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פותח על ידי קלירמאש פתרונות בע"מ -
Expression of chicken 75-kDa gelatinase B-like enzyme in perivascular chondrocytes suggests its role in vascularization of the growth plate
Year:
2003
Authors :
גנין, אולגה
;
.
מונסונגו-אורנן, אפרת
;
.
פינס, מרק
;
.
Volume :
18
Co-Authors:
Tong, A., Institute of Animal Science, Volcani Center, Bet Dagan, Israel
Reich, A., Institute of Animal Science, Volcani Center, Bet Dagan, Israel
Genin, O., Institute of Animal Science, Volcani Center, Bet Dagan, Israel
Pines, M., Institute of Animal Science, Volcani Center, Bet Dagan, Israel
Monsonego-Ornan, E., Institute of Animal Science, Volcani Center, Bet Dagan, Israel, Institute of Animal Science, Volcani Center, Bet Dagan 50250, Israel
Facilitators :
From page:
1443
To page:
1452
(
Total pages:
10
)
Abstract:
A newly cloned avian 75-kDa gelatinase B-Iike enzyme is expressed by the cells surrounding the blood vessels of the growth plate and upregulated by angiogenic substances in cultured chondrocytes. Despite its low homology to mammalian gelatinase-B, the avian 75-kDa seems to function similarly in the context of endochondral bone formation. Introduction: Gelatinase B/metalloproteinase (MMP)-9, a zinc-dependent protease of the MMP family, is a key regulator in the final step of endochondral ossification, Recently an avian 75-kDa gelatinase B-like enzyme that shows low sequence similarity to the mammalian enzyme (59% on the protein level) was cloned and characterized. However, its expression pattern in the chicken growth plate and its role in bone formation have not, so far, been examined. Results: Based on the published sequence, we cloned a 700-bp fragment from cDNA of the chicken growth plate and studied its expression pattern in primary chondrocytes. Because the basal expression level of gelatinase B was almost undetectable, we induced its expression by different culturing conditions, the most dramatic induction achieved by treatment with retinoic acid, which is known as an inducer of vascular invasion in the epiphyseal plates. The gelatinolitic activity, checked by zymography, detected bands corresponding to the gelatinase A and B as well as a new high-molecular weight band of ∼200 kDa. We further studied the expression pattern of gelatinase B by in situ hybridization. The gelatinase B was expressed by the cells surrounding the blood vessels penetrating the growth plate and by chondrocytes located in the front of these vascular invasions in the borders between the bone and the cartilage, resembling the expression of mouse gelatinase B in the growth plate. The induction of rickets by a vitamin D-deficient diet reduced the expression levels of gelatinase B in the growth plate of 12-day-old chickens but did not affect the expression of gelatinase A mRNA. Conclusion: The chicken growth plate has a distinctly different structure from the mammalian one: it is much wider, it contains more cells in each zone, and the blood vessels penetrate deeper into the hypertrophic zone. Nevertheless, the upregulation of the avian 75-kDa gelatinase B-like enzyme by vitamins A and D, coupled with its perivascular expression pattern in the growth plate, implies a similar role for the mammalian and avian genes in bone formation. © 2003 American Society for Bone and Mineral Research.
Note:
Related Files :
angiogenesis
animal tissue
enzyme
epiphysis plate
Growth plate
Matrix metalloproteinase
retinoic acid
unclassified drug
zymography
עוד תגיות
תוכן קשור
More details
DOI :
10.1359/jbmr.2003.18.8.1443
Article number:
0
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
32692
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 01:11
You may also be interested in
Scientific Publication
Expression of chicken 75-kDa gelatinase B-like enzyme in perivascular chondrocytes suggests its role in vascularization of the growth plate
18
Tong, A., Institute of Animal Science, Volcani Center, Bet Dagan, Israel
Reich, A., Institute of Animal Science, Volcani Center, Bet Dagan, Israel
Genin, O., Institute of Animal Science, Volcani Center, Bet Dagan, Israel
Pines, M., Institute of Animal Science, Volcani Center, Bet Dagan, Israel
Monsonego-Ornan, E., Institute of Animal Science, Volcani Center, Bet Dagan, Israel, Institute of Animal Science, Volcani Center, Bet Dagan 50250, Israel
Expression of chicken 75-kDa gelatinase B-like enzyme in perivascular chondrocytes suggests its role in vascularization of the growth plate
A newly cloned avian 75-kDa gelatinase B-Iike enzyme is expressed by the cells surrounding the blood vessels of the growth plate and upregulated by angiogenic substances in cultured chondrocytes. Despite its low homology to mammalian gelatinase-B, the avian 75-kDa seems to function similarly in the context of endochondral bone formation. Introduction: Gelatinase B/metalloproteinase (MMP)-9, a zinc-dependent protease of the MMP family, is a key regulator in the final step of endochondral ossification, Recently an avian 75-kDa gelatinase B-like enzyme that shows low sequence similarity to the mammalian enzyme (59% on the protein level) was cloned and characterized. However, its expression pattern in the chicken growth plate and its role in bone formation have not, so far, been examined. Results: Based on the published sequence, we cloned a 700-bp fragment from cDNA of the chicken growth plate and studied its expression pattern in primary chondrocytes. Because the basal expression level of gelatinase B was almost undetectable, we induced its expression by different culturing conditions, the most dramatic induction achieved by treatment with retinoic acid, which is known as an inducer of vascular invasion in the epiphyseal plates. The gelatinolitic activity, checked by zymography, detected bands corresponding to the gelatinase A and B as well as a new high-molecular weight band of ∼200 kDa. We further studied the expression pattern of gelatinase B by in situ hybridization. The gelatinase B was expressed by the cells surrounding the blood vessels penetrating the growth plate and by chondrocytes located in the front of these vascular invasions in the borders between the bone and the cartilage, resembling the expression of mouse gelatinase B in the growth plate. The induction of rickets by a vitamin D-deficient diet reduced the expression levels of gelatinase B in the growth plate of 12-day-old chickens but did not affect the expression of gelatinase A mRNA. Conclusion: The chicken growth plate has a distinctly different structure from the mammalian one: it is much wider, it contains more cells in each zone, and the blood vessels penetrate deeper into the hypertrophic zone. Nevertheless, the upregulation of the avian 75-kDa gelatinase B-like enzyme by vitamins A and D, coupled with its perivascular expression pattern in the growth plate, implies a similar role for the mammalian and avian genes in bone formation. © 2003 American Society for Bone and Mineral Research.
Scientific Publication
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