Cited by 83Bone Metabolism and DiseasesBone and Dental Protein StudiesBiosimilars and Bioanalytical Methods

Characterization of monomeric and homodimeric forms of osteoclastogenesis inhibitory factor.

Tomoyasu, Akihiro, Goto, Masaaki, Fujise, Nobuaki, Mochizuki, Shin-ichi, Yasuda, Hisataka, Morinaga, Tomonori, Tsuda, Eisuke, Higashio, Kanji·1998·Biochemical and Biophysical Research Communications

Abstract

Osteoclastogenesis inhibitory factor (OCIF) is present naturally as two molecular forms, a monomer and a homodimer. The two forms of recombinant human OCIF (rOCIF) produced by Chinese hamster ovary (CHO) cells were purified to homogeneity. Determination of the C-terminal amino-acid sequences of the two forms of rOCIF revealed that the monomeric rOCIF lacked several amino acids including Cys379, which is involved in the intermolecular disulfide bond, in its C-terminal region. The two forms of rOCIF were indistinguishable in stability, sialic acid content, and specific activity in inhibition of osteoclastogenesis. In contrast, the homodimeric rOCIF was stronger in heparin-binding ability than the monomeric rOCIF. The homodimeric rOCIF was significantly shorter in initial half-life and smaller in AUC value in rats than the monomeric rOCIF, but exerted more potent biological activity in reducing the calcium concentration in serum of rats than did the monomeric rOCIF.

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Crossref · 10.1006/bbrc.1998.8443

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Authors
Tomoyasu, A., Goto, M., Fujise, N., Mochizuki, S.-I., Yasuda, H., Morinaga, T., Tsuda, E., & Higashio, K.
Affiliations
Megmilk Snow Brand (Japan) (JP)
Corresponding author
Goto, Masaaki
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
1998-04
Volume
245
Issue
2
Pages
382-387
ISSN
0006-291X (ISSN-L)
OpenAlex
W2133418994
Cited by
83
References
33
Citations by year
2026: 1 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 3 · 2019: 3 · 2017: 1 · 2016: 2 · 2015: 1 · 2013: 2 · 2012: 2
FWCI
2.44
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
  • Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
  • Life Sciences › Immunology and Microbiology › Immunology › Biosimilars and Bioanalytical Methods
Keywords
osteoprotegerin, homodimer, monomers, recombinant protein, C-terminal sequence, disulfide bonds, sialic acid, heparin binding, protein stability, serum calcium, osteoclastogenesis inhibition, pharmacokinetics
MeSH terms
Amino Acid Sequence, Animals, Calcium, Disulfides, Glycoproteins, Cricetinae, Heparin, Humans, Molecular Sequence Data, Protein Binding, Recombinant Proteins, CHO Cells, Sequence Analysis, Receptors, Tumor Necrosis Factor, Receptors, Cytoplasmic and Nuclear, N-Acetylneuraminic Acid, Dimerization, Osteoprotegerin

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