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Aminopeptidases and Dipeptidyl Peptidases Activities in Chicken Bone Tissue

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Aminopeptidases and Dipeptidyl Peptidases Activities in Chicken Bone Tissue Acta Histochem. Cytochem. Vol. 28 No. 3 281-286 (1995) Aminopeptidases and Dipeptidyl Peptidases Activities in Chicken Bone Tissue Osamu Fukushima and Hiroshi Yamashita Department of Anatomy (I), The Jikei University, School of Medicine, Minato-ku, Tokyo 105 Received for publication April 14, 1995 and in revised form July 4, 1995 There have been very few papers reporting ed. These activities were sensitive to on the localizations of aminopeptidases and 10 mM of ethylenediaminetetraacetic acid dipeptidyl peptidases activities in bone (EDTA). A DPP-I was seen in osteoclasts, tissue, although these peptidases seem to osteoblasts and osteocytes in the presence have important roles in bone resorption and of mercaptoethylamine (MEA), however Gly- osteoid degradation. The present study Arg-MNA hydrolyzing activity in the absence demonstrates these peptidases in fixed and of MEA was restricted to only osteoclasts. decalcified tibial metaphyses of 3-week-old DPP-II activity was present in osteoblasts chickens using the azo-dye methods at light and osteocytes, using Lys-Pro-MNA as a microscopic level. As substrates, amino substrate. There was no Lys-Ala-MNA acid derivatives of 4-methoxy-2-naphthyl- hydrolyzing activity in bone cells. The pre- amine (MNA) were used: Leu- or Ala-MNA sent study failed to demonstrate DPP-IV for aminopeptidase-M (AP-M, EC 3.4.11.2), activity in either 4% paraformaldehyde- or Glu-MNA for aminopeptidase-A (AP-A, EC 2.5% glutaraldehyde-fixed samples, 3.4.11.7), Gly-Arg-MNA for dipeptidyl pep- although it was observed in the glomerulus tidase-I (DPP-I, EC 3.4.14.1), Lys-Ala- or and proximal convoluted tubule cells of the Lys-Pro-MNA for dipeptidyl peptidase-II rat kidney fixed with glutaraldehyde. The (DPP-II, EC 3.4.14.2), and Gly-Pro-MNA for present study suggests that AP-M and DPP-I dipeptidyl peptidase-IV (DPP-IV, EC in osteoclasts, and AP-A, DPP-I and DPP-II in 3.4.14.5). An AP-M in osteoclasts, and AP- osteoblasts seem to function in the bone A in osteoblasts and osteocytes were observ- remodeling process. Key words: Bone, Aminopeptidase, Dipeptidyl peptidase, Enzyme histochemistry I. Introduction 2-naphthylamide substrate caused significant diffusion of the reaction product due to the slow rate of coupling of The bone matrix consists mainly of hydroxyapatite, 2-naphthylamide to a diazonium salt and considerable collagen, non-collagenous proteins and proteoglycans, aqueous solubility of the reaction product. They recom- and is constantly remodeled. Therefore, proteases have mended 4-methoxy-2-naphthylamine (MNA) substrates important roles in matrix resorption. However, there for investigating precise localizations of proteases with en- have been very few papers addressing histochemical zyme histochemical techniques (azo-dye methods). San- localizations of proteases, with the exception of cathepsins nes and colleagues [15] employed MNA substrates for B, L and D [5, 6, 9, 13, 15, 20]. Lipp [10] first reported demonstration of dipeptidyl peptidases I and II (DPP-I, that aminopeptidase-M (AP-M) activity was present in DPP-II), and showed DPP-I in osteoblasts, osteocytes, osteoclasts, osteoblasts and endothelial cells at the and chondrocytes in proliferating and hypertrophic vascular invasion in growth plate using Leu-2-naphthyl- regions of the growth plate, and DPP-II in osteoblasts, amide as a substrate. Smith and van Frank [18] showed osteocytes, and chondrocytes in the resting zone. In the same experiment, they failed to demonstrate cathepsin B This work was supported by a Grand-in Aid for Scientific Research, activity in the bone, although it was strongly positive in No. 05670030, from the Ministry of Education, Science and Culture, osteoclasts with other enzyme histochemical [5, 20] and im- Japan. munohistochemical studies [6, 9, 13, 16]. Further, there Correspondence to: Dr. Osamu Fukushima, Department of Anatomy has been no trial to demonstrate AP-A and DPP-IV (I), The Jikei University, School of Medicine, 25-8 Nishishinbashi-3- activities in the bone. chome, Minato-ku, Tokyo 105, Japan. The present study, using azo-dye methods with MNA 281 282 Fukushima and Yamashita substrates, showed AP-M and DPP-I in osteoclasts, and B. DPP-IV medium: 1.0 mM Gly-Pro-MNA, 0.1 M AP-A, DPP-I and DPP-II in osteoblasts and osteocytes. cacodylate buffer (pH 7.4), 2.0 mM Fast Blue B. All substrate was purchased from Enzyme System Products II. Materials and Methods (CA, U.S.A.). As controls, substrate-omitted media (all media), 10 mM EDTA containing media (AP-M