The Distribution of Unsulphated and Sulphated Glycosaminoglycans in Palmar Fascia from Patients with Dupuytren’s Disease and Healthy Subjects

Abstract

Eighty specimens from 20 patients with Dupuytren's disease and 7 biopsies of healthy palmar fascia were analysed for their glycosaminoglycan isomer patterns with a combined enzymatic/HPLC method. The diseased portions of palmar fascia tissue were characterized by elevated total glycosaminoglycans together with a relative increase in the sulphated fractions. The macroscopic stages of nodules, bands and unaffected tissue could be classified very well by multivariate statistical analysis on the basis of their glycosaminoglycan patterns. The biochemical analysis provided evidence of the pathological process even in those specimens that did not yet show any clinical symptoms of the disease.Because of the role played by sulphated glycosamiThe mechanisms involved in the pathogenesis of Du-noglycans in the interaction with collagen (12), the puytren's disease are still unknown (1). Recent studies question arises of whether there are changes in the on the morphological changes in diseased tissue have proportions of glycosaminoglycans and their unsuldemonstfated occlusioii of capillaries by cells that phated and sulphated isomers in affected palmar fasmigrate into the perivascular space. These cells are cia that may have an influence on the collagen pattern thought to be the origin of dedifferentiated cells that and the macromolecular structure. The present study proliferate and metabolize in such Way that they cause was conducted to determine the types and amounts contracture of the aponeurosis (2, 3). As to the pa-of the various sulphated and unsulphated glycosathobiochemistry, an increase in collagen type III pro-minoglycans and to reassess the data published so far tein has been reported (4-7), as has an increase in on the glycosaminoglycan content of both healthy the proportion of chondroitin sulphate (4, 8 -11). human palmar fascia and tissue from Dupuytren'ŝ contracture, by employing a method of determination ') With support of the Deutsche Forschungsgemeinschaft (SFB more specific than any used previously. The new 54). method also enabled differentiation of the unsul-2 ) Present address: Institute for Clinical Chemistry and Labo-, , ~A . . -, n< e "i«i^t-/i ^mnr^ntc ratory Medicine, university Hospital "BergmannsheiT Bo-P hated > C4-sulphated and C6-sulphated components chum, FRG (11).

Alterations in the Extracellular Matrix Proteoglycan Profile in Dupuytren's Contracture Affect the Palmar Fascia

“…Connected with Dupuytren's contracture, the alterations in matrix PGs lead to an accumulation of DS and CS in diseased tissue. This latter phenomenon has been reported by others (33,34). It is worthy of note that similar remodeling of the matrix PG (and matrix GAG) profile has been observed in the case of hypertrophic skin scars (35) and scarred fascia lata (15), demonstrating the existence of common mechanisms involved in some types of wound healing and Dupuytren's disease.…”

Dermatan sulfate remodeling associated with advanced Dupuytren's contracture.

“…tion II DS in relation to fraction I GAG found in DF as compared to normal tissue. Moreover, our suggestion concerning the oversulfation of DF derived DS is confirmed by the results of Tunn et al (1988), who found increased content of sulfated disaccharides generated by chondroitinase ABC action on the GAG from such tissue samples. The profound remodeling of DS profile also involving an increase in this GAG content, observed by us in advanced DC, may be due to two reasons: (i) alterations in expression of particular DSPGs manifested most probably by enhanced biosynthesis of small leucine rich PG biglycan (Koźma et al, 2005) as well as (ii) changes in activity of GAG modifying enzymes.…”

“…On the other hand, as it has been revealed in in vitro studies, these molecules influence glycosaminoglycan metabolism also affecting DS structure (Kinsella et al, 2004;Tiedemann et al, 2005). Indeed, an accumulation of DS and chondroitin sulfate (CS) is observed in Dupuytren's fascia (Flint et al, 1982;Tunn et al, 1988). However, the detailed aspects of disease-associated metabolism of DS as the major GAG both of normal and Dupuytren's fascia ECM (Flint et al, 1982) is poorly known.…”

Comparison of palmar aponeuroses from individuals with diabetes Mellitus and Dupuytren's contracture

“…The increase in collagen denaturation temperature observed in palmar aponeuroses from patients with NIDDM is the consequence of increased cross-linking due to NEG. On the other hand, in DC several biochemical changes have been described: (1) increase in the relative proportion of type III collagen (Bailey et al, 1977), (2) increased proteoglycan content relative to collagen (Tunn et al, 1988), (3) a lysyl-overmodification of collagen type I (Bailey et al, 1977), and (4) fewer cross-links than found in normal palmar aponeuroses (Bailey, 1994). Of these changes, the third and the fourth explain the reduction in collagen denaturation temperature which was already described by Nemetschek et al (1976).…”