Summary
Mandibular condyles of 4-week-old Wistar strain rats and mandibles of ICR strain mice from 14 days gestation stage to 2 days postnatal stage were used to investigate the localization of Maclura pomifera lectin (MPA) during two modes of osteogenesis. During endochondral ossification of the mandibular condyle, MPA was only localized at the peripheral regions of calcified cartilage after the destruction of chondrocyte lacunae. Bone extracellular matrix (ECM) was not reacted with MPA. In intramembranous ossification of mice mandibles, MPA was stained intensively in the early bone ECM. The intensity of the MPA reaction decreased during bone development. In both cases of osteogenesis, chondroclasts and osteoclasts showed the strong affinity to MPA. These results indicated that the time- and position-specific changes within ECM proceeded during osteogenesis and that MPA was the useful probe to detect chondroclasts and osteoclasts.
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Akita H, Kobayashi Y, Kagayama M (1988) A histochemical study on lectin binding in the immature enamel and secretory ameloblasts of rat incisors. Tohoku J Exp Med 155:139–149
Arsenault AL, Ottensmeyer FP (1984) Visualization of early intramembranous ossification by electron microscopic and spectroscopic imaging. J Cell Biol 98:911–921
Aulthouse AL, Solursh M (1987) The detection of a precartilage, blastema-specific marker. Dev Biol 120:377–384
Bernard GW, Pease DC (1969) An electron microscopic study of initial intramembranous osteogenesis. Am J Anat 125:271–290
Buckwalter JA, Rosenberg LC, Ungar R (1987) Changes in proteoglycan aggregates during cartilage mineralization. Calcif Tissue Int 41:228–236
Burnell JM, Teubner EJ, Miller AG (1980) Normal maturational changes in bone matrix, mineral, and crystal size in the rat. Calcif Tissue Int 31:13–19
Campo RD, Betz RR (1987) Loss of proteoglycans during decalcification of fresh metaphyses with disodium ethylenediaminetetraacetate (EDTA). Calcif Tissue Int 41:52–55
Campo RD, Romano JE (1986) Changes in cartilage proteoglycans associated with calcification. Calcif Tissue Int 39:175–184
Durkin JF, Heeley JD, Irving JT (1973) The cartilage of the mandibular condyle. Oral Sci Rev 2:29–99
Farnum CE (1985) Binding of lectin fluorescein conjugates to intracellular components of growth-plate chondrocytes in situ. Am J Anat 174:419–435
Gallagher JT (1984) Carbohydrate-binding properties of lectins: A possible approach to lectin nomenclature and classification. Biosci Rep 4:621–632
Gibson GJ, Flint MH (1985) Type X collagen synthesis by chick sterna cartilage and its relationship to endochondral development. J Cell Biol 101:277–284
Gibson GJ, Beaumont BW, Flint MH (1984) Synthesis of a low molecular weight collagen by chondrocytes from the presumptive calcification region of the embryonic chick sterna: The influence of culture with collagen gels. J Cell Biol 99:208–216
Grynpas MD, Hunter GK (1988) Bone mineral and glycosaminoglycans in newborn and mature rabbits. J Bone Min Res 3:159–164
Hall BK (1983) Tissue interactions and chondrogenesis. In: Hall BK (ed) Cartilage, vol 2: Development, differentiation, and growth. Academic Press, New York, pp 187–222
Horton WA, Dwyer C, Goering R, Dean DC (1983) Immunohistochemistry of types I and II collagen in undecalcified skeletal tissues. J Histochem Cytochem 31:417–425
Irwin MH, Silvers SH, Mayne R (1985) Monoclonal antibody against chicken type IX collagen: Preparation, characterization, and recognition of the intact form of type IX collagen secreted by chondrocytes. J Cell Biol 101:814–823
Jee WSS (1983) The skeletal tissue. In: Weiss L (ed) Histology, Cell and tissue biology. 5th edn. Macmillan Press, London, pp 200–255
Kallio DM, Garant PR, Minkin C (1971) Evidence of coated membranes in the ruffled border of the osteoclast. J Ultrastruct Res 37:169–177
Krane SM, Dayer J-M, Simon LS, Byrne MS (1985) Mononuclear cell-conditioned medium containing mononuclear cell factor (MCF), homologous with interleukin 1, stimulates collagen and fibronectin synthesis by adherent rheumatoid synovial cells: effects of prostaglandin E2 and indomethacin. Collagen Relat Res. 5:99–117
Kumpulainen T, Väänänen HK (1982) Immunohistochemical demonstration of extracellular carbonic anhydrase in epiphyseal growth plate cartilage. Calcif Tissue Int 34:428–430
