High impact information on GLYCAM1

• Substrate specificity, immunoblotting with type-specific antisera, and the amino acid sequences of peptides derived from PP3 indicate that PP3 is not an isoform of any known serine/threonine protein phosphatase [1].
• This procedure applied to the bovine milk PP3 protein containing 25% modifications by weight yielded all known modifications (five phosphorylations, two O- and one N-glycosylation) as well as the previously unreported NeuNAc-Hex-[NeuNAc]HexNAc group O-linked to Ser60 [2].
• Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage [2].
• An experimental in vivo induction model for lactation, developed by Kann et al., showed that the expression of GLYCAM1 is hormonally regulated in the mammary gland of ewes [3].
• GLYCAM1, a member of the glycoprotein mucin family, is a component of the milk fat globule membrane (MFGM) [3].

Biological context of GLYCAM1

• Bovine retroposons of the short interspersed nuclear element sequence class (SINES) and one microsatellite were localized in the PP3 gene [4].
• A genomic 4.5-kb clone has been sequenced comprising a 2.9-kb PP3 transcriptional unit plus 1 kb of 5' and 0.6 kb of 3' flanking sequence [4].
• The N-terminal amino acid sequence showed no homology to any known protein sequence, but the amino acid composition indicated that the 28 kDa protein is identical with the PP3 component from the proteose peptone fraction of bovine milk, or part of it [5].
• Phosphorylation, glycosylation and amino acid sequence of component PP3 from the proteose peptone fraction of bovine milk [6].
• A full length PP3 (Proteose-Peptone component 3) cDNA of 679 bp was isolated from a bovine mammary gland cDNA library [7].

Anatomical context of GLYCAM1

• Immunostimulation effects of proteose-peptone component 3 fragment on human hybridomas and peripheral blood lymphocytes [8].
• PP3 was found to be expressed in mammary gland but not in peripheral lymph nodes, Peyer's pathes, lung, spleen, heart, and muscle [7].

Associations of GLYCAM1 with chemical compounds

• Finally, the immunoreactive proteins from caprine and ovine milks were purified and characterized as PP3 analogues by amino acid analysis and N-terminal sequence analysis [9].
• Role of the O-phosphoserine clusters in the interaction of the bovine milk alpha s1-, beta-, kappa-caseins and the PP3 component with immobilized iron (III) ions [10].
• alpha s1- and beta-Caseins have a sequence cluster -Ser(P)-Ser(P)-Ser(P)-Glu-Glu- which is not present in kappa-casein and the whey PP3 component [10].
• The study of the affinity of a few free amino acids towards iron(III)-IDA showed that the secondary site involved tryptophan and tyrosine residues for alpha s1- and beta-caseins, histidine residues for PP3 and cysteine residues for kappa-casein [10].

Other interactions of GLYCAM1

• Rapid communication: detection and mapping of polymorphisms in the bovine Lactoperoxidase (LPO) gene and in the Glycosylation-dependent cell adhesion molecule 1 (GlyCAM1) gene using fluorescent single-strand conformation polymorphism analysis [11].

Analytical, diagnostic and therapeutic context of GLYCAM1

• The heat-stable acid-soluble phosphoglycoprotein component PP3 was isolated from the bovine milk proteose peptone fraction by concanavalin A affinity chromatography [12].
• Glycopeptides from the ConA-bound fraction corresponding to the component PP3 were obtained by Pronase digestion and were separated by gel filtration into high and low-molecular-mass glycopeptides [13].
• The conformation of the synthetic peptide corresponding to the C-terminal f 119-135 part of bovine component PP3 was analyzed by circular dichroism experiments using various media [14].
• Western blot analysis with anti-bovine PP3 immunoglobulins was used to analyze caprine, ovine, and human milks, and immunoreactive proteins were detected in caprine and ovine milks [9].

References