Visualization of sulfur-containing components associated with proliferating chondrocytes from rat epiphyseal growth plate cartilage: Possible proteoglycan and collagen co-migration

Journal Article · Thu Feb 01 04:00:00 EST 1990 · Anatomical Record; (USA)

DOI:https://doi.org/10.1002/ar.1092260205· OSTI ID:7191972

Landis, W J; Hodgens, K J ^[1]

---

1. Harvard Medical School, Boston, MA (USA)

Electron microscopy of epiphyseal growth plate cartilage from normal 4-5-week-old rats has revealed extensive fibrillar aggregates and globules in the pericellular spaces of proliferating chondrocytes. These cells contained small globules and diffusely coiled, fine filaments located within large, membrane-invested vacuoles. All such structures were observed after a variety of different tissue fixation regimes, including glutaraldehyde, osmium tetroxide, and potassium pyroantimonate. The fibrillar aggregates and globules were often overlapping and intermeshed and extended to 0.5 micron in length from their point of origin at cell membranes. Vacuoles were usually found at the periphery of cells, and some, by membrane fusion with the cell envelope, appeared contiguous with extracellular spaces wherein their contents could be discharged. Fine filaments and globules were occasionally observed in the Golgi complex and cisternae of endoplasmic reticulum of the chondrocytes. Further characterization of the cellular and pericellular components by electron microscopic radioautography, electron probe microanalysis, and electron spectroscopic imaging indicated the presence of sulfur, a result suggesting these aggregates, filaments, and globules in part represent proteoglycans in various stages of synthesis, secretion, and assembly. Additional radioautography utilizing 3H-proline implied that filament bundles are also composed of collagen, a result posing the possibility that this protein and the putative proteoglycans may co-migrate both intracellularly and within pericellular matrices. In extracellular matrices adjacent to cell lacunae, the fibrillar aggregates appeared in close association with typical collagen type II fibrils, an observation providing evidence for proteoglycan-collagen network formation in this region of the rat epiphysis.

• OSTI ID: 7191972
• Journal Information: Anatomical Record; (USA), Journal Name: Anatomical Record; (USA) Vol. 226:2; ISSN ANREA; ISSN 0003-276X
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINES
AMINO ACIDS
ANIMAL CELLS
ANIMAL TISSUES
ANIMALS
AUTORADIOGRAPHY
AZOLES
BIOSYNTHESIS
BODY
CARBOXYLIC ACIDS
CARTILAGE
CELL PROLIFERATION
CHEMICAL ANALYSIS
CHEMICAL COMPOSITION
COLLAGEN
CONNECTIVE TISSUE
ELECTRON MICROPROBE ANALYSIS
GLYCOPROTEINS
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HYDROGEN COMPOUNDS
MAMMALS
MICROANALYSIS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PROLINE
PROTEINS
PYRROLES
PYRROLIDINES
RATS
RODENTS
SCLEROPROTEINS
SYNTHESIS
TISSUES
TRITIUM COMPOUNDS
VERTEBRATES