Biomedical subjects

L G Hennighausen

Publications and source records attributed to L G Hennighausen.

5 recordsLinked to original sources

PubMed1984

Comparison of the whey acidic protein genes of the rat and mouse.

Whey acidic protein (WAP), a hormonally-regulated 14,000 dalton cysteine-rich protein, is the principal whey protein found in rodent milk. Genomic clones encompassing both the 2.8 Kb rat and 3.3 Kb mouse WAP genes have been characterized. The genes consist of four exons and three introns. The middle two exons encode the two cysteine-rich regions which probably form separate protein domains. Homology in the 5' flanking DNA of the mouse and rat extends at least 325 bp upstream of the putative CAP site, including a precisely conserved stretch of 50 bp around the unusual TATA and CAAT sites. The homology previously observed between the 3' noncoding sequences of the rat and mouse mRNAs extends at least 20 bp into the 3' flanking region. Several potential glucocorticoid receptor binding sites have been found in the 5' flanking region of the WAP gene. The conservation of the 5' flanking region of the WAP genes may be related to regulation of expression of WAP by peptide and/or steroid hormones.

Amino Acid Sequence↗

PubMed1982

Nucleotide sequence of cloned cDNA coding for mouse epsilon casein.

We isolated cDNA clones, which correspond to the mRNA coding for the smallest of the seven mouse caseins. From the nucleotide sequence of the cDNA we deduced the amino acid sequence of the protein, which we named epsilon casein. Mouse epsilon casein and cow alpha s2 casein show amino acid sequence homologies in the N-terminal region of the mature protein. The signal peptide of mouse epsilon casein shows in length and sequence remarkable homology to the signal peptides of the calcium-precipitable caseins of other species. In accordance with this group of caseins mouse epsilon casein contains in the sequence -Ser-Ser-Glu-Glu- a site for potential multiple phosphorylation.

Animals↗

PubMed1982

Comparative sequence analysis of the mRNAs coding for mouse and rat whey protein.

Whey acidic protein (WAP) is a major milk protein found in mouse and rat. Cloned WAP cDNAs from both species have been sequenced and the respective protein sequences have been deduced. Mouse and rat WAP (134 and 137 amino acids respectively) are acidic, cysteine rich proteins which contain a N-terminal signal peptide of 19 amino acids. Most of the cysteines are located in two clusters containing six cysteine residues each, arranged in an identical pattern. Comparison of the mouse and rat WAPs show that the signal peptide and the first cysteine domain are conserved to a greater extent than the rest of the protein. This result is reflected in the nucleotide sequence homology, where the regions coding for the signal peptide and cysteine domain I are the only regions where the rate of replacement substitution is lower than the rate of silent substitution. The 3' non-coding regions show a 91% conservation which is half the substitution rate for the coding region. This low rate of sequence divergence in the 3' non-translated region of the mRNA may indicate a functional importance for this region.

Amino Acid Sequence↗

PubMed1982

Characterization and cloning of the mRNAs specific for the lactating mouse mammary gland.

We have characterized and cloned the lactation-specific mRNAs of mouse mammary glands. The group of eight milk-protein-specific mRNAs were identified (a) by size and antigenic properties of their translation products in vitro and (b) by characterization of their respective cDNA clones. Two alpha-caseins (43 kDa and 39 kDa) are encoded by mRNAs of 1600 nucleotides and two beta-caseins (26 kDa) are encoded by mRNAs of 1450 nucleotides in length. Three smaller caseins, gamma-casein (23.7 kDa), delta-casein (21 kDa) and epsilon-casein (14.5 kDa) are synthesized by mRNAs of 880, 1150 and 860 nucleotides. Beside these casein mRNAs a mammary specific 620 nucleotide mRNA codes for a novel acidic whey protein (13.7 kDa). cDNA clones corresponding to the mRNAs for the lactation-specific proteins have been isolated from a mammary-specific cDNA library. Cloned alpha-casein cDNA hybridizes to both alpha-casein specific mRNAs and cloned beta-casein cDNAs hybridize with both beta-casein specific mRNAs. By RNA blot analysis we show that the cloned cDNAs for mouse alpha-casein, beta-casein, gamma-casein and epsilon-casein and the acidic whey protein cross-hybridize with mRNAs of the rat, demonstrating partial sequence homology between the corresponding mRNAs of those species.

Animals↗

PubMed1982

Mouse whey acidic protein is a novel member of the family of 'four-disulfide core' proteins.

Unlike in other mammalian species, the major whey protein in mouse is not alpha-lactalbumin, but a cysteine rich, acidic protein with a molecular weight of 14.0 kDa. We have deduced the amino acid sequence of this mouse acidic of whey protein from the nucleotide sequence of cloned cDNA. The positions of the half cysteines suggest that mouse whey acidic protein (WAP) is a two domain protein, very similar in structure to the plant lectin wheat germ agglutinin and the hypothalamic carrier protein neurophysin.

Amino Acid Sequence↗