Myllyharju J, Kivirikko KI, et al.
Annals of medicine. Date of publication 2001 Feb 1;volume 33(1):7-21.
1. Ann Med. 2001 Feb;33(1):7-21.
Collagens and collagen-related diseases.
Myllyharju J(1), Kivirikko KI.
Author information:
(1)Biocenter and Department of Medical Biochemistry, University of Oulu, Finland.
The collagen superfamily of proteins plays a dominant role in maintaining the
integrity of various tissues and also has a number of other important functions.
The superfamily now includes more than 20 collagen types with altogether at least
38 distinct polypeptide chains, and more than 15 additional proteins that have
collagen-like domains. Most collagens form polymeric assemblies, such as fibrils,
networks and filaments, and the superfamily can be divided into several families
based on these assemblies and other features. All collagens also contain
noncollagenous domains, and many of these have important functions that are
distinct from those of the collagen domains. Major interest has been focused on
endostatin, a fragment released from type XVIII collagen, which potently inhibits
angiogenesis and tumour growth. Collagen synthesis requires eight specific
post-translational enzymes, some of which are attractive targets for the
development of drugs to inhibit collagen accumulation in fibrotic diseases. The
critical roles of collagens have been clearly illustrated by the wide spectrum of
diseases caused by the more than 1,000 mutations that have thus far been
identified in 22 genes for 12 out of the more than 20 collagen types. These
diseases include osteogenesis imperfecta, many chondrodysplasias, several
subtypes of the Ehlers-Danlos syndrome, Alport syndrome, Bethlem myopathy,
certain subtypes of epidermolysis bullosa, Knobloch syndrome and also some cases
of osteoporosis, arterial aneurysms, osteoarthrosis, and intervertebral disc
disease. The characterization of mutations in additional collagen genes will
probably add further diseases to this list. Mice with genetically engineered
collagen mutations have proved valuable for defining the functions of various
collagens and for studying many aspects of the related diseases.
DOI: 10.3109/07853890109002055
PMID: 11310942 [Indexed for MEDLINE]
