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The University
of Prince Edward Island
Atlantic Veterinary College
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Glenda M. Wright, BSc, PhD
Professor
Cell and Developmental Biology
Research Activities
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Lampreys
and hagfishes are living representatives of a group of jawless
fishes, which were common 500 million years ago. As the most ancient
vertebrates alive today and are important in studies of molecular evolution
and in investigations to determine vertebrate features which are primitive
and those that have arisen subsequent to the origin of the vertebrates.
Non-collagenous cartilages: their matrix proteins, development,
physical properties and phylogeny
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The
skeleton of the hagfishes and lampreys is cartilaginous. Collagen is the
major structural protein of most cartilages in the jawed vertebrates.
Our lab has shown that the cartilages of hagfishes and lampreys lack collagen
and therefore may be termed non-collagenous cartilages. The
annular (mouth), piston (tongue) and trabecular (neurocranial) cartilages
of the sea lamprey (Petromyzon marinus) are composed primarily of
a previously unrecognized but major structural protein of unique composition
which we termed lamprin. Myxinin is an unusual structural protein of unique
composition constituting the major structural protein of the lingual
cartilage in the Atlantic hagfish (Myxine glutinosa).
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Lamprin
has been cloned, sequenced and partially characterized (1) and the
spatial and temporal distribution of lamprin transcripts during chondrogenesis
of the trabecular cartilage in embryonic lamprey has been determined
(2). We have defined the ultrastructural features of chondrogenesis of
lamprin-based trabecular cartilage in lamprey embryos (3) and
shown evidence identifying two different non-collagenous cartilages in
lamprey designated as cranial (those composed of lamprin) and branchial
(4). Both lamprin and branchial cartilage matrix protein share similarities
with vertebrate elastins (5).
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At least two types of non-collagenous
cartilages have been identified in hagfish, designated as hard and soft,
each with a distinct matrix protein (6). Myxinin is found in hard
cartilages.
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Preliminary investigations
of the endoskeletal elements of the gills in the horseshoe crab indicate
that this cartilaginous tissue contains a non-collagenous, fibrillar matrix
protein which could be a related protein (7).
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The structure and organization
of the lamprin genes have been determined (8) and we have defined the morphological
aspects of branchial cartilage chondrogenesis during lamprey embryogenesis
(9). Recently we have expanded our understanding of lamprey development
through the analysis of key external and internal developmental events
in sea lamprey embryos of different chronological ages (10).
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The physical properties of lamprey
cartilages are being studied in collaboration with Dr.
M.E. DeMont (Department of Biology, St. Francis Xavier University).
We have compared the equilibrium stress-relaxation behaviour of lamprey
and bovine cartilages and found that despite mechanical and functional
differences, lamprey cranial and branchial cartilages demonstrate equilibrium
stiffnesses and relaxation properties similar to those of mammalian cartilages
(11).
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Using morphological, biochemical,
molecular and biomechanical approaches we continue to investigate the matrix
proteins of lamprey, hagfish and horseshoe crab cartilages, the molecules
involved in regulating cartilage development in embryonic lamprey,
and measure the physical properties of the non-collagenous cartilages.
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This research is supported
by NSERC.
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Graduate student
positions are available.
Publications
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1. Robson, P., G.M. Wright, E. Sitarz, A. Maiti, M. Rawat, J.H.
Youson, F.W. Keeley. 1993. Characterization of lamprin, an unusual matrix
protein from lamprey cartilage. J. Biol. Chem., 268:1440-1447.
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2. McBurney, K.M., F.W. Keeley, F.S.B. Kibenge, G.M. Wright. 1996.
Spatial and temporal distribution of lamprin mRNA during chondrogenesis
of trabecular cartilage in the sea lamprey. Anat. Embryol., 193:419-426.
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3. McBurney, K.M., G.M. Wright. 1996. Chondrogenesis of a non-collagen-based
cartilage in the sea lamprey, Petromyzon marinus. Can. J. Zool.,
74: 2118-2130.
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4. Robson, P., G.M. Wright, J.H. Youson, F.W. Keeley. 1997. Non
collagen-based cartilages in the skeleton of the sea lamprey, Petromyzon
marinus. Comp. Biochem. Physiol., 118B: 71-78.
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5. Wright, G.M., F.W. Keeley, P. Robson. 2001. The unusual
cartilaginous tissues of jawless craniates, cephalochordates and invertebrates.
Cell Tissue Res., 304:165-174.
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6. Robson, P., G.M. Wright, F.W. Keeley. 2000. Distinct
non-collagen based cartilages comprising the endoskeleton of the Atlantic
hagfish, Myxine glutinosa. Anat. Embryol., 202:281-290.
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7. Robson, P., G.M. Wright, J.H. Youson, F.W. Keeley. 2000.
The structure and organization of lamprin genes: Multiple-copy genes
with alternative splicing and convergent evolution with insect structural
proteins. Mol. Biol. Evol., 17:1739-1752.
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8. Morrison, S.L., C.K. Campbell, G.M. Wright. 2000.
Chondrogenesis of the branchial skeleton in embryonic sea lamprey,
Petromyzon
marinus. Anat. Rec., 260:252-267.
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9. Richardson, M.K., G.M. Wright. 2003. Developmental transformations
in a normal series of embryos of the sea lamprey Petromyzon marinus
(Linneaus). J. Morphol., 257:348-363.
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10. Courtland, H.W., G.M. Wright, R.G. Root, M.E. DeMont.
2003. Comparative equilibrium mechanical properties of bovine and
lamprey cartilaginous tissues. J. Exp. Biol., 206:1397-1408.
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And Now For Something Completely Different
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of Biomedical Sciences
For more information contact:
Dr. Glenda Wright
550 University Avenue
Charlottetown, P.E.Island
C1A 4P3
phone: (902)566-0805
fax: (902)566-0832
Last updated February 2005
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