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重要 procollagen trafficking, processing and fibrillogenesis
Commentary 1341
Procollagen trafficking, processing and fibrillogenesis
Elizabeth G. Canty and Karl E. Kadler
Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, The University of Manchester, Michael Smith Building, Oxford Road,
Manchester M13 9PT, UK
(e-mail: elizabeth.g.canty@manchester.ac.uk; karl.kadler@manchester.ac.uk)
Journal of Cell Science 118, 1341-1353 Published by The Company of Biologists 2005
doi:10.1242/jcs.01731
Summary
Collagen fibrils in the extracellular matrix allow connective metalloproteinases, and the directional deposition of fibrils
tissues such as tendon, skin and bone to withstand tensile involving the plasma membrane and late secretory
forces. The fibrils are indeterminate in length, insoluble pathway. Fibril-associated molecules are targeted to the
and form elaborate three-dimensional arrays that extend surface of collagen fibrils, and these molecules play an
over numerous cell lengths. Studies of the molecular basis important role in regulating the diameter and interactions
of collagen fibrillogenesis have provided insight into the between the fibrils.
trafficking of procollagen (the precursor of collagen)
through the cellular secretory pathway, the conversion
of procollagen to collagen by the procollagen Key words: Procollagen, Collagen, Fibrillogenesis, ECM
e
c
n Introduction collagen type. To date, 27 different collagen types have been
e
i Collagen fibril
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