GSP-37, a novel goldfish scale matrix protein: identification, localization and functional analysis

• DOI: 10.1039/c2fd20051a
• Publication Date: 2012-05-14T08:31:44Z
• Authors: Kousei Miyabe; Hiroki Tokunaga; Hirotoshi Endo; Hirotaka Inoue; Michio Suzuki; Naoaki Tsutsui; Naoki Yokoo; Toshihiro Kogure; Hiromichi Nagasawa
• Keywords: 0301 basic medicine; 03 medical and health sciences

A novel noncollagenous acidic protein was identified from the scales of goldfish (Carassius auratus), a freshwater teleost. Using an in vitro calcium phosphate crystallization assay, EDTA-soluble fraction these screened for inhibitory activity, and highly phosphorylated glycoprotein, named scale (GSP)-37, isolated through 5 HPLC purification steps. The cDNA GSP-37 has open reading frame encoding precursor protein, consisting signal peptide GSP-37, with 19 137 amino acid residues, respectively. C-terminal region contains RGD consensus sequence cell adhesion. Although native strongly inhibited crystallization, alkaline phosphatase treatment dramatically reduced its activity. Reverse transcription-PCR analysis revealed that is expressed only but not other calcified tissues, bones or pharyngeal teeth. In situ hybridization demonstrated GSP-37-expressing cells were localized central regions regenerating scales, where organic matrices actively synthesized stained either tartrate-resistant phosphatase, osteoblastic osteoclastic markers, Immunohistochemical analyses showed uppermost bony layer scale, which thought to correspond enamel enameloid vertebrate All data indicate deeply associated calcification fish scales.