p146 type II alveolar epithelial cell antigen is identical to aminopeptidase N
| Autor: | J. D. Funkhouser, S. D. Tangada, M. Jones, S. J. O, R. D. Peterson |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Pulmonary and Respiratory Medicine
Physiology medicine.drug_class Proteolysis Molecular Sequence Data CD13 Antigens Biology Kidney Monoclonal antibody Aminopeptidases Aminopeptidase Chromatography Affinity Epithelium Alveolar cells Antigen Affinity chromatography Sequence Homology Nucleic Acid Physiology (medical) medicine Animals Humans Amino Acid Sequence Lung medicine.diagnostic_test Protein primary structure Antibodies Monoclonal Cell Biology Antigens Differentiation Rats Pulmonary Alveoli medicine.anatomical_structure Biochemistry Electrophoresis Polyacrylamide Gel Pulmonary alveolus |
| Zdroj: | American Journal of Physiology-Lung Cellular and Molecular Physiology. 260:L274-L279 |
| ISSN: | 1522-1504 1040-0605 |
| DOI: | 10.1152/ajplung.1991.260.4.l274 |
| Popis: | A prominent membrane protein of rat type II alveolar cells, p146, was originally identified by one of many mouse monoclonal antibodies that were produced to rat lung cells in the course of a search for differentiation antigens that might prove useful in studying lung differentiation. We report here results from analysis of the primary structure of this molecule and, based on this knowledge, the elucidation of the function of the protein. Amino acid sequencing of the NH2-terminal portion of the p146 protein, plus partial sequencing of several peptides obtained by limited proteolysis, indicates it is identical to aminopeptidase N. Further, the immunoaffinity purified p146 protein has aminopeptidase N activity. The discussion includes references to other molecules such as CD 13 and CD 10 (CALLA) that were recognized as differentiation antigens and subsequently found to be peptidases. The possible biological implications of such a peptidase on the luminal surface of type II alveolar cells are also considered. |
| Databáze: | OpenAIRE |
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