title: Different expression of 25-kDa heat-shock protein (Hsp25) in Meckel's cartilage compared with other cartilages in the mouse.
abstract: The 25-kDa heat-shock protein (Hsp25) is expressed in the cartilage of the growth plate and suggested to function in chondrocyte differentiation and degeneration. Using immunohistochemistry, we examined the temporal and spatial occurrence of Hsp25 in Meckel's cartilage in embryonic mice mandibles, and in other types of cartilage in both embryonic and adult mice. In adults, Hsp25 immunoreactivity was detected in the hypertrophic chondrocytes located in growth plates of long bones and in non-osteogenic laryngeal and tracheal cartilages. No chondrocytes in the resting or proliferating phase exhibited Hsp25 immunoreactivity. In the embryonic mandibles, resting and proliferating chondrocytes in the anterior and intermediate portions of Meckel's cartilage showed Hsp25 immunoreactivity from the 12th day of gestation (E12) through E15, whereas those in the posterior portion showed little or no immunoreactivity. After E16, the overall Hsp25 immunoreactivity in Meckel's cartilage substantially reduced in intensity, and little or no immunoreactivity was detected in the hypertrophic chondrocytes located in the degenerating portions of Meckel's cartilage. The antisense oligonucleotide for Hsp25 mRNA applied to the culture media of the mandibular explants from E10 embryos caused significant inhibition of the development of the anterior and middle portions of Meckel's cartilage. These results suggested that Hsp25 is essential for the development of Meckel's cartilage and plays different roles in Meckel's cartilage from those in the permanent cartilages and the cartilages undergoing endochondral ossification.
authors.affiliation: Department of Histology and Embryology, Kanazawa University Graduate School of Medical Science, 920-8640, Kanazawa, Japan. m.shimada@oral.m.kanazawa-u.ac.jp
authors.forename: Mayumi
authors.initials: M
authors.lastname: Shimada
authors.forename: Miyuki
authors.initials: M
authors.lastname: Yamamoto
authors.forename: Tomohiko
authors.initials: T
authors.lastname: Wakayama
authors.forename: Shoichi
authors.initials: S
authors.lastname: Iseki
authors.forename: Osamu
authors.initials: O
authors.lastname: Amano
mesh_terms: D000818:Animals; D000831:Animals, Newborn; D001934:Branchial Region / Q000166:cytology / Q000196:embryology* / Q000378:metabolism*; D002356:Cartilage / Q000166:cytology / Q000196:embryology* / Q000378:metabolism*; D002454:Cell Differentiation / Q000502:physiology; D002455:Cell Division / Q000502:physiology; D019902:Chondrocytes / Q000166:cytology / Q000378:metabolism; D005260:Female; D005333:Fetus; D005786:Gene Expression Regulation / Q000502:physiology; D006132:Growth Plate / Q000166:cytology / Q000196:embryology / Q000378:metabolism; D006360:Heat-Shock Proteins; D008334:Mandible / Q000166:cytology / Q000196:embryology* / Q000378:metabolism*; D051379:Mice; D018832:Molecular Chaperones; D009363:Neoplasm Proteins / Q000235:genetics / Q000378:metabolism*; D016376:Oligonucleotides, Antisense; D010012:Osteogenesis / Q000502:physiology; D012333:RNA, Messenger / Q000037:antagonists & inhibitors / Q000378:metabolism; D013957:Thyroid Cartilage / Q000166:cytology / Q000196:embryology / Q000378:metabolism; D014132:Trachea / Q000166:cytology / Q000196:embryology / Q000378:metabolism
chemical_list: D006360:Heat-Shock Proteins; C486113:Hsbp1 protein, mouse; D018832:Molecular Chaperones; D009363:Neoplasm Proteins; D016376:Oligonucleotides, Antisense; D012333:RNA, Messenger