Identification of a calcium-dependent microsomal proteinase responsible for monobasic cleavage of chicken proalbumin
The location and nature of the endoproteolytic activity involved in processing of proproteins has been studied in chicken liver microsomes. A membrane-bound, calcium-dependent proteinase was found to cleave chicken proalbumin with a monobasic cleavage site approx. 10-times faster than human proalbum...
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| Published in | Biochimica et biophysica acta Vol. 990; no. 3; pp. 276 - 279 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Amsterdam
Elsevier B.V
24.03.1989
Elsevier North-Holland |
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| Abstract | The location and nature of the endoproteolytic activity involved in processing of proproteins has been studied in chicken liver microsomes. A membrane-bound, calcium-dependent proteinase was found to cleave chicken proalbumin with a monobasic cleavage site approx. 10-times faster than human proalbumin, which has a dibasic cleavage site. The mutant (human) proalbumin Christchurch (Arg(−1) → Gln), with a potential monobasic site, was not processed. The enzyme, which had a pH optimum of between 5.0 and 7.0, was not inhibited by serine or aspartyl proteinase inhibitors but was affected by some inhibitors of cysteine proteinases. The convertase was specifically inhibited by the reactive centre variant
α
1-antitrypsin Pittsburgh, but not by normal
α
1-antitrypsin. |
|---|---|
| AbstractList | The location and nature of the endoproteolytic activity involved in processing of proproteins has been studied in chicken liver microsomes. A membrane-bound, calcium-dependent proteinase was found to cleave chicken proalbumin with a monobasic cleavage site approx. 10-times faster than human proalbumin, which has a dibasic cleavage site. The mutant (human) proalbumin Christchurch (Arg(-1)---Gln), with a potential monobasic site, was not processed. The enzyme, which had a pH optimum of between 5.0 and 7.0, was not inhibited by serine or aspartyl proteinase inhibitors but was affected by some inhibitors of cysteine proteinases. The convertase was specifically inhibited by the reactive centre variant alpha 1-antitrypsin Pittsburgh, but not by normal alpha 1-antitrypsin. The location and nature of the endoproteolytic activity involved in processing of proproteins has been studied in chicken liver microsomes. A membrane-bound, calcium-dependent proteinase was found to cleave chicken proalbumin with a monobasic cleavage site approx. 10-times faster than human proalbumin, which has a dibasic cleavage site. The mutant (human) proalbumin Christchurch (Arg(−1) → Gln), with a potential monobasic site, was not processed. The enzyme, which had a pH optimum of between 5.0 and 7.0, was not inhibited by serine or aspartyl proteinase inhibitors but was affected by some inhibitors of cysteine proteinases. The convertase was specifically inhibited by the reactive centre variant α 1-antitrypsin Pittsburgh, but not by normal α 1-antitrypsin. The location and nature of the endoproteolytic activity involved in processing of proproteins has been studied in chicken liver microsomes. A membrane-bound, calcium-dependent proteinase was found to cleave chicken proalbumin with a monobasic cleavage site approx. 10-times faster than human proalbumin, which has a dibasic cleavage site. The mutant (human) proalbumin Christchurch (Arg(-1)---Gln), with a potential monobasic site, was not processed. The enzyme, which had a pH optimum of between 5.0 and 7.0, was not inhibited by serine or aspartyl proteinase inhibitors but was affected by some inhibitors of cysteine proteinases. The convertase was specifically inhibited by the reactive centre variant alpha 1-antitrypsin Pittsburgh, but not by normal alpha 1-antitrypsin.The location and nature of the endoproteolytic activity involved in processing of proproteins has been studied in chicken liver microsomes. A membrane-bound, calcium-dependent proteinase was found to cleave chicken proalbumin with a monobasic cleavage site approx. 10-times faster than human proalbumin, which has a dibasic cleavage site. The mutant (human) proalbumin Christchurch (Arg(-1)---Gln), with a potential monobasic site, was not processed. The enzyme, which had a pH optimum of between 5.0 and 7.0, was not inhibited by serine or aspartyl proteinase inhibitors but was affected by some inhibitors of cysteine proteinases. The convertase was specifically inhibited by the reactive centre variant alpha 1-antitrypsin Pittsburgh, but not by normal alpha 1-antitrypsin. |
| Author | Peach, Robert J. Brennan, Stephen O. |
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| Cites_doi | 10.1146/annurev.bi.53.070184.003313 10.1016/S0021-9258(18)32659-0 10.1016/0167-4838(86)90183-4 10.1016/S0021-9258(17)39719-3 10.1016/0092-8674(86)90319-3 10.1016/0005-2795(80)90064-1 10.1146/annurev.ph.44.030182.003205 10.1126/science.3541206 10.1042/bj2460279 10.1016/S0006-291X(87)80036-0 10.1056/NEJM198309223091203 10.1093/oxfordjournals.bmb.a071161 10.1016/0304-4165(84)90029-1 10.1016/0006-291X(77)90528-9 10.1042/bj2440457 10.1002/j.1460-2075.1985.tb02333.x 10.3109/00365517209102747 10.1016/0092-8674(84)90354-4 10.1016/0014-5793(88)80819-6 |
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| Keywords | Liver microsome Proalbumin Christchurch α 1-Antitrypsin Pittsburgh Proalbumin processing Yeast PMSF TLCK Chicken KEX2 proteinase PCMB Human Enzyme Cleavage site Liver Proteinase Albumin Microsome Ripening Autoradiography Vertebrata Electrophoretic mobility Aves |
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| References | Rosen, Geller (bib14) 1977; 78 Brennan, Carrell (bib13) 1986; 873 Johansson (bib16) 1972; 29 Loh, Tam, Russell (bib17) 1984; 259 Douglass, Civelli, Herbert (bib2) 1984; 53 Brennan, Carrell (bib12) 1980; 621 Mizuno, Nakamura, Takada, Sakakibara, Matsuo (bib4) 1987; 144 Hache, Wiskocil, Vasa, Roy, Lau, Deeley (bib10) 1983; 258 Achstetter, Wolf (bib18) 1985; 4 Davidson, Peshavaria, Hutton (bib21) 1987; 246 Docherty, Steiner (bib1) 1982; 44 Russell, Geller (bib8) 1975; 70 Brennan, Peach (bib6) 1988; 229 Owen, Brennan, Lewis, Carrell (bib11) 1983; 309 Bentley, Rees, Rizza, Brownlee (bib19) 1986; 45 Hutton, Davidson, Peshavaria (bib20) 1987; 244 Bostian, Elliot, Bussey, Burn, Smith, Tipper (bib5) 1984; 36 Brennan, Owen, Boswell, Lewis, Carrell (bib9) 1984; 802 Fuller, Brake, Thorner (bib3) 1986 Bathurst, Brennan, Carrell, Cousens, Brake, Barr (bib7) 1987; 235 Hunter (bib15) 1974; 30 Owen (10.1016/S0304-4165(89)80045-5_bib11) 1983; 309 Bentley (10.1016/S0304-4165(89)80045-5_bib19) 1986; 45 Hache (10.1016/S0304-4165(89)80045-5_bib10) 1983; 258 Brennan (10.1016/S0304-4165(89)80045-5_bib6) 1988; 229 Russell (10.1016/S0304-4165(89)80045-5_bib8) 1975; 70 Douglass (10.1016/S0304-4165(89)80045-5_bib2) 1984; 53 Hunter (10.1016/S0304-4165(89)80045-5_bib15) 1974; 30 Docherty (10.1016/S0304-4165(89)80045-5_bib1) 1982; 44 Bathurst (10.1016/S0304-4165(89)80045-5_bib7) 1987; 235 Rosen (10.1016/S0304-4165(89)80045-5_bib14) 1977; 78 Hutton (10.1016/S0304-4165(89)80045-5_bib20) 1987; 244 Achstetter (10.1016/S0304-4165(89)80045-5_bib18) 1985; 4 Johansson (10.1016/S0304-4165(89)80045-5_bib16) 1972; 29 Davidson (10.1016/S0304-4165(89)80045-5_bib21) 1987; 246 Brennan (10.1016/S0304-4165(89)80045-5_bib12) 1980; 621 Brennan (10.1016/S0304-4165(89)80045-5_bib9) 1984; 802 Mizuno (10.1016/S0304-4165(89)80045-5_bib4) 1987; 144 Loh (10.1016/S0304-4165(89)80045-5_bib17) 1984; 259 Bostian (10.1016/S0304-4165(89)80045-5_bib5) 1984; 36 Fuller (10.1016/S0304-4165(89)80045-5_bib3) 1986 Brennan (10.1016/S0304-4165(89)80045-5_bib13) 1986; 873 |
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| SubjectTerms | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Calcium - physiology Chicken Chickens Child Endopeptidases - physiology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humans Hydrogen-Ion Concentration Hydrolases Hydrolysis KEX2 proteinase Liver microsome Microsomes, Liver - enzymology Molecular Sequence Data Prealbumin - isolation & purification Prealbumin - metabolism Proalbumin Christchurch Proalbumin processing Serum Albumin - isolation & purification Yeast α1-Antitrypsin Pittsburgh |
| Title | Identification of a calcium-dependent microsomal proteinase responsible for monobasic cleavage of chicken proalbumin |
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