINO ACID RACEMIZATIONAmino acids are vital components in living organisms and are subunit structure of all proteins. The amino acid structure is composed of a carbon atom (C) which has four different groups include an amino group (-NH 2 ), a carboxyl group (-COOH), a hydrogen atom (-H), and side chain or Rgroup (-R). Side chain is different part of amino acids that depends upon the kind of as aspartic acid racemization in human provides more accuracy and less error of estimated age in age determination. During aging, amino acids within protein transform between D-and L-form (racemization), which results in increasing concentration of D-amino acids. This change of amino acids is related to aging. Aspartic acid has been generally applied in racemization because it has fastest rate of racemization. Racemization of aspartic acid not only takes place in teeth and many kinds of bone, but also can occur in the flexible structure which contain mostly elastin. For example, skin yellow ligament, lung parenchyma, and aorta. Elastin is essential protein which is comprised most composition of several structures and it is major content in the elastic fibers. Additionally, elastin is the longest lasting protein in the body with slow metabolic turnover rate. Recently, there is a purification technique to obtain only single protein in human aorta.There was a good correlation between degree of racemization (D/L ratio) and age. Therefore, aspartic acid racemization by purifies elastin from aorta is a one of indicator for age estimation. This review provides an overview of aspartic acid racemization, elastin protein, purification method bases on racemization and the application of D/L ratio by purified of elastin in artery for age estimation.

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Racemization of aspartic acid in human proteins

Cited by 169 publications

References 111 publications

Racemisation and human cataract. d-Ser, d-Asp/Asn and d-Thr are higher in the lifelong proteins of cataract lenses than in age-matched normal lenses

Racemisation and human cataract. d-Ser, d-Asp/Asn and d-Thr are higher in the lifelong proteins of cataract lenses than in age-matched normal lenses

Aspartic Acid Racemization Method for Age Estimation in Human Tissues: A Review

Age Estimation by Using Aspartic Acid Racemization from Purified Elastin of Aorta

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