Partial cloning and sequencing of chick fibrillin-1 cDNA

被引:0
作者
Guimei Zhou
Christopher E. Price
Thomas H. Rosenquist
Preston E. Gadson
Maurice Godfrey
机构
[1] University of Nebraska Medical Center,Munroe Center for Human Genetics
[2] University of Nebraska Medical Center,Department of Cell Biology and Anatomy
[3] University of Nebraska Medical Center,Department of Pediatrics
[4] University of Nebraska Medical Center,985430 Nebraska Medical Center
关键词
fibrillin; chick; development; in situ hybridization; extracellular matrix;
D O I
10.1290/1071-2690(2000)036<0019:PCASOC>2.0.CO;2
中图分类号
学科分类号
摘要
The recent identification of numerous matrix genes and gene products has allowed a detailed examination of their roles in development. Two of these extracellular matrix proteins, fibrillin-1 and fibrillin-2, are components of the elastin-associated microfibrils. Given what is known about the distribution of the fibrillins in normal tissues and the abnormalities that result when mutations occur, a basic hypothesis has emerged: fibrillin-1 is primarily responsible for load bearing and providing structural integrity, whereas fibrillin-2 may be a director of elastogenesis. Nevertheless, examination of phenotypes in disorders caused by mutations in fibrillin-1 or fibrillin-2 suggests some common functions. To better understand these similar and diverse roles, it would be helpful to examine these proteins during chick development. To accomplish this goal, it is first necessary to characterize the chick homologs of the known fibrillins. In this study, the partial chick FBN1 cDNA was identified by polymerase chain reaction-aided cloning as a first step toward elucidating these goals. Sequence analysis indicated that there is striking conservation between chick and mammalian fibrillin-1 at the DNA and protein levels. Antisense and sense riboprobes were synthesized and used in in situ hybridization in stage 14 chick embryos and high levels of FBN1 transcripts were observed in the heart.
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页码:19 / 25
页数:6
相关论文
共 95 条
[1]  
Andaloro V. J.(1998)Dextromethorphan and other N-methyl- Pediatr. Res. 43 1-7
[2]  
Monaghan D. T.(1996)-aspartate receptor antagonists are teratogenic in the avian embryo model Int. J. Biochem. Cell Biol. 28 531-542
[3]  
Rosenquist T. H.(1993)Analysis of the human gene encoding latent transforming growth factor-beta-binding protein-2 J. Cell Biol. 121 201-212
[4]  
Bashir M. M.(1983)Emilin, a component of elastic fibers preferentially located at the elastin-microfibrils interface Int. Rev. Conn. Tissue Res. 10 97-209
[5]  
Han M. D.(1995)Elastin-associated microfibrils and microfibrillar proteins Human Mol. Genet. 4 1799-1809
[6]  
Abrams W. R.(1989)Mutations in the human gene for fibrillin-1 (FBN1) in the Marfan syndrome and related disorders FEBS Lett. 251 1-7
[7]  
Bressan G. M.(1997)EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation? Exp. Cell Res. 230 169-180
[8]  
Daga Gordini D.(1993)Differential response of mesoderm- and neural crest-derived smooth muscle to TGF-beta 1: regulation of c-myb and alpha 1 (I) procollagen genes Dev. Dyn. 196 70-78
[9]  
Colombatti A.(1995)Fibrillin delineates the primary axis of the early avian embryo Mol. Cell. Biol. 15 6932-6942
[10]  
Cleary E. G.(1991)Bovine latent transforming growth factor beta 1-binding protein 2: molecular cloning, identification of tissue isoforms, and immunolocalization to elastin-associated microfibrils J. Biol. Chem. 266 7596-7601