Abstract
The activities of some glycosaminoglycan-degrading enzymes in uterine leiomyomas.
Both normal human myometrium and uterine leiomyoma contain several glycosaminoglycans
(GAGs). In contrast to many normal and tumour tissues the amount of hyaluronic acid
(HA) is very low and the proportional amount of sulphated glycosaminoglycans is distinctly
higher. We compared the activity of GAG-degrading enzymes in normal myometrium and
in uterine leiomyomas. Growth of uterine leiomyomas results in significant reduction
in the activities of neutral endoglycosidases degrading most of the sulphated glycosaminoglycans.
The activities of acid endoglycosidases also decreased (with the exception of chondroitin-6-sulphate).
Thus, the differentiated activity of glycosidases degrading glycosaminoglycans can
be a factor modifying the quantity of GAGs.
Keywords
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References
- Matrix proteoglycans: from molecular design to cellular function.Annu. Rev. Biochem. 1998; 67: 609-652
- Glycosaminoglycans: molecular properties, protein interaction, and role in physiological processes.Physiol. Rev. 1991; 71: 481-525
- Extracellular matrix components in uterine leiomyoma and their alteration during the tumour growth.Mol. Cell Biochem. 1998; 189: 145-152
- Glikozoaminoglikany w miGin. Pol. 1998; 69: 12-16
śniakach macicy.
Fosang AJ, Hardingham TE. Matrix proteoglycans. In: Comper WD, editor. Extracellular matrix, vol. 2. Amsterdam: Harwood Academic Publishers; 1996. p. 200–29.
- Proteoglycans: many forms, many functions.FASEB J. 1992; 6: 861-870
- The activities of some glycosaminoglycan-degrading enzymes in the wall of the umbilical cord artery and their alteration in edema, proteinuria, hypertension (EPH)-gestosis.Clin. Chem. Lab. Med. 1999; 37: 417-421
- Activities of some glycosaminoglycan-degrading enzymes in Wharton’s jelly and their alteration in EPH-gestosis (preeclampsia).Biol. Neonate. 1999; 76: 144-152
- Glycosaminoglycan-degrading enzymes in the skin of fasted rats.Comp. Biochem. Physiol. B. 2002; 131: 551-557
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Anal. Biochem. 1976; 72: 248-254
- Structure and biological activity of the extracellular matrix.J. Mol. Med. 1998; 76: 253-265
- Supramolecular organisation of extracellular matrix glycosaminoglycans in vitro and in the tissues.FASEB J. 1992; 6: 2639-2645
- Alterations in glycosaminoglycan composition of methylcholanthrene-induced sarcoma at various stages of the tumor growth.Folia Histochem. Cytobiol. 1996; 34: 21-26
- Proteoglycans: structure and interactions.Annu. Rev. Biochem. 1991; 60: 443-475
- Proteoglycans in health and disease: structures and functions.Biochem. J. 1986; 236: 1-14
- Effect of glycosaminoglycans on the growth of cultured tumor cells.J. Osaka Dent. Univ. 1993; 27: 121-133
- Enzymatic degradation of glycosaminoglycans.Crit. Rev. Biochem. Mol. Biol. 1995; 30: 387-444
- Glycosaminoglycan degradation.Adv. Enzymol. Relat. Areas Mol. Biol. 1987; 60: 217-311
Gallagher JT. Heparan sulphate proteoglycans. The control of cell growth. In: Comper WD, editor. Extracellular matrix, vol. 2. Amsterdam: Harwood Academic Publishers; 1996. p. 230–45.
- Matrix proteoglycans: from molecular design to cellular function.Annu. Rev. Biochem. 1998; 67: 609-652
Article info
Publication history
Accepted:
October 18,
2002
Received in revised form:
October 10,
2002
Received:
February 28,
2002
Identification
Copyright
© 2003 Elsevier Science Ireland Ltd. Published by Elsevier Inc. All rights reserved.