and AP-A For the present study, 9 domestic chickens of 3 weeks media), and MEA-omitted medium (DPP-I medium) were of age (body weight 120-140g), were purchased from also prepared. After incubation, sections were rinsed Saitamajikkendoubutsu-kyokyusho (Saitama, Japan). with distilled water, and immersed in 2% CuSO4 for The chickens were anesthetized with ether, then tibial 5 min. Sections were rinsed in distilled water again, then metaphyses were dissected out quickly and cut into small mounted with glycerin jelly, and observed by conventional blocks. The blocks were divided into three groups, and light microscopy. each group was immersed in one of the following three As positive controls, kidneys (cortex) of Wistar male kinds of fixative for 60 min at 0-4•Ž: 4% parafor- rats (8-weeks old) fixed with 1% GLA-4% PFA were also maldehyde (PFA) in 0.1 M cacodylate buffer (pH 7.2) con- prepared. taining 8% sucrose, 1% glutaraldehyde (GLA)-4% PFA in 0.1 M cacodylate buffer (pH 7.2), or 2.5% GLA in 0.1 M III. Results cacodylate buffer (pH 7.2) containing 8% sucrose. The blocks were rinsed in 0.1 M cacodylate buffer (pH 7.2) 1. AP-M activity containing 8% sucrose (cacodylate-buffered sucrose), AP-M activity was seen in osteoclasts which were then decalcified with 5% ethylenediaminetetraacetic acid attached to the bone matrix, using either Leu-MNA or (EDTA) in 30 mM N-(2-hydroxyethyp-piperazine-N'-2- Ala-MNA as a substrate. There was no difference in ethanesulfonic acid (HEPES) buffer (pH 7.2) containing localization and intensity of the activity between the 8% sucrose [4] at 4•Ž for 3 days. The blocks were treated two substrates. No activity was observed in osteoblasts, sequentially with 10%, 15%, 20% and 25% sucrose, then osteocytes and endothelial cells (Fig. 1). There was no embedded in OCT compound (Tissue Tek, Miles Inc. IN, reaction product in the bone matrix. The activity was U.S.A.), and frozen in dry-ice acetone. Frozen blocks markedly inhibited by 10 mM EDTA (Fig. 2). The were stored at -80•Ž until use. Cryostat sections, 8 ƒÊm substrate-omitted medium yielded no activity (not in thickness, were placed on poly-L-lysine (Sigma, P-1524) shown). The activity was observed in 4% PFA-, 1% coated slide glasses, and air dried. Sections were in- GLA-4% PFA-, and 2.5% GLA-fixed samples. cubated in the following media for 30 min at 37•Ž, accor- In the rat kidney, the activity was restricted to the ding to Sannes [14]. AP-M medium: 1.6 mM Leu-MNA brush border of proximal convoluted tubule cells (not or Ala-MNA, 0.1 M phosphate buffer (pH 6.7), 2.0 mM shown). Fast Blue B (Sigma, D-3502). AP-A medium: 1.7 mM Glu-MNA, 0.1 M phosphate buffer (pH 6.7), 2.0 mM Fast 2. AP-A activity Blue B. DPP-I medium: 1.0 mM Gly-Arg-MNA, 0.1 M AP-A activity was present in osteoblasts and phosphate buffer (pH 6.0), 10 mM EDTA, 1.0 mM mercap- osteocytes. Osteoclasts did not possess the activity. The toethylamine (MEA, Sigma, M-6500), 0.2 mM Fast Blue activity was seen only in 4% PFA-fixed samples (Fig. 3), B. DPP-II medium: 1.0 mM Lys-Pro-MNA or Lys-Ala- with no reaction product in 1% GLA-4% PFA-, and 2.5% MNA, 0.05 M cacodylate buffer (pH 5.5), 2 mM Fast Blue GLA-fixed bone tissues (not shown). EDTA had a strong Fig. 1. Aminopeptidase-M (EC 3.4.11.2) activity using Leu-MNA as a substrate in 2.5% GLA-fixed chicken tibial metaphyses. The activity was present in osteoclasts which were attached to the bone matrix. There was no activity in osteoblasts, osteocytes, pre-osteoclasts and detach- ed osteoclasts. Arrows indicate attached osteoclasts. •~480. Fig. 2. Aminopeptidase-M activity in the presence of 10 mM EDTA in 2.5% GLA-fixed bone tissues. As a substrate, Leu-MNA was employed. The activity was significantly inhibited by EDTA. Arrow indicates an attached osteoclast. •~480. Fig. 3. Aminopeptidase-A (EC 3.4.11.7) activity in 4% PFA-fixed bone tissues. The activity was seen in osteoblasts and osteocytes. Osteoclasts (arrow) did not possess the enzyme. •~240. Fig. 4. Aminopeptidase-A activity in the influence of 10 mM EDTA in 4% PFA-fixed bone tissues. The activity was significantly inhibited by EDTA. Arrow indicates an osteoclast. •~240. Fig. 5. Dipeptidyl peptidase-I (EC 3.4.14.1) activity in 2.5% GLA-fixed bone tissues. In the presence of MEA, a SH-reagent, the activity was present in osteoblasts, osteocytes and osteoclasts (arrows). •~240. Fig. 6. A Gly-Arg-MNA hydrolyzing activity in the absence of MEA in 2.5% GLA-fixed bone tissues. The activity was restricted to only osteoclasts. There was no reaction product in osteoblasts and osteocytes. Arrow indicates an osteoclast. •~480. Fig. 7. Dipeptidyl peptidase-II (EC 3.4.14.2) activity with Lys-Pro-MNA as a substrate in 2.5% GLA-fixed bone tissues.
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