Expression of a 95–100 kDa glycoprotein on the apical surfaces of bovine mammary epithelial cells during lactation

Kaetzel, Charlotte S.; Banghart, Lisa R.; Jackson, Dawn Y.; Madara, Patricia; Jarasch, Ernst-Dieter; Mather, Ian H.

doi:10.1042/bst0151117

Cited by 6 publications

(2 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The protein appears heterodisperse with apparent molecular mass ranging from 95 to over 100 kDa in polyacrylamide gels. Antibody staining of sections from bovine prelactating and lactating mammary gland using monoclonal and polyclonal antibodies has shown that PAS III is largely concentrated on apical surfaces of the mammary epithelial cells [23].…”

mentioning

confidence: 99%

Isolation and characterization of MUC15, a novel cell membrane‐associated mucin

Pallesen

Berglund

Rasmussen

et al. 2002

European Journal of Biochemistry

119

View full text Add to dashboard Cite

The present work reports isolation and characterization of a highly glycosylated protein from bovine milk fat globule membranes, known as PAS III. Partial amino-acid sequencing of the purified protein allowed construction of degenerate oligonucleotide primers, enabling isolation of a full-length cDNA encoding a protein of 330 amino-acid residues. N-terminal amino-acid sequencing of derived peptides and the purified protein confirmed 76% of the sequence and demonstrated presence of a cleavable signal peptide of 23 residues, leaving a mature protein of 307 amino acids. Database searches showed no homology to any other proteins. A survey of the human genome indicated the presence of a corresponding gene on chromosome band 11p14.3. Isolation and sequencing of the complete cDNA sequence of the human homologue proved the existence of the gene product (334 amino-acid residues). This novel mucin-like protein was named MUC15 by appointment of the HUGO Gene Nomenclature Committee. The deduced amino-acid sequences of human and bovine MUC15 demonstrated structural hallmarks characteristic for other membrane-bound mucins, such as a serine, threonine, and proline-rich extracellular region with several potential glycosylation sites, a putative transmembrane domain, and a short cytoplasmic C-terminal. We have shown the presence of O-glycosylations, identified N-glycosylations at 11 of 15 potential sites in bovine MUC15, and a splice variant encoding a short secreted mucin. Finally, analysis of human and bovine cDNA panels and libraries showed MUC15 gene expression in adult human spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocyte, bone marrow, lymph node, tonsil, breast, fetal liver, bovine lymph nodes and lungs of both species.

show abstract

mentioning

confidence: 99%

Isolation and characterization of MUC15, a novel cell membrane‐associated mucin

Pallesen

Berglund

Rasmussen

et al. 2002

European Journal of Biochemistry

119

View full text Add to dashboard Cite

show abstract

“…A second mucin, MUC15, previously called PAS III, in bovine MFGM (Kaetzel et al, 1987;Mather, 2000), has been isolated recently and characterized by biochemical and molecular cloning techniques (EMBL accession number AJ417816; Pallesen et al, 2002). The human homologue also was cloned and shares 67% similarity in linear sequence with bovine MUC15.…”

Section: Proteins Of the Mfgmmentioning

confidence: 98%

Intracellular Origin of Milk Fat Globules and the Nature of the Milk Fat Globule Membrane

Keenan

Mather

Advanced Dairy Chemistry Volume 2 Lipids

107

162

View full text Add to dashboard Cite

In this chapter, we review what is known about the intracellular origin, growth, cytoplasmic transit and secretion of the lipid globules of milk, and the nature and intracellular origin of the milk fat globule membrane (MFGM). Material found in the MFGM appears to originate from the endoplasmic reticulum during the initial formation of the lipid droplet precursors of milk fat globules, and from post-Golgi membranes, including the apical plasma membrane, during the secretion of lipid droplets from the cell. Milk fat globules constitute 95%, by weight, of the lipids in cow's milk, of which more than 98% comprise triacylglycerols. The remainder of the mass of fat globules is composed of diacylglycerols, sterols, sterