Synthesis and secretion of collagen by cells of connective tissue, bone, and dentin.

The production of type I collagen by fibroblasts, odontoblasts, and osteoblasts is reviewed on the basis of results obtained by electron microscopy, 3H-proline radioautography, and immunostaining for type I procollagen. In the three cell types, the precursors of type I collagen are processed along the rough endoplasmic reticulum (rER)-Golgi-secretory granule pathway in the same manner as secretory proteins, but the available evidence suggests a few special features: 1) From the rER site of synthesis, the initial collagen precursors, known as pro-alpha chains, are transported to the Golgi apparatus within tubular structures, referred to as intermediate tubules, rather than within vesicles. 2) The pro-alpha chains coil into a triple helix within spherical distensions present along the saccules on the cis side of Golgi stacks. 3) The resulting procollagens are fairly rigid and form bundles that cause spherical distensions to lengthen into cylindrical ones, whereas by an unknown mechanism these distensions become part of the saccules on the trans-side of Golgi stacks. 4) The procollagen-containing cylindrical distensions are released from trans-saccules to become secretory granules, and some procollagen material finds its way into lysosomes. 5) The secretory granules release their procollagen content by exocytosis at the cell surface. 6) The released procollagen is transformed into collagen before or, more probably, after associating with the surface of a collagen fibril.