PREFERENTIAL LOCALIZATION OF HEAT-SHOCK PROTEIN-47 IN DILATED ENDOPLASMIC-RETICULUM OF CHICKEN CHONDROCYTES

被引:19
作者
KAMBE, K
YAMAMOTO, A
YOSHIMORI, T
HIRAYOSHI, K
OGAWA, R
TASHIRO, Y
机构
[1] KANSAI MED UNIV,DEPT PHYSIOL,MORIGUCHI,OSAKA 570,JAPAN
[2] KANSAI MED UNIV,LIVER RES CTR CELL BIOL,MORIGUCHI,OSAKA,JAPAN
[3] KANSAI MED UNIV,DEPT ORTHOPED SURG,MORIGUCHI,OSAKA,JAPAN
[4] KYOTO UNIV,CHEST DIS RES INST,KYOTO 606,JAPAN
关键词
CHICKEN EPIPHYSEAL CARTILAGE; CHONDROCYTES; HEAT SHOCK PROTEIN 47; PROTEIN A COLLOIDAL GOLD TECHNIQUE; TYPE II COLLAGEN;
D O I
10.1177/42.7.8014466
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
We investigated the distribution of heat shock protein 47 (hsp47) in cultured chicken embryonic chondrocytes and epiphyseal chondrocytes of tibial bones from 1-day-old to Ci-week-old chickens. Northern blot and immunoblot analyses revealed that hsp47 exists in epiphyseal cartilage and cultured chondrocytes. Confocal laser immunofluorescence microscopy showed that hsp47 was localized mainly in the many granular structures found in the cytoplasm that contain Type II collagen. Epiphyseal cartilage and cultured chondrocytes were embedded in LR White resin and hsp47 was detected by protein A-immunogold electron microscopy. Gold particles were localized exclusively in the cisternal space of the endoplasmic reticulum (ER), and the labeling density of the cisternal space of the dilated ER was always higher than that of the non-dilated ER. In all the differentiating zones of epiphyseal cartilage, the labeling density was highest in the hypertrophic cells. These findings suggest that hsp47 plays an important role(s) in the synthesis, processing, and assembly of Type II collagen.
引用
收藏
页码:833 / 841
页数:9
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