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Biomedical subjects

K Bessho

Publications and source records attributed to K Bessho.

70 records · Page 4Linked to original sources
PubMed1990

Purification of rabbit bone morphogenetic protein derived from bone, dentin, and wound tissue after tooth extraction.

Bone morphogenetic protein (BMP) was extracted from bone matrix, dentin matrix, and wound tissue after tooth extraction in rabbits, and purified. These purified fractions were shown to be homogeneous by sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis (SDS-PAGE), and induced new bone in situ in 3 weeks when implanted into the calf muscles of Wistar rats. The dentin matrix-derived BMP was different from the other two types in molecular weight and the properties revealed in the process of purification. However, each tissue-derived BMP was shown to induce new bone growth in a bioassay of xenogenic implantation. For this reason, BMP is thought to have subunits with certain commonalities in different tissue.

Animals↗
PubMed1989

Purification of bone morphogenetic protein derived from bovine bone matrix.

Bone morphogenetic protein (BMP) was extracted from the bovine bone matrix and purified by liquid chromatography. The molecular weight of the BMP was 18 kDa by SDS-PAGE, and its pI value was 4.9. Amino acid analysis suggested that the BMP is a polypeptide containing 163 amino acids. In the present study, telopeptide-free type I collagen was used as a carrier of BMP.

Amino Acids↗
PubMed1989

Monostotic fibrous dysplasia with involvement of the mandibular canal.

A 72-year-old woman sought treatment with a rare monostotic fibrous dysplasia occurring in the mandible and involving the mandibular canal. Her chief complaint was swelling, which had appeared about 2 years previously, had enlarged gradually, and was associated with spontaneous pain. X-ray film examination revealed a ground-glass opaque image of blurred demarcation, and 99mTc-methylene diphosphonate bone scintigraphy disclosed an area of marked radioisotope uptake. Histopathologic examination revealed the area of bone marrow and spongy bone to be replaced by fibrous tissue, irregular beam-shaped woven bone, and lamellar bone. Contouring of the expanded portion of the bone and surgical decompression of the mandibular canal were performed with good results.

Aged↗
PubMed1988

Studies on peptides CLVIII. Model experiments for the synthesis of open-chain unsymmetrical cystine-peptides.

Treatment of a mixture of Cys(R)(O) and Cys(R') with an acid was found to generate cystine in fairly good yields, when suitable R, R', and an acid were selected. An unsymmetrical cystine peptide was prepared by treatment of a mixture of Z(OMe)-Cys(R) (0)-Ala-NH2 (R = Acm or MBzl) and Z(OMe)-Cys(MBzl)-Gly-OBzl with TFA or 1 M TFMSA/TFA3. Oxytocin was obtained in an excellent yield by TFA treatment of the protected peptide containing Cys(Acm)(0) and Cys(MBzl). Thus, formation of the disulfide bond was found feasible at the position of Cys(R) (0).

Cystine↗
PubMed1987

Osteoma in mandibular condyle.

A case of peripheral osteoma occurring in the mandibular ramus in a 26-year-old man is reported. Radiographic examination revealed a pedunculated, protruding globular, bone-like opaque mass around the notch of the right mandibular ramus. Histopathological examination showed a lamellar bone structure with irregular arrangement. Wide trabeculae, narrow interstitial areas, and many fibrovascular channels were detected by scanning electron microscopy. Thus, characteristic findings of a compact osteoma were obtained clinically and histopathologically.

Adult↗
PubMed1984

[Undifferentiated carcinoma of the thyroid gland with osteoclast-like giant cells--a case report].

