A comparative analysis of structure and spatial distribution of decorin in human leiomyoma and normal myometrium
Autor: | Yara M. Michelacci, Alessandra G. A. Berto, Celia R.C Franco, Lucia O. Sampaio, Roberto M. Cesar |
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Rok vydání: | 2003 |
Předmět: |
Adult
medicine.medical_specialty Glycosylation Protein Conformation Decorin Molecular Sequence Data Biophysics Biochemistry Extracellular matrix Type IV collagen Internal medicine medicine Humans Amino Acid Sequence Molecular Biology Electrophoresis Agar Gel Extracellular Matrix Proteins Leiomyoma Sequence Homology Amino Acid biology Chemistry Myometrium Middle Aged Chromatography Ion Exchange musculoskeletal system medicine.disease female genital diseases and pregnancy complications Cell biology carbohydrates (lipids) Endocrinology Microscopy Fluorescence Proteoglycan Uterine Neoplasms Chromatography Gel biology.protein Female Proteoglycans Type I collagen Extracellular matrix organization |
Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 1619:98-112 |
ISSN: | 0304-4165 |
Popis: | Leiomyoma is a benign smooth muscle tumor of the uterus that affects many women in active reproductive life. It is composed by bundles of smooth muscle cells surrounded by extracellular matrix. We have recently shown that the glycosylation of extracellular matrix proteoglycans is modified in leiomyoma: increased amounts of galactosaminoglycans with structural modifications are present. The data here presented show that decorin is present in both normal myometrium and leiomyoma but tumoral decorin is glycosylated with longer galactosaminoglycan side chains. Furthermore, these chains contain a higher ratio D-glucuronate/L-iduronate, as compared to normal tissue. To determine if these changes in proteoglycan glycosylation correlates with modifications in the extracellular matrix organization, we compared the general structural architecture of leiomyoma to normal myometrium. By histochemical and immunofluorescence methods, we found a reorganization of muscle fibers and extracellular matrix, with changes in the distribution of glycoproteins, proteoglycans, and collagen. Thin reticular fibers, possibly composed by types I and III collagen, were replaced by thick fibers, possibly richer in type I collagen. Type I collagen colocalized with decorin both in leiomyoma and normal myometrium, in contrast to type IV collagen that did not. The relative amount of decorin was increased and the distribution of decorin and collagen was totally modified in the tumor, as compared to the normal myometrium. These findings reveal that not only decorin structure is modified in leiomyoma but also the tissue architecture changed, especially concerning extracellular matrix. |
Databáze: | OpenAIRE |
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