Important note: Information in this article was accurate in 1992. The state of the art may have changed since the publication date.
ISOLATION AND BIOCHEMICAL CHARACTERIZATION OF A SERINE PROTEINASE INHIBITOR FROM A HTLV-1-TRANSFORMED ESTABLISHED HUMAN T LYMPHOCYTE LINE
Diss Abstr Int [B]; 52(5):2488 1991. Unique Identifier : AIDSLINE ICDB/92679483 Cearlock DM; Univ. of Illinois at Chicago, Health Sciences Center
Abstract:
Selected biochemical characteristics of a serine proteinase inhibitor produced by a human T-cell leukemia virus, type 1 (HTLV-1)-transformed human T-lymphocyte line were investigated. A total of 21 selected T, B, and non-T/non-B established human lymphocyte lines (17 T-cell lines, 3 B-cell lines and 2 non-T/non-B cell lines) were screened for antitrypsin activity. Of these, only two CD4-positive HTLV-1 transformed T-cell lines exhibited such activity. Significant detectable activity against a battery of enzymes including a number of serine proteinases (chymotrypsin, thrombin, plasmin, and kallikrein), a cysteine (thiol) proteinase (papain), and an aspartic (carboxyl) proteinase (pepsin) could not be demonstrated. Evidence for the active synthesis of trypsin inhibitory activity by both cell lines was obtained through several experimental approaches. The most convincing of these was the demonstration of trypsin inhibitory activity from endogenously radiolabeled cell culture supernatants as radioactive inhibitory bands in gelatin-containing polyacrylamide gels. The cell line C91/PL was selected for further studies investigating the biochemical characterization of the serine proteinase (trypsin) inhibitor. The trypsin inhibitor was isolated from cell culture supernatants, and the relative molecular mass of the purified molecule was estimated by the use of several chromatographic techniques to be approx 60 kD. Purity of the serine proteinase inhibitor after an isolation procedure involving anion exchange and affinity chromatography was evaluated. First, purified material appeared as a homogeneous band after electrophoresis in sodium dodecyl sulfate polyacrylamide gels. Second, specific antitrypsin activities were calculated to have increased by a factor of nearly 800-fold for samples of the purified material as compared to the starting material. Experiments were performed to evaluate the phosphorylation and glycosylation status of the trypsin inhibitor; no evidence of either could be demonstrated. This study investigated the biochemical properties of a serine proteinase inhibitor produced by CD4-positive HTLV-1-transformed human T lymphocytes. This inhibitor may plan an immunoregulatory role in the life cycle of T lymphocytes. (Full text available from University Microfilms International, Ann Arbor, MI, as Order No. AAD91-32102).
Keywords: Antigens, CD4/ANALYSIS *Cell Transformation, Viral Electrophoresis, Polyacrylamide Gel Human *HTLV-I Serine Proteinase Inhibitors/ANALYSIS/*ISOLATION & PURIF/ PHARMACOLOGY T-Lymphocytes/*CHEMISTRY THESIS 920630
M9261019
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Important note: Information in this article was accurate in 1992. The state of the art may have changed since the publication date.
