Barbara M. Vertel

TL;DR: Heterogeneity of keratan sulfate synthesis at the level of individual chondrocytes, even for cells apparently containing equivalent amounts of intracellular chondroitin sulfate proteoglycan, is suggested.

TL;DR: The intracellular compartments of chondrocytes involved in the synthesis and processing of type II procollagen and chondroitin sulfate proteoglycan (CSPG) monomer were investigated using simultaneous double immunofluorescence and lectin localization reactions and the perinuclear cytoplasm seems to correspond to the Golgi complex.

TL;DR: It is concluded that the vesicles accumulate CSPG precursors which have not been modified by Golgi-mediated processes, and the data indicate that matrix molecules may be segregated selectively prior to transit through the Golgi complex.

TL;DR: Early steps in the biosynthesis of chondroitin sulfate proteoglycan and collagenous cartilage matrix molecules were examined by the comparison of products translated in mRNA-directed cell-free reactions and those synthesized by intact cartilage cells, suggesting that the observed time-dependent increases in Mr are a consequence of collagen hydroxylation.