새로운 프롤린 풍부 단백질의 동정 및 특성 연구 (Identification and Characterization of Novel Proline Rich Proteins)

서지정보

· 발행기관 : 대한구강악안면병리학회
· 수록지 정보 : 대한구강악안면병리학회지 / 34권 / 6호 / 339 ~ 346페이지
· 저자명 : 김연숙

초록

In the previous molecular cloning study from human salivary gland cDNA library novel clones (C75‐014, C76‐022) were known as candidate genes for proline rich proteins by GenBank data base search and RNA in situ hybridization. C75‐014and C76‐022 genes were characterized as those expressing excretory basic proteins primarily composed of alanine, proline, and leucine residues, mimicking basic proline‐rich proteins (bPRPs) with helical structures and multiple consensus sequences of phosphorylation sites. In the immunohistochemical stainings using polyclonal antisera against each C75‐014and C76‐022 peptide showed strong reaction in the secretory granules of striated and excretory ducts. And in Western blot for the different salivary specimens relatively distinctive bands appeared at lower molecular weight, ranging about 15‐50 kDa. This study was aimed to identify the molecular characteristics of C75‐014 and C76‐022 proteins, which showed properties of basic proline rich protein. These data suggest that C75‐014 and C76‐022 are candidate genes for proline rich proteins in human salivary gland, which may play a role for protecting and stabilizing the mucosal epithelium against numerous proteolytic damages and stresses.

영어초록

In the previous molecular cloning study from human salivary gland cDNA library novel clones (C75‐014, C76‐022) were known as candidate genes for proline rich proteins by GenBank data base search and RNA in situ hybridization. C75‐014and C76‐022 genes were characterized as those expressing excretory basic proteins primarily composed of alanine, proline, and leucine residues, mimicking basic proline‐rich proteins (bPRPs) with helical structures and multiple consensus sequences of phosphorylation sites. In the immunohistochemical stainings using polyclonal antisera against each C75‐014and C76‐022 peptide showed strong reaction in the secretory granules of striated and excretory ducts. And in Western blot for the different salivary specimens relatively distinctive bands appeared at lower molecular weight, ranging about 15‐50 kDa. This study was aimed to identify the molecular characteristics of C75‐014 and C76‐022 proteins, which showed properties of basic proline rich protein. These data suggest that C75‐014 and C76‐022 are candidate genes for proline rich proteins in human salivary gland, which may play a role for protecting and stabilizing the mucosal epithelium against numerous proteolytic damages and stresses.

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