We describe a cell surface protein that is abundant in liver and has close structural and biochemical similarities to the low density lipoprotein (LDL) receptor. The complete sequence of the protein containing 4544 amino acids is presented. From the sequence a remarkable resemblance to the LDL‐receptor and epidermal growth factor (EGF) precursor is apparent. Three types of repeating sequence motifs entirely account for the extracellular domain of the molecule. These are arranged in a manner resembling four copies of the ligand binding and the EGF‐precursor homologous region of the LDL‐receptor. Following a proline‐rich segment of 17 amino acids are found six consecutive repeats with close homology to EGF. A single membrane‐spanning segment precedes a carboxy‐terminal ‘tail’ of 100 amino acids. This contains two seven‐amino acid sequences with striking homology to the cytoplasmic tail of the LDL‐receptor in the region that contains the signal for clustering into coated pits. The mRNA for this protein is most abundant in liver, brain and lung. By using an antibody raised against a 13‐amino acid peptide corresponding to the deduced amino acid sequence of the carboxy‐terminus of the protein we have demonstrated its existence on the cell surface and its abundance in liver. Like the LDL‐receptor this protein also strongly binds calcium, a cation absolutely required for binding of apolipoproteins B and E to their receptors. We propose that this LDL‐receptor related protein (LRP) is a recycling lipoprotein receptor with possible growth‐modulating effects.

The genotyping of 13 sires and 250 of their sons for casein polymorphisms revealed 10 different haplotypes for Norwegian Cattle. Associations between haplotypes and yields of protein, milk, and fat were studied using a granddaughter design. Three subsets of data containing families with haplotypes 1, 5, and 10 were analyzed independently and denoted by analyses 1, 5, and 10, respectively. In addition, all sire families of all haplotypes were pooled and analyzed in analysis T. No associations were found between haplotypes and traits for milk yield in analyses 1, 10, and T. However, the null hypothesis of an equal effect within sire of bulls was rejected in analysis 5 for yields of protein and milk. The increase in protein yield associated with haplotype 5 ranged from 2.52 to 14.58 kg (from .09 to .51 phenotypic standard deviations). These results may indicate the presence of at least one quantitative trait locus in the region of the casein genes that affects protein yield of Norwegian Cattle. The findings were confirmed with a new analysis of two large sire families segregating haplotype 5 (analysis 5N).

The polymeric immunoglobulin receptor (transmembrane secretory component) mediates transcellular transport of dimeric immunoglobulin A (IgA) and pentameric IgM in glandular and mucosal epithelial cells. cDNAs encoding two forms of the bovine polymeric immunoglobulin receptor (pIgR) have been cloned and sequenced. The long form contains 3,527 bp and predicts a single open reading frame of 2,271 bp encoding a protein of 757 bp. The extracellular part contains five immunoglobulin (Ig)-like domains. The shorter form lacks the region from residues 458-1,111 corresponding to Ig-like domains 2 and 3. In Northern blot analysis of various bovine tissues, only the long form of pIgR mRNA was detected. By using the reverse transcription-polymerase chain reaction (RT-PCR), both forms were detected. An alignment of the cytoplasmic tail of the pIgR from bovine, human, rabbit, and rat revealed highly conserved areas that may reflect the importance of these regions for intracellular sorting of the receptor.

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