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Tanzer, Marvin L.

doi:10.1007/978-1-4757-4602-0_4

Cited by 54 publications

(15 citation statements)

References 103 publications

(105 reference statements)

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“…The ligaments contained DHLNL, which is known to be specific to bone or cartilage collagen, as the major reducible cross-link [36]. The amount of DHLNL in ACL tissue was much higher than in the other ligaments.…”

Section: Discussionmentioning

confidence: 99%

Biochemical properties of collagen from ligaments and periarticular tendons of the human knee

Fujii

Yamagishi

Nagafuchi

et al. 1994

Knee Surg, Sports traumatol, Arthroscopy

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The biochemical properties of collagens from the periarticular connective tissues of the human knee (ligaments, semitendinosus and gracilis tendons, and the iliotibial band) were investigated in subjects ranging from 20 to 70 years of age. Although the total collagen content of most tissues was more than 90% of the dry weight, the anterior cruciate ligament and the iliotibial band had relatively low collagen contents. There were no significant changes in the tissue collagen content with aging. However, the anterior cruciate ligament and the patellar tendon of the 20-year-old subject had a higher content of soluble collagen than the other ligaments and tendons. The iliotibial band of the 20-year-old subject contained more collagen that was soluble by a combination of salt, sodium citrate extractions and pepsin digestion. Dihydroxylysinonorleucine was the major reducible cross-link of collagen from all the ligaments. The amount of dihydroxylysinonorleucine in the anterior cruciate ligament of the 20-year-old subject was much higher than that in the other ligaments. In contrast, the tendons and the iliotibial band contained a large amount of histidino-hydroxymerodesmosine and hydroxylysinonorleucine, while the patellar tendon was the only tendon with a significant content of dihydroxylysinonorleucine. Hydroxypyridinium non-reducible cross-links were more abundant in collagens from ligaments than in collagens from the other tissues. The cross-link study and the analysis of collagen solubility showed that patellar tendon collagen more closely resembled the collagen from the anterior cruciate ligament than that from periarticular tendons. It was also shown that the anterior cruciate ligament contains relatively immature collagen compared with the other ligaments.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Discussionmentioning

confidence: 99%

Biochemical properties of collagen from ligaments and periarticular tendons of the human knee

Fujii

Yamagishi

Nagafuchi

et al. 1994

Knee Surg, Sports traumatol, Arthroscopy

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“…Michael addition of N3 imidazole of histidine to the ACP produces deH-AH (dehydro-aldolhistidine) which can further condense with the ε-amino group of hydroxylysine forming an aldimine bond to produce deH-HHMD (dehydro-histidinohydroxymerodesmosine) [105] (Figure 5), one of the major cross-links in soft connective tissue collagen [62,106]. This crosslink, which involves four amino acids, has the most complex chemical structure in all of the known collagen cross-links.…”

Section: Extracellular Lysine Modificationsmentioning

confidence: 99%

Lysine post-translational modifications of collagen

Yamauchi

Sricholpech

2012

Essays in Biochemistry

491

497

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Type I collagen is the most abundant structural protein in vertebrates. It is a heterotrimeric molecule composed of two α1 chains and one α2 chain, forming a long uninterrupted triple helical structure with short non-triple helical telopeptides at both the N- and C-termini. During biosynthesis, collagen acquires a number of post-translational modifications, including lysine modifications, that are critical to the structure and biological functions of this protein. Lysine modifications of collagen are highly complicated sequential processes catalysed by several groups of enzymes leading to the final step of biosynthesis, covalent intermolecular cross-linking. In the cell, specific lysine residues are hydroxylated to form hydroxylysine. Then specific hydroxylysine residues located in the helical domain of the molecule are glycosylated by the addition of galactose or glucose-galactose. Outside the cell, lysine and hydroxylysine residues in the N- and C-telopeptides can be oxidatively deaminated to produce reactive aldehydes that undergo a series of non-enzymatic condensation reactions to form covalent intra- and inter-molecular cross-links. Owing to the recent advances in molecular and cellular biology, and analytical technologies, the biological significance and molecular mechanisms of these modifications have been gradually elucidated. This chapter provides an overview on these enzymatic lysine modifications and subsequent cross-linking.

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“…Peroxidase-mediated tyrosine-tyrosine cross-links are involved in the hardening of the sea urchin fertilization membrane (6,13), and a variety of cross-links involving lysine oxidase are present in collagen (10,35).…”

mentioning

confidence: 99%

Cloning and characterization of a cluster of genes encoding polypeptides present in the insoluble fraction of the spore coat of Bacillus subtilis

1993

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The Bacilus subtilis spore coat is composed of at least 15 polypeptides plus an insoluble protein fraction arranged in three morphological layers. The insoluble fraction accounts for about 30% of the coat protein and is resistant to solubilization by a variety of reagents, implying extensive cross-linking. A dodecapeptide was purified from this fraction by formic acid hydrolysis and reverse-phase high-performance liquid chromatography. This peptide was sequenced, and a gene designated cotX was cloned by reverse genetics. The cotX gene encoding the dodecapeptide at its amino end was clustered with four other genes designated cotV, cotW, cotY, and cotZ. These genes were mapped to 1070 between thiB and metA on the B. subtilis chromosome. The deduced amino acid sequences of the cotY and cotZ genes are very similar. Both proteins are cysteine rich, and CotY antigen was present in spore coat extracts as disulfide cross-linked multimers. There was little CotX antigen in the spore coat soluble fraction, and deletion of this gene resulted in a 30%o reduction in the spore coat insoluble fraction. Spores produced by strains with deletions of the cotX, cotYZ, or cotXYZ genes were heat and lysozyme resistant but readily clumped and responded more rapidly to germinants than did spores from the wild type. In electron micrographs, there was a less densely staining outer coat in spores produced by the cotX null mutant, and those produced by a strain with a deletion of the cotXYZ genes had an incomplete outer coat. These proteins, as part of the coat insoluble fraction, appear to be localized to the outer coat and influence spore hydrophobicity as well as the accessibility of germinants.

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Cited by 54 publications

References 103 publications

Biochemical properties of collagen from ligaments and periarticular tendons of the human knee

Biochemical properties of collagen from ligaments and periarticular tendons of the human knee

Lysine post-translational modifications of collagen

Cloning and characterization of a cluster of genes encoding polypeptides present in the insoluble fraction of the spore coat of Bacillus subtilis

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