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

Abstract

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)

Biochemical Study of Collagen and Its Crosslinks in the Anterior Cruciate Ligament and the Tissues Used as a Graft for Reconstruction of the Anterior Cruciate Ligament

“…Two previous reports have addressed the crosslinks of collagen of the tendons and ligaments [13,14]. Eyre et al [13] reported on the concentrations of crosslinks in various mammalian (human, bovine, rat, rabbit) and avian (chicken) connective tissues.…”

“…Only 1 tendon sample, a patellar tendon, was examined in that study [13]. Fujii et al [14] reported on the biochemical properties of ligaments and periarticular tendons (ACL, posterior cruciate ligament, medial collateral ligament, lateral collateral ligament, PT, ST, gracilis, and iliotibial band) of the human knee. In their study, the samples were collected from 5 fresh cadavers [14].…”

“…Previous reports showed that the extracellular matrix of the ligaments and tendons were collagen rich, and that the amounts of crosslinks of collagen were different in each tissue [13,14]. There are many kinds of crosslinks of collagen that play a role physiologically in the connective tissues [8][9][10][11][12].…”

Collagen cross-links as a determinant of bone quality: a possible explanation for bone fragility in aging, osteoporosis, and diabetes mellitus

“…1). Tissue-specific composition of enzymatic cross-links in bone [14][15][16][17][18], tendon [14,[19][20][21], ligament [17,19,21,22], and skin [14,18,23] depends on the degree of telopeptide Lys hydroxylation, although type I collagen in all tissues is genetically identical. Thus, Hyl aldehyde-derived cross-links, that is dehydro-dihydroxylysinonorleucine (deH-DHLNL), dehydro-hydroxylysinonorleucine (deH-HLNL), and their mature forms, pyridinium and pyrrole cross-links, are the predominant type of cross-link in bone.…”

Single-Column High-Performance Liquid Chromatographic–Fluorescence Detection of Immature, Mature, and Senescent Cross-Links of Collagen

“…One of the trivalent mature cross-links, HHL, is analyzed by amino acid analysis Cross-links of collagen play an important role in the on ion-exchange column after a preliminary fractionexpression of physiological functions of collagen fibers ation step (18, 22), whereas Pyr, Dpyr, and Pen are and are significant factors in various kinds of connecanalyzed by a reverse-phase HPLC simultaneously detive tissue abnormalities in disease and age-dependent changes (1)(2)(3)(4). The borohydride-reducible lysyl oxidase-mediated cross-links of collagen, which form the tected by natural fluorescence (23,24).…”