Fluorescent Antibody Studies of Alpha-1-Antitrypsin in Adult Human Lung

Abstract

The histologic distribution of alpha-1-antitrypsin in frozen sections prepared from four specimens of human lung was determined by the indirect fluorescent antibody technic. Three of the specimens were obtained directly from surgical procedures and were peripheral tissue excised with tumors. The tumors were a mixed-cell "scar cancer" (Case 1), a bronchiolar carcinoma (Case 2), and a benign hemartoma (Case 3). The fourth specimen (Case 4) was obtained at autopsy following death by myocardial infarction. Specific fluorescence for alpha-1-antitrypsin was observed lining the terminal airways and alveoli throughout the sections from Cases 1 and 4. In specimens from Cases 2 and 3, a few focal areas of specific fluorescence were observed. The results of this study suggest that alpha-1-antitrypsin may be distributed in lung in variable concentration in association with pulmonary surfactant.

An evaluation of the prognostic significance of alpha-1-antitrypsin expression in adenocarcinomas of the lung: an immunohistochemical analysis

“…Since AAT can inactivate a wide variety of proteolytic enzymes such as pancreatic and leukocyte elastase, trypsin, chymotrypsin, collagenase, plasmin and thrombin, it is considered to be important in regulating a variety of proteolytic and thromboplastic processes on both systemic and local levels (Rimon et al, 1966;Eisen et al, 1970;Koj et al, 1972;Beatty et al, 1980). AAT is expressed not only in normal livers but also in other normal tissues such as the lung, gall bladder, pancreas, and the gastrointestinal tract (Tuttle & Jones, 1975;Ray et al, 1978;Kittas et al, 1982a;Geboes et al, 1982;Tahara et al, 1984;Aroni et al, 1984). Moreover, AAT has also been demonstrated in several neoplasms including carcinomas, mesenchymal tumours, hemopoietic and brain tumours (Reintoft & Hargerstrand, 1979;Kittas et al, 1982b;Glasgow et al, 1982;Aroni et al, 1984;Tahara et al, 1984;Krugliak et al, 1986;Wittekind et al, 1986;Sawaya et al, 1987;Soini & Miettinen, 1989;Kataoka et al, 1989;Perlmutter et al, 1989;Karashima et al, 1990).…”

Molecular evolution of serpins: homologous structure of the human .alpha.1-antichymotrypsin and .alpha.1-antitrypsin genes

“…Its target substrates include neutrophile cathepsin G, mast cell chymase, and proteases that convert angiotensin I to the biologically active vasoconstrictor angiotensin II in vitro (Reilly et al, 1982;Wintroub et al, 1981;Tonnensen et al, 1982). It is a glycoprotein of 68000 daltons and is structurally related to arantitrypsin (AAT) (Morii & Travis, 1983a,b), which is a specific inhibitor of neutrophile elastase and protects the lung elastin fibers from degradation by this protease (Olsen et al, 1975; Tuttle & Jones, 1975). The physiological function of ACT has not been clearly defined.…”

Elastosis in lung carcinoma: Immunohistochemical, ultrastructural and clinical studies

“…Our results also showed that the cytoplasms of some tumor cells were slightly to markedly positive for α‐1‐antitrypsin in all cases except for small‐cell carcinoma. Although it has been reported that the presence of α‐1‐antitrypsin in tumor cells was due to its production by tumor cells themselves, 29–35 it is suggested that α‐1‐antitrypsin in elastosis may be mainly from plasma, because it is well known that plasma contains a large amount of α‐1‐antitrypsin. 36…”