Lenette DA (1978) An improved mounting medium for immunofluorescence microscopy. Am J Clin Pathol 69:647–648
Mackie EJ, Thesleff I, Chiquet-Ehrismann R (1987) Tenascin is associated with chondrogenic and osteogenic differentiation in vivo and promote chondrogenesis in vitro. J Cell Biol 105:2569–2579
Marie PJ, Hott M (1987) Histochemical identification of carbonic anhydrase in fetal rat bone embedded in glycomethacrylate. J Histochem Cytochem 35:245–250
Martino LJ, Yeager VL, Taylor JJ (1979) An ultrastructural study of the role of calcification nodules in the mineralization of woven bone. Calcif Tissue Int 27:57–64
Mundy GR, Roodman GD (1987) Osteoclast ontogeny and function. In: Peck WA (ed) Bone and mineral research/5. A yearly survey of developments in the field of bone and mineral metabolism. Elsevier, Amsterdam New York Oxford, pp 209–279
Oursler MJ, Bell LV, Clevinger B, Osdoby P (1985) Identification of osteoclasts-specific monoclonal antibodies. J Cell Biol 100:1592–1600
Owen M, Shetlar MR (1968) Uptake of 3H-glucosamine by osteoclasts. Nature 220:1335–1336
Poole AR, Pidoux I, Rosenberg LC (1982a) Role of proteoglycans in endochondral ossification: Immunofluorescent localization of link protein and proteoglycan monomer in bovine fetal epiphyseal growth plate. J Cell Biol 92:249–260
Poole AR, Pidoux I, Reiner A, Rosenberg LC (1982b) An immunoelectron microscopic study of the organization of proteoglycan monomer, link protein, and collagen in the matrix of articular cartilage. J Cell Biol 92:921–937
Poole AR, Pidoux I, Reiner A, Choi H, Rosenberg LC (1984) Association of an extracellular protein (chondrocalcin) with the calcification of cartilage in endochondral bone formation. J Cell Biol 98:54–65
Rifas L, Shen V, Mitchell K, Peck WA (1984) Macrophage-derived growth factor for osteoblast-like cells and chondrocytes. Proc Natl Acad Sci USA 81:4558–4562
Sarkar M, Wu AM, Kabat EA (1981) Immunochemical studies on the carbohydrate specificity of Maclura pomifera lectin. Arch Biochem Biophys 209:204–218
Schmid TM, Linsenmayer TF (1985) Immunohistochemical localization of short chain cartilage collagen (type X) in avian tissues. J Cell Biol 100:598–605
Sherft JP (1972) The lamina limitans of the organic matrix of calcified cartilage and bone. J Ultrastruct Res 38:318–331
Shimokado K, Raines EW, madtes DK, Barrett TB, Benditt EP, Ross R (1985) A significant part of macrophage-derived growth factor consists of at least two forms of PDGF. Cell 43:277–286
Takagi M, Saito I, Kuwata F, Otsuka K (1988a) Specific binding of peanut agglutinin and soybean agglutinin to chondroitinase ABC-digested cartilage proteoglycans: histochemical, ultrastructural cytochemical, and biochemical characterization. Histochem J 20:88–98
Takagi M, Yagasaki H, Baba T, Baba H (1988b) Ultrastructural visualization of selective peanut agglutinin binding sites in rat osteoclasts. J Histochem Cytochem 36:95–101
Thesleff I, Kantomaa T, Mackie E, Chiquet-Ehrismann R (1988) Immunohistochemical localization of the matrix glycoprotein tenascin in the skull of the growing rat. Archs Oral Biol 33:383–390
Väänänen KK, Malmi R, Tuukkanen J, Sundquist K, Harkonen P (1986) Identification of osteoclasts by rhodamine-conjugated peanut agglutinin. Calcif Tissue Int 39:161–165
Van der Rest M, Rosenberg LC, Olsen BR, Poole AR (1986) Chondrocalcin is identical to the C-propeptide of type II procollagen. Biochem J 297:923–925
Velasco A, Hidalgo J (1987) Light and electron microscopical localization of concanavalin-A lectin binding sites in rat epiphyseal chondrocytes. Histochem J 19:7–14
Velasco A, Hidalgo J, Muller M, Garcia-Herduga G (1988) Ultrastructural demonstration of lectin binding sites in the golgi apparatus of rat epiphyseal chondrocytes. Histochemistry 89:177–184
Wright GM, Leblond CP (1981) Immunohistochemical localization of procollagens. III. Type I procollagen antigenesity in osteoblasts and prebone (osteoid). J Histochem Cytochem 29:791–804
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Nakamura, M., Akita, H., Mizoguchi, I. et al. A histochemical localization on Maclura pomifera lectin during osteogenesis. Histochemistry 92, 225–230 (1989). https://doi.org/10.1007/BF00500922
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DOI: https://doi.org/10.1007/BF00500922