Collagen type XI alpha1 may be involved in the structural plasticity of the vertebral column in Atlantic salmon (Salmo salar L.).
Atlantic salmon (Salmo salar L.) vertebral bone displays plasticity in structure, osteoid secretion and mineralization in response to photoperiod. Other properties of the vertebral bone, such as mineral content and mechanical strength, are also associated with common malformations in farmed Atlantic salmon. The biological mechanisms that underlie these changes in bone physiology are unknown, and in order to elucidate which factors might be involved in this process, microarray assays were performed on vertebral bone of Atlantic salmon reared under natural or continuous light. Eight genes were upregulated in response to continuous light treatment, whereas only one of them was upregulated in a duplicate experiment. The transcriptionally regulated gene was predicted to code for collagen type XI alpha1, a protein known to be involved in controlling the diameter of fibrillar collagens in mammals. Furthermore, the gene was highly expressed in the vertebrae, where spatial expression was found in trabecular and compact bone osteoblasts and in the chordoblasts of the notochordal sheath. When we measured the expression level of the gene in the tissue compartments of the vertebrae, the collagen turned out to be 150 and 25 times more highly expressed in the notochord and compact bone respectively, relative to the expression in the trabecular bone. Gene expression was induced in response to continuous light, and reduced in compressed vertebrae. The downregulation in compressed vertebrae was due to reduced expression in the compact bone, while expression in the trabecular bone and the notochord was unaffected. These data support the hypothesis that this gene codes for a presumptive collagen type XI alpha1, which may be involved in the regulatory pathway leading to structural adaptation of the vertebral architecture.
Institute of Marine Research, PO Box 1870 Nordnes, Bergen, NO-5817, Norway. anna.wargelius@imr.no
A
A
Wargelius
P G
PG
Fjelldal
U
U
Nordgarden
A
A
Grini
C
C
Krossøy
S
S
Grotmol
G K
GK
Totland
T
T
Hansen
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D001842:Bone and Bones / Q000378:metabolism / Q000528:radiation effects; D003001:Cloning, Molecular; D024161:Collagen Type XI / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020869:Gene Expression Profiling; D005786:Gene Expression Regulation / Q000528:radiation effects; D008027:Light; D008969:Molecular Sequence Data; D009672:Notochord / Q000378:metabolism / Q000528:radiation effects; D020411:Oligonucleotide Array Sequence Analysis; D009928:Organ Specificity / Q000235:genetics / Q000528:radiation effects; D010802:Phylogeny; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011859:Radiography; D020317:Salmo salar / Q000235:genetics / Q000378:metabolism*; D017422:Sequence Analysis, DNA; D013131:Spine / Q000033:anatomy & histology* / Q000166:cytology / Q000000981:diagnostic imaging / Q000378:metabolism*
D024161:Collagen Type XI; D020033:Protein Isoforms