Human osteoarthritic knee cartilage: fingerprinting of adhesion/growth-regulatory galectins in vitro and in situ indicates differential upregulation in severe degeneration

被引：62

作者：

Toegel, Stefan ^{[1
]}

Bieder, Daniela ^{[1
]}

Andre, Sabine ^{[2
]}

Kayser, Klaus ^{[3
]}

Walzer, Sonja M. ^{[1
]}

Hobusch, Gerhard ^{[1
]}

Windhager, Reinhard ^{[1
]}

Gabius, Hans-Joachim ^{[2
]}

机构：

[1] Med Univ Vienna, Dept Orthopaed, Karl Chiari Lab Orthopaed Biol, Vienna, Austria

[2] Univ Munich, Inst Physiol Chem, Fac Vet Med, D-80539 Munich, Germany

[3] Charite, Inst Pathol, Berlin, Germany

来源：

HISTOCHEMISTRY AND CELL BIOLOGY | 2014年 / 142卷 / 04期

关键词：

Glycosylation; Lectin; Mankin score; Osteoarthritis; Sialylation; POLYPORUS-SQUAMOSUS LECTIN; ARTICULAR-CARTILAGE; DOWN-REGULATION; COLON-CANCER; N-GLYCANS; BINDING; EXPRESSION; LOCALIZATION; CHONDROCYTES; RECOGNITION;

D O I：

10.1007/s00418-014-1234-x

中图分类号：

Q2 [细胞生物学];

学科分类号：

071013 [干细胞生物学];

摘要：

The apparent connection of galectin-3 to chondrocyte survival and osteoarthritis-like cartilage modifications in animal models provided incentive for the mapping of seven members of this family of adhesion/growth-regulatory proteins in human cartilage specimens. Starting with work in vitro, RT-qPCR analyses and immunocytochemistry revealed gene transcription and protein presence in cultured OA chondrocytes, especially for galectin-1, galectin-3 and galectin-8. Immunohistochemistry in clinical specimens with mild and severe cartilage degeneration detected galectins in chondrocytes-with upregulation, especially of galectin-1 in areas of severe degeneration-accompanied by alpha 2,6-sialylation in the pericellular matrix. Given the possibility for additive/antagonistic activities between galectins, these results direct further research toward examining cellular effects of (1) these proteins (alone or in combination) on chondrocytes and (2) remodeling of the chondrocyte glycophenotype.

引用

页码：373 / 388

页数：16

共 57 条

[1]

Tumour suppressor p16INK4a-anoikis-favouring decrease in N/O-glycan/cell surface sialylation by down-regulation of enzymes in sialic acid biosynthesis in tandem in a pancreatic carcinoma model [J].