Linked Life Data

1703444

Source:http://linkedlifedata.com/resource/pubmed/id/1703444

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-3-6
pubmed:databankReference
pubmed:abstractText
A 1008 basepair (bp) cDNA clone encoding 335 amino acids followed by an inframe TGA translation termination codon and a 295-nucleotide 3' untranslated (UT) region has been isolated from a pig liver cDNA library. Based on the deduced amino acid and nucleotide sequence homology to a human cDNA (Kaumeyer, J.F., Polazzi, J.O. and Kotick, M.P. (1986) Nucleic Acids Res. 14, 7839-7850), the 5' amino terminus was found to code for alpha 1-microglobulin (alpha 1-M), a 183 amino acid protein belonging to the lipocalin protein superfamily (Pervaiz, S. and Brew, K. (1985) Science 228, 335-337). The 3' half encoded HI-30 which constitutes the Kunitz-type proteinase inhibitory (L-chain) domain of porcine inter-alpha-trypsin inhibitor (I alpha TI). In Northern blot hybridization, this cDNA identified two equally abundant mRNA species of approx. 1.3 kb and 1.6 kb in length. However, a 125 bp cDNA probe derived from the 3' UT region of the cDNA hybridized only to the 1.6 kb mRNA. The differences observed in the 3' UT region of these mRNAs suggest the utilization of alternative polyadenylation signals or presence of unprocessed nuclear RNA. Densitometric scanning of Northern blots indicated that alpha 1-M/HI-30 mRNA levels were higher (5-8-fold) in fetal and neonatal liver compared to that of primiparous pigs. In contrast, the RNA levels did not change significantly during pregnancy. Dot blot analysis of RNA indicated liver to be the major site of alpha 1-M/HI-30 mRNA expression with lower levels observed in the stomach. The results suggest that modulation of alpha 1-M/HI-30 gene expression could play a role during porcine growth. Increased I alpha TI L-chain mRNA levels may be particularly important in fetal and neonatal development when regulation of the inflammatory response and protection of macromolecules from proteolytic degradation is vital to survival and sustained growth.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
1088
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47-56
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1703444-Alpha-Globulins, pubmed-meshheading:1703444-Amino Acid Sequence, pubmed-meshheading:1703444-Animals, pubmed-meshheading:1703444-Base Sequence, pubmed-meshheading:1703444-Blotting, Northern, pubmed-meshheading:1703444-Cloning, Molecular, pubmed-meshheading:1703444-DNA, pubmed-meshheading:1703444-DNA, Viral, pubmed-meshheading:1703444-Female, pubmed-meshheading:1703444-Liver, pubmed-meshheading:1703444-Molecular Sequence Data, pubmed-meshheading:1703444-Nucleic Acid Hybridization, pubmed-meshheading:1703444-Pregnancy, pubmed-meshheading:1703444-Protease Inhibitors, pubmed-meshheading:1703444-RNA, pubmed-meshheading:1703444-RNA, Messenger, pubmed-meshheading:1703444-Restriction Mapping, pubmed-meshheading:1703444-Sequence Homology, Nucleic Acid, pubmed-meshheading:1703444-Serum Albumin, pubmed-meshheading:1703444-Swine
pubmed:year
1991
pubmed:articleTitle
Molecular cloning of porcine alpha 1-microglobulin/HI-30 reveals developmental and tissue-specific expression of two variant messenger ribonucleic acids.
pubmed:affiliation
Department of Dermatology, University of Michigan, Ann Arbor.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't