Expression of genes encoding the collagen-binding heat shock protein (Hsp47) and type II collagen in developing zebrafish embryos.
Hsp47 is a heat-shock protein which interacts with newly synthesize procollagen chains in the endoplasmic reticulum (ER) of collagen-secreting cells and is thought to assist in procollagen triple helix assembly and subsequent transport to the cis-Golgi. This is supported by studies which have reported that genes encoding collagen and Hsp47 are subject to co-ordinate increases and decreases in expression in cultured cells. However, limited information is available regarding hsp47 expression in vivo, particularly during early embryonic development when a variety of collagen genes are expressed. Here we show that the zebrafish hsp47 gene is expressed in a dynamic spatiotemporal pattern in developing embryos. Strong expression of hsp47 mRNA is co-incident predominantly with expression of the type II collagen gene (col2a1) in a number of chondrogenic and non-chondrogenic tissues including the notochord, otic vesicle and developing fins. Notochordal expression of both genes is disrupted in floating head ( flh) and no tail (ntl) embryos, which lack properly differentiated notochords. Surprisingly, no hsp47 mRNA is detectable in the strongly col2a1-expressing cells of the floor plate and hypochord, indicating that the two genes are not strictly co-regulated. Finally, Northern blot analysis revealed two alternative transcripts of col2a1 which are expressed in distinct temporal patterns. Appearance of the larger transcript occurs following somitogenesis, a time which coincides with the co-activation of hsp47 and col2a1 gene expression in tissues outside of the notochord.[1]References
- Expression of genes encoding the collagen-binding heat shock protein (Hsp47) and type II collagen in developing zebrafish embryos. Lele, Z., Krone, P.H. Mech. Dev. (1997) [Pubmed]
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