Characterization of a Monoclonal Antibody Recognizing Small Collagenous Proteins in Fetal Bone

Kuwata, Fumiyuki; Maeno, Masao; Yao, Kam-Ling; Domenicucci, Carmelo; Goldberg, Harvey A.; Wasi, Safia; Aubin, Jane E.; Sodek, Jaro

doi:10.1016/s0174-173x(87)80020-1

“…Our data suggest that MBP-322 could be a useful method for identification of bone matrix-resorbing osteo- clasts, as it identifies degraded collagen within those cells, suggesting recent bone resorption activity (Kuwata et al, 1987;Salonen et al, 1990), and does not identify osteoclast precursors or apoptotic cells, as determined by TRAP assessment. Identification of bone matrix-resorbing osteoclasts is important because they are required for alveolar bone remodeling coincident to tooth translocation.…”

Section: Discussionmentioning

confidence: 88%

“…This antibody has been reported to recognize an epitope within the unfolded alpha chains of interstitial collagens I-III and the alpha1 chain of type V collagen, but not the native forms of these collagens (Kuwata et al, 1987). Thus, the MBP-322 antibody could possibly be a valid marker for osteoclasts involved in bone matrix degradation, because it specifically recognizes denatured collagen and collagen fragments within both cells and tissues (Kuwata et al, 1987;Salonen et al, 1990). This methodology has advantages for histomorphometric analysis of bone resorption over enzymatic methods detecting cathepsin K and matrix metalloproteinases, which only indicate cells that secrete collagenolytic enzymes (Zaidi et al, 2003).…”

mentioning

confidence: 99%

“…The MBP-322 antibody has been used for examining the relationship between the presence of denatured/ unfolded collagen within regions of rapid collagen remodeling, such as within the PDL (Salonen et al, 1990). This antibody has been reported to recognize an epitope within the unfolded alpha chains of interstitial collagens I-III and the alpha1 chain of type V collagen, but not the native forms of these collagens (Kuwata et al, 1987). Thus, the MBP-322 antibody could possibly be a valid marker for osteoclasts involved in bone matrix degradation, because it specifically recognizes denatured collagen and collagen fragments within both cells and tissues (Kuwata et al, 1987;Salonen et al, 1990).…”

mentioning

confidence: 99%

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Osteoclast distribution within the rat interdental septum coincident to experimental tooth movement using light forces

Johnson

¹

2006

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There is little quantitative information concerning the number and distribution of bone-matrix resorbing osteoclasts (BMRO) within the adjacent alveolar bone coincident to tooth movement. We moved the right first maxillary molar tooth anteriorly in 40 female rats (E), the left side was untreated, serving as an internal control (IC). Forty female age and weight matched rats were untreated, serving as external controls (EC). BMRO were identified on periosteal and endosteal surfaces of the interdental sep-tum from 1-5 days after initial force application using the MTB-322 anti-body. The number of BMRO at periosteal surfaces of E was greater in IC and EC from 2-5 days (P < 0.001). Similarly, the number of BMRO at endo-steal surfaces was greater from 1-5 days (P < 0.001). The number of BMRO at periosteal and endosteal surfaces was greater within E than within EC from 1-5 days (P < 0.001). Outcome data from IC were often significantly different from EC. Our data suggest that relatively low forces increase the number of BMRO, which are not uniformly distributed onto both periosteal and endosteal surfaces. Thus, the interdental septum resorbs at the alveolar wall and within spaces between the trabeculae, which, taken together, results in net removal of bone from areas of compression. These data also suggest that experimental tooth movement produces significant differences in the number and distribution of BMRO within IC and EC. Thus, EC groups should be included in studies of tooth movement. Anat Rec, 290:74-82, 2007.

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“…Proteins were electrophoretically transferred from gels onto nitrocellulose membranes (Immobilon PVDF; Millipore Co., Bedford, MA, USA) at 0.8 mA/cm 2 for 80 min using semi-dry electro-blotting system (Sartoblot; Sartorius, Goettinggen, Germany). Immunoblotting (Western blotting) was performed according to a modification of a protocol of Kuwata et al [18]. Briefly, the transferred nitrocellulose sheets were washed with 0.15 M NaC1/10mM Tris (TBS), pH 7.4, for 10 rain, then incubated with a blocking reagent (Boehringer Mannheim Biochemica, Mannheim, Germany) at pH 7.4 overnight at 4~…”

Section: Western Blotsmentioning

confidence: 99%

Biochemical study on the tissue compartmentalization of phosphophoryn, osteopontin and bone sialoprotein (BSP) in rat incisor dentin

