Ultrastructure and Proteoglycan Composition in the Developing Fibrocartilaginous Region of Bovine Tendon

doi:10.1016/S0934-8832(11)80150-2

Matrix

Volume 10, Issue 6, December 1990, Pages 420-436

https://doi.org/10.1016/S0934-8832(11)80150-2 Get rights and content

Abstract

Clear distinctions in morphology and proteoglycan composition have been described in regions of adult tendon that pass under bone and are subjected to compressive as well as tensional forces. In this study, developing bovine deep flexor tendon from early fetal stages through 6 months of age was examined biochemically and by light and electron microscopy. Longitudinal collagen fibers were seen in the tensional region of tendon throughout development; whereas a well established network arrangement of collagen fibers with wide interfibrillar spaces was seen in the compressed region by 7 months of fetal age. Collagen fibril diameters of both regions increased with age with the mean diameter in tensional tissue always greater than in compressed tissue. Glycosaminoglycan hexosamine content of the tensional region remained low throughout development (∼0.2% of dry tissue weight), but increased in the compressed region from 0.4% of dry weight at the 7-month fetal stage, to 1.0% dry weight at 6 months. Keratan sulfate was not detectable in tensional tendon at any age as measured by inhibition ELISA, but was found in increasing quantities in the pressure bearing region of tendon from young calves. Small proteoglycans predominated in both tensional and compressed regions throughout fetal and early neonatal development, and were of both PG I (biglycan) and PG 11 (decorin) types. Large proteoglycans represented only a small proportion of total proteoglycans in both regions of fetal tendon. By SDS/PAGE analysis, immunoreactivity, and molecular sieve chromatography, large proteoglycans of fetal compressed tendon were similar to large proteoglycans of adult tensional tendon in that they contained only chondroitin-6-sulfate, with little if any KS, and appeared to be slightly smaller than cartilage large proteoglycans. In mature compressed tendon, a different population of large proteoglycans containing KS and both C-6-S and C-4-S was predominant. This large proteoglycan population, which is more like proteoglycans of cartilage, did not accumulate in pressure bearing tendon until 3–6 months of age. Rearrangement of collagen fibers in the compressed region of tendon occurred in utero, significantly before the accumulation of cartilage-like large proteoglycans.

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^a: Stephen Evanko, University of New Mexico, Department of Biology, Albuquerque, NM 87131, USA.

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Ultrastructure and Proteoglycan Composition in the Developing Fibrocartilaginous Region of Bovine Tendon

Abstract

J. Invest. Dermatol.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

Anal. Biochem.

J. Biol. Chem.

Amer. J. Ophthal.

J. Biol. Chem.

J. Biol. Chem.

Int. Rev. Cytol.

Determination of glycosaminoglycans (mucopolysaccharides) from tissues on the microgram scale

Biochim. Biophys. Acta

Two improved and simplified methods for the spectrophotometric determination of hydroxyproline

Anal. Chem.

Determination of pentose in the presence of large quantities of glucose

Arch. Biochem. Biophys.

Production and characterization of monoclonal antibodies directed against connective tissue proteoglycans

Fed. Proc.

Development of regional specializations in rabbit fibrocartilage

J. Cell Biol.

Streaming potentials: a sensitive index of enzymatic degradation in articular cartilage

J. Orthopaed. Res.