A case of undifferentiated carcinoma of the thyroid gland with osteoclast-like giant cells resembling those of a giant cell tumor of the bone is presented. A 79-year-old female had noticed swelling on the left frontal neck. Histological examination of frontal-neck tumor revealed undifferentiated carcinoma of the thyroid gland. The patient was treated with a Cobalt 60 unit and received a total tumor dose of 2800 rad. However, because of a rapid increase in size of the tumor and its metastasis, the patient died about 2 months after admission. An autopsy was performed. Histologically, the tumor differed from the usual undifferentiated carcinoma of the giant cell type in having osteoclast-like giant cells with many small, uniform, benign appearing nuclei. It is proposed that the osteoclast-like giant cell is reactive rather than neoplastic in nature because of the benign appearance, phagocytotic activity and some ultrastructural features.

Aged↗
PubMedDate not supplied

Osteoinduction by recombinant human bone morphogenetic protein-2 in muscles of non-human primates.

Heterotopic osteoinduction in a muscle of a medium-sized, non-human primate (Japanese macaque monkey; Macaca fuscata) was investigated with recombinant human bone morphogenetic protein-2 (rhBMP-2) mixed with atelopeptide type I collagen as the carrier. Nine monkeys were divided into three groups of three: groups I (1.25 mg rhBMP-2), II (250 micrograms rhBMP-2) and III (50 micrograms rhBMP-2). Four weeks after implanting into the calf muscle pouch, the implant was examined radiographically and histologically. In one specimen of three in group I, marked radio-opaque shadow, massive chondrogenesis and partial osteogenesis were observed. In the other two specimens, only microscopic calcification signs were recognized. In groups II and III, no findings of heterotopic osteoinduction were radiographically observed; however, nuclei from muscle bundles reacted to rhBMP-2 and were large and round, as in muscle bundles near the site of osteogenesis in group I. A positive control study using rats was carried out in parallel. This was a dose-finding study, with the monkeys in group III acting as a sub-effective dose (placebo) control, and rats acting as an active control, or verum, to show that the techniques are sufficiently sensitive. Bone morphogenetic protein appears to osteoinduce less bony material in soft tissue in primates than in rats.

Animals↗
PubMedDate not supplied

Bone morphogenetic protein-2 and type IV collagen expression in psammoma body forming ovarian cancer.

Psammoma bodies (PBs), characterized as calco-spherules with concentric laminations, are common in serous tumors of the ovary. However, there is no agreements as to how the PBs are formed. Bone morphogenetic protein-2 (BMP-2) has recently been proposed to be involved in the calcification of tumor cells and recent electron microscopic studies demonstrated the presence of type IV collagen in PBs. Based on this evidence, we postulated a possibe role for BMP-2 and type IV collagen in the formation of PBs in ovarian cancer. We examined the expression of BMP-2 and typle IV collagen by immunohistochemistry and reverse transcription PCR (RT-PCR) in PBs-forming (NK-211) and -non-forming (SHIN-3, KF-1, A2780, KK-92, KOC-2S, SKOV-3, OMC-3, MN-1, EC, and KEN-3) ovarian cancer cell lines in vitro and in surgical specimens of serous adenocarcinoma (SA) with/without PBs and mucinous adenocarcinoma (MA) of the ovary. Cellular growth of cell lines was also evaluated by their doubling time in vitro. Transcripts for BMP-2 mRNA were detected by RT-PCR in all cell lines. By immunohistochemistry, BMP-2 protein expression was positive in 45% (5 out of 11) of cell lines. 36.4% (4 out of 11) were positive for type IV collagen. PBs-forming NK-211 was intensively positive for both BMP-2 and type IV collagen. In addition, NK-211 demonstrated extremely slow growth with a doubling time of 450 hours. In surgical specimens, BMP-2 vs. type IV collagen positivities in tumor cells were 100% (20 out of 20) vs. 40% (8 out of 20) in SA with PBs, 61.1% (11 out of 18) vs. 0% (0 out of 18) in SA without PBs and 75% (9 out of 12) vs. 0% (0 out of 12) in MA. In PBs themselves, 100% (20 out of 20) positivity for BMP-2 and 80% (16 out of 20) for type IV collagen was shown. These results raise the possibility that BMP-2 and type IV collagen-producing slow growing tumor cells form PBs in ovarian cancer.

Bone Morphogenetic Protein 2↗