Nagata

¹

,

Kawahara

²

,

Kasahara

³

et al. 1994

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Abstract:The tissue compartmentalization of phosphophoryn, osteopontin (OPN) and bone sialoprotein (BSP) in dentin was biochemically analyzed. The radicular portion of rat incisor was excised and sequentially extracted; i.e., proteins non-covalently bound to matrix such as soft tissues were solubilized with 4 M guanidinium chloride (G1), mineral-binding proteins were then extracted with 0.5 M EDTA (E), proteins noncovalently bound to the collagen matrix were extracted with 4 M guanidinium chloride (G2) after E, and finally the proteins covalently bound to the collagen matrix were extracted by bacterial collagenase digestion (C). Stains-All and Rhodamine B staining, which selectively stain calciun~-binding proteins, revealed a 50~80 kDa broad band in the E extract on 10 % polyacrylamide gels. This intense band disappeared after precipitation with CaC12, indicating that the protein is phosphophoryn. After removing phosphophoryn from the E extract, 67 kDa intense and 50 kDa weak bands appeared on the gels stained with Stains-All. The 67 kDa protein was observed similarly in the G2 and C extracts. Western blots using monoclonal antibodies revealed the presence of 67 kDa BSP and 50 kDa OPN. When the tissue compartmentalization was compared, these three proteins were not detected in the G1 extract, phosphophoryn and osteopontin were localized only in the E extract, and BSP was observed not only in the E extract but also in the G2 and C extracts. These findings indicate that phosphophoryn, OPN and BSP are rapidly incorporated into the mineralized fraction and that BSP also binds to collagen-related fraction, suggesting the association with intial mineralization in the dentin.

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“…The MBP‐322 antibody has been used for examining the relationship between the presence of denatured/unfolded collagen within regions of rapid collagen remodeling, such as within the PDL (Salonen et al, 1990). This antibody has been reported to recognize an epitope within the unfolded alpha chains of interstitial collagens I–III and the alpha1 chain of type V collagen, but not the native forms of these collagens (Kuwata et al, 1987). Thus, the MBP‐322 antibody could possibly be a valid marker for osteoclasts involved in bone matrix degradation, because it specifically recognizes denatured collagen and collagen fragments within both cells and tissues (Kuwata et al, 1987; Salonen et al, 1990).…”

mentioning

confidence: 99%

Osteoclast distribution within the rat interdental septum coincident to experimental tooth movement using light forces

Johnson¹

2007

The Anatomical Record

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There is little quantitative information concerning the number and distribution of bone-matrix resorbing osteoclasts (BMRO) within the adjacent alveolar bone coincident to tooth movement. We moved the right first maxillary molar tooth anteriorly in 40 female rats (E), the left side was untreated, serving as an internal control (IC). Forty female age and weight matched rats were untreated, serving as external controls (EC). BMRO were identified on periosteal and endosteal surfaces of the interdental septum from 1-5 days after initial force application using the MTB-322 antibody. The number of BMRO at periosteal surfaces of E was greater in IC and EC from 2-5 days (P < 0.001). Similarly, the number of BMRO at endosteal surfaces was greater from 1-5 days (P < 0.001). The number of BMRO at periosteal and endosteal surfaces was greater within E than within EC from 1-5 days (P < 0.001). Outcome data from IC were often significantly different from EC. Our data suggest that relatively low forces increase the number of BMRO, which are not uniformly distributed onto both periosteal and endosteal surfaces. Thus, the interdental septum resorbs at the alveolar wall and within spaces between the trabeculae, which, taken together, results in net removal of bone from areas of compression. These data also suggest that experimental tooth movement produces significant differences in the number and distribution of BMRO within IC and EC. Thus, EC groups should be included in studies of tooth movement. Anat Rec, 290:74-82, 2007. 2006 Wiley-Liss, Inc.Key words: experimental tooth movement; osteoclast; alveolar bone; ratExperimental tooth movement produces tension/compression forces within the periodontal ligament (PDL), which are transferred to the adjacent alveolar bone (Tanne et al., 1987;Katona et al., 1995;Middleton et al., 1996;Puente et al., 1996;Tamatsu et al., 1996). These forces initiate cellular responses, which produce selective remodeling of the alveolus for support of the migrating tooth. During this process, bone is deposited onto the alveolar wall within regions experiencing tension forces, and bone resorption is evident at sites experiencing compression forces (Macapanpan et al., 1954;Waldo and Rothblatt, 1954;Zaki and Van Huysen, 1963;Azuma, 1970;Lopez Otero et al., 1973;Heller and Nanda, 1979;Yamasaki et al., 1980;Lilja et al., 1984;Martinez and Johnson, 1987;Chao et al., 1988;Lee, 1990;King et al., 1991aKing et al., , 1991bKing and Keeling, 1995;Ashizawa and Sahara, 1998). Alveolar bone resorption occurs at the alveolar wall adjacent to regions of compression within the PDL (periosteal surfaces) and within the vascular intertrabecular spaces (endosteal surfaces).

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Characterization of a Monoclonal Antibody Recognizing Small Collagenous Proteins in Fetal Bone

Cited by 15 publications

References 29 publications

Osteoclast distribution within the rat interdental septum coincident to experimental tooth movement using light forces

Osteoclast distribution within the rat interdental septum coincident to experimental tooth movement using light forces

Biochemical study on the tissue compartmentalization of phosphophoryn, osteopontin and bone sialoprotein (BSP) in rat incisor dentin

Osteoclast distribution within the rat interdental septum coincident to experimental tooth movement using light forces

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