Summary
Carbonic anhydrase isoenzymes I and II have been localized in human bone and cartilage. Osteoclasts are strongly positive for carbonic anhydrase II but very little if any reaction is observed for carbonic anhydrase I. In tendon giant cell tumor osteoclastlike-giant cells contained high amounts of carbonic anhydrase II suggesting the close relation of these cells to normal osteoclasts. In growth plate cartilage strong staining was obtained in late proliferative and hypertrophic chondroxytes as well as in extracellular matrix of hypertrophic zone also only with anti-human carbonic anhydrase II.
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Baron R, Neff L, Louvard D, Courtoy PJ (1983) Specific localization of a lysosomal membrane protein related to a proton pump at the ruffled border of osteoclasts. J Cell Biol 97:108
Cuervo LA, Pita JC, Howell DS (1981) Ultramicroanalysis of pH, pCO2 and carbonic anhydrase activity at calcifying sites in cartilage. Calcif Tissues Res 7:220–231
Fallon MD (1983) Bone resorption fluid from osteoclasts is acidic. An in vitro micropuncture study. VIIIth International Conference on Calcium Regulating Hormones, Kobe, Japan
Gay CV, Mueller WJ (1974) Carbonic anhydrase and osteoclasts: Localization by labelled inhibitor autoradiography. Science 183:432–434
Gay CV, Anderson RE, Schraer H, Howell DS (1982) Identification of carbonic anhydrase in chick growth plate cartilage. J Histochem Cytochem 30:391–394
Kumpulainen T, Korhonen LK (1978) Immunohistochemical demonstration of carbonic anhydrase. Histochemistry 58:183–192
Kumpulainen T, Väänänen HK (1982) Immunohistochemical demonstration of extracellular carbonic anhydrase in epiphyseal growth cartilage. Calcif Tissue Int 34:428–430
Sly WS, Hewett-Emmett D, Whyte MP, Yh YS, Tashian RE (1983) Carbonic anhydrase II deficiency identified as the primary defect in the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification. Proc Natl Acad Sci USA 80:2752–2756
Tashian RW, Hewett-Emmett D, Goodman M (1983) In: Rattazzi MC, Scandalios JG, Whitt GS (eds) Isoenzymes, Current topics in biological and medical research, Vol. 7 Liss, New York, pp 79–100
Wistrand PJ (1981) The importance of carbonic anhydrase B and C for the unleading of CO2 by the human erythrocyte. Acta Physiol Scand 113:417–426
Väänänen HK, Parvinen EK (1983) High active isoenzyme of carbonic anhydrase in rat calvaria osteoclasts. Histochemistry 78:481–485
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Väänänen, H.K. Immunohistochemical localization of carbonic anhydrase isoenzymes I and II in human bone, cartilage and giant cell tumor. Histochemistry 81, 485–487 (1984). https://doi.org/10.1007/BF00489754
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DOI: https://doi.org/10.1007/BF00489754