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Glyoxylate cycle in the epiphyseal growth plate: isocitrate lyase and malate synthase identified in mammalian cartilage.
Anat Rec. 1989 Apr; 223(4):357-62.AR

Abstract

Peroxisomes were identified in chondrocytes from all zones of the mammalian epiphyseal growth plate by using light microscopic techniques for the cytochemical demonstration of catalase, the marker enzyme for these organelles. Additional cytochemistry showed the presence of malate-synthase-positive structures within the chondrocytes. The latter enzyme, also associated with peroxisomes, is unique to the glyoxylate shunt, a metabolic pathway thought to be absent in vertebrate tissues. The glyoxylate cycle allows the net conversion of lipid to carbohydrate, i.e., gluconeogenesis. Biochemical studies on growth plate cartilage indicate that this tissue has the capacity to carry out cyanide-insensitive B-oxidation of fatty acids. The latter takes place in a nonmitochondrial compartment, most likely the peroxisomal compartment. Additionally, both of the unique enzymes associated with the glyoxylate cycle, i.e., isocitrate lyase and malate synthase, were also identified in a cell-free homogenate of this cartilage. These studies indicate that cartilage, a poorly vascularized tissue characterized by its low oxygen tension and anaerobic glycolysis, may have the capacity to convert lipid to carbohydrate, i.e., gluconeogenesis via the glyoxylate pathway. In this way, cartilage may be unique among mammalian tissues.

Authors+Show Affiliations

Department of Anatomy, Baylor College of Dentistry, Dallas, Texas 75246.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

2712349

Citation

Davis, W L., et al. "Glyoxylate Cycle in the Epiphyseal Growth Plate: Isocitrate Lyase and Malate Synthase Identified in Mammalian Cartilage." The Anatomical Record, vol. 223, no. 4, 1989, pp. 357-62.
Davis WL, Jones RG, Farmer GR, et al. Glyoxylate cycle in the epiphyseal growth plate: isocitrate lyase and malate synthase identified in mammalian cartilage. Anat Rec. 1989;223(4):357-62.
Davis, W. L., Jones, R. G., Farmer, G. R., Matthews, J. L., & Goodman, D. B. (1989). Glyoxylate cycle in the epiphyseal growth plate: isocitrate lyase and malate synthase identified in mammalian cartilage. The Anatomical Record, 223(4), 357-62.
Davis WL, et al. Glyoxylate Cycle in the Epiphyseal Growth Plate: Isocitrate Lyase and Malate Synthase Identified in Mammalian Cartilage. Anat Rec. 1989;223(4):357-62. PubMed PMID: 2712349.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Glyoxylate cycle in the epiphyseal growth plate: isocitrate lyase and malate synthase identified in mammalian cartilage. AU - Davis,W L, AU - Jones,R G, AU - Farmer,G R, AU - Matthews,J L, AU - Goodman,D B, PY - 1989/4/1/pubmed PY - 1989/4/1/medline PY - 1989/4/1/entrez SP - 357 EP - 62 JF - The Anatomical record JO - Anat Rec VL - 223 IS - 4 N2 - Peroxisomes were identified in chondrocytes from all zones of the mammalian epiphyseal growth plate by using light microscopic techniques for the cytochemical demonstration of catalase, the marker enzyme for these organelles. Additional cytochemistry showed the presence of malate-synthase-positive structures within the chondrocytes. The latter enzyme, also associated with peroxisomes, is unique to the glyoxylate shunt, a metabolic pathway thought to be absent in vertebrate tissues. The glyoxylate cycle allows the net conversion of lipid to carbohydrate, i.e., gluconeogenesis. Biochemical studies on growth plate cartilage indicate that this tissue has the capacity to carry out cyanide-insensitive B-oxidation of fatty acids. The latter takes place in a nonmitochondrial compartment, most likely the peroxisomal compartment. Additionally, both of the unique enzymes associated with the glyoxylate cycle, i.e., isocitrate lyase and malate synthase, were also identified in a cell-free homogenate of this cartilage. These studies indicate that cartilage, a poorly vascularized tissue characterized by its low oxygen tension and anaerobic glycolysis, may have the capacity to convert lipid to carbohydrate, i.e., gluconeogenesis via the glyoxylate pathway. In this way, cartilage may be unique among mammalian tissues. SN - 0003-276X UR - https://www.unboundmedicine.com/medline/citation/2712349/Glyoxylate_cycle_in_the_epiphyseal_growth_plate:_isocitrate_lyase_and_malate_synthase_identified_in_mammalian_cartilage_ L2 - https://doi.org/10.1002/ar.1092230402 DB - PRIME DP - Unbound Medicine ER -