α 1-Antitrypsin and serum albumin mRNA accumulation in normal, acute phase and ZZ human liver
α 1-Antitrypsin and albumin mRNA levels of 4 human livers were assessed using a newly sequenced cDNA clone of the carboxyterminal third of α 1-antitrypsin and a previously cloned albumin cDNA sequence. The relative concentration of α 1-antitrypsin mRNA was the same in poly(A)-containing RNA isolated...
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| Published in | FEBS letters Vol. 189; no. 2; pp. 361 - 366 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Elsevier B.V
23.09.1985
|
| Subjects | |
| Online Access | Get full text |
| ISSN | 0014-5793 1873-3468 |
| DOI | 10.1016/0014-5793(85)81056-5 |
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| Abstract | α
1-Antitrypsin and albumin mRNA levels of 4 human livers were assessed using a newly sequenced cDNA clone of the carboxyterminal third of α
1-antitrypsin and a previously cloned albumin cDNA sequence. The relative concentration of α
1-antitrypsin mRNA was the same in poly(A)-containing RNA isolated from acute phase (MM) and α
1-antitrypsin deficient (ZZ) individuals. In the acute phase liver relative to the normal (MM) liver, total RNA extracts showed a marked decrease in albumin mRNA concentration but no increase in α
1-antitrypsin mRNA. The ZZ liver showed decreased total and poly(A)-containing RNA content but the same proportion of α-antitrypsin to albumin mRNA as in the normal (MM) liver. This supports other evidence that ZZ α
1-antitrypsin deficiency is due to a defect in polypeptide processing (secretion) rather than a deficiency in mRNA accumulation. |
|---|---|
| AbstractList | α
1
‐Antitrypsin and albumin mRNA levels of 4 human livers were assessed using a newly sequenced cDNA clone of the carboxyterminal third of α
1
‐antitrypsin and a previously cloned albumin cDNA sequence. The relative concentration of α
1
‐antitrypsin mRNA was the same in poly(A)‐containing RNA isolated from acute phase (MM) and α
1
‐antitrypsin deficient (ZZ) individuals. In the acute phase liver relative to the normal (MM) liver, total RNA extracts showed a marked decrease in albumin mRNA concentration but no increase in α
1
‐antitrypsin mRNA. The ZZ liver showed decreased total and poly(A)‐containing RNA content but the same proportion of α‐antitrypsin to albumin mRNA as in the normal (MM) liver. This supports other evidence that ZZ α
1
‐antitrypsin deficiency is due to a defect in polypeptide processing (secretion) rather than a deficiency in mRNA accumulation. Alpha 1-Antitrypsin and albumin mRNA levels of 4 human livers were assessed using a newly sequenced cDNA clone of the carboxyterminal third of alpha 1-antitrypsin and a previously cloned albumin cDNA sequence. The relative concentration of alpha 1-antitrypsin mRNA was the same in poly(A)-containing RNA isolated from acute phase (MM) and alpha1-antitrypsin deficient (ZZ) individuals. In the acute phase liver relative to the normal (MM) liver, total RNA extracts showed a marked decrease in albumin mRNA concentration but no increase in alpha 1-antitrypsin mRNA. The ZZ liver showed decreased total and poly(A)-containing RNA content but the same proportion of alpha 1-antitrypsin to albumin mRNA as in the normal (MM) liver. This supports other evidence that ZZ alpha 1-antitrypsin deficiency is due to a defect in polypeptide processing (secretion) rather than a deficiency in mRNA accumulation.Alpha 1-Antitrypsin and albumin mRNA levels of 4 human livers were assessed using a newly sequenced cDNA clone of the carboxyterminal third of alpha 1-antitrypsin and a previously cloned albumin cDNA sequence. The relative concentration of alpha 1-antitrypsin mRNA was the same in poly(A)-containing RNA isolated from acute phase (MM) and alpha1-antitrypsin deficient (ZZ) individuals. In the acute phase liver relative to the normal (MM) liver, total RNA extracts showed a marked decrease in albumin mRNA concentration but no increase in alpha 1-antitrypsin mRNA. The ZZ liver showed decreased total and poly(A)-containing RNA content but the same proportion of alpha 1-antitrypsin to albumin mRNA as in the normal (MM) liver. This supports other evidence that ZZ alpha 1-antitrypsin deficiency is due to a defect in polypeptide processing (secretion) rather than a deficiency in mRNA accumulation. Alpha 1-Antitrypsin and albumin mRNA levels of 4 human livers were assessed using a newly sequenced cDNA clone of the carboxyterminal third of alpha 1-antitrypsin and a previously cloned albumin cDNA sequence. The relative concentration of alpha 1-antitrypsin mRNA was the same in poly(A)-containing RNA isolated from acute phase (MM) and alpha1-antitrypsin deficient (ZZ) individuals. In the acute phase liver relative to the normal (MM) liver, total RNA extracts showed a marked decrease in albumin mRNA concentration but no increase in alpha 1-antitrypsin mRNA. The ZZ liver showed decreased total and poly(A)-containing RNA content but the same proportion of alpha 1-antitrypsin to albumin mRNA as in the normal (MM) liver. This supports other evidence that ZZ alpha 1-antitrypsin deficiency is due to a defect in polypeptide processing (secretion) rather than a deficiency in mRNA accumulation. α 1-Antitrypsin and albumin mRNA levels of 4 human livers were assessed using a newly sequenced cDNA clone of the carboxyterminal third of α 1-antitrypsin and a previously cloned albumin cDNA sequence. The relative concentration of α 1-antitrypsin mRNA was the same in poly(A)-containing RNA isolated from acute phase (MM) and α 1-antitrypsin deficient (ZZ) individuals. In the acute phase liver relative to the normal (MM) liver, total RNA extracts showed a marked decrease in albumin mRNA concentration but no increase in α 1-antitrypsin mRNA. The ZZ liver showed decreased total and poly(A)-containing RNA content but the same proportion of α-antitrypsin to albumin mRNA as in the normal (MM) liver. This supports other evidence that ZZ α 1-antitrypsin deficiency is due to a defect in polypeptide processing (secretion) rather than a deficiency in mRNA accumulation. |
| Author | Carrell, R.W. Edbrooke, M.R. Craig, R.K. Bathurst, I.C. Riley, J.H. |
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| Cites_doi | 10.1073/pnas.80.19.5951 10.1038/312077a0 10.1021/bi00316a003 10.1016/0014-5793(85)80798-5 10.1073/pnas.78.8.4718 10.1111/j.1432-1033.1984.tb07954.x 10.1016/0006-291X(83)90532-6 10.1042/bj1990725 10.1042/bj2190223 10.1016/0014-5793(83)80622-X 10.1042/bj1940989 10.1016/S0076-6879(80)65059-9 10.1016/0014-5793(84)80211-2 10.1016/0307-4412(85)90175-X 10.1016/S0021-9258(18)34015-8 10.1042/bj1600057 10.1016/0014-5793(82)81247-7 10.1007/978-1-4684-2676-2_4 10.1016/S0021-9258(18)70943-5 10.1056/NEJM198103053041001 10.1016/0006-291X(81)90513-1 10.1111/j.0954-6820.1978.tb08452.x |
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| Keywords | Z human α 1-antitrypsin Acute phase protein Liver mRNA cDNA sequence α 1-antitrypsin |
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| Snippet | α
1-Antitrypsin and albumin mRNA levels of 4 human livers were assessed using a newly sequenced cDNA clone of the carboxyterminal third of α
1-antitrypsin and... α 1 ‐Antitrypsin and albumin mRNA levels of 4 human livers were assessed using a newly sequenced cDNA clone of the carboxyterminal third of α 1 ‐antitrypsin... Alpha 1-Antitrypsin and albumin mRNA levels of 4 human livers were assessed using a newly sequenced cDNA clone of the carboxyterminal third of alpha... |
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| SubjectTerms | Acute phase protein Adolescent Adult alpha 1-Antitrypsin - genetics Amino Acid Sequence Base Sequence C-Reactive Protein - analysis cDNA sequence α 1-antitrypsin DNA - metabolism Female Humans Liver - metabolism Liver mRNA Male Middle Aged RNA, Messenger - metabolism Serum Albumin - genetics Time Factors Z human α 1-antitrypsin |
| Title | α 1-Antitrypsin and serum albumin mRNA accumulation in normal, acute phase and ZZ human liver |
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