Napsin A, a member of the aspartic protease family, is abundantly expressed in normal lung and kidney tissue and is expressed in lung adenocarcinomas

• Published in: FEBS letters Vol. 462; no. 1; pp. 129 - 134
• Main Authors: Chuman, Yoshiko, Bergman, Ann-Charlotte, Ueno, Takayuki, Saito, Shin’ichi, Sakaguchi, Kazuyasu, Alaiya, Ayodele A., Franzén, Bo, Bergman, Tomas, Arnott, David, Auer, Gert, Appella, Ettore, Jörnvall, Hans, Linder, Stig
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 26.11.1999
• Subjects: Adenocarcinoma - enzymology; Amino Acid Sequence; Apoproteins - metabolism; Aspartic Acid Endopeptidases - biosynthesis; Aspartic Acid Endopeptidases - genetics; Aspartic protease; Cloning, Molecular; DNA, Complementary - analysis; Humans; Kidney - enzymology; Lung - enzymology; Lung adenocarcinoma; Lung Neoplasms - enzymology; Mass spectrometry; Medicin och hälsovetenskap; Molecular Sequence Data; Pulmonary Surfactant-Associated Proteins; Pulmonary Surfactants - metabolism; RNA, Messenger - biosynthesis; Tissue Distribution; Tumor diagnosis; Aspartic protease; Tumor diagnosis; Lung adenocarcinoma; Mass spectrometry
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(99)01493-3

A pair of 35 kDa polypeptides (TAO1/TAO2) are expressed in more than 90% of all primary lung adenocarcinomas but not in other major malignancies. Mass spectrometry of tryptic peptides showed that TAO1/TAO2 is identical to napsin A, a recently described member of the aspartic proteinase family. The site of processing of pronapsin A to the mature form was located. Napsin expression was detected in human lung adenocarcinoma tumors, compatible with the marker nature of TAO1/TAO2 in the diagnosis of primary lung adenocarcinoma. This is important since identification of markers which can distinguish primary lung adenocarcinomas from distant metastases is desirable. Northern blot analysis showed expression of napsin also in normal lung and kidney tissue, and in situ hybridization showed expression in type II alveolar cells of the lung. This protease is concluded to have a specific functional role in the normal alveolar epithelium and is a candidate protease for the proteolytic processing of surfactant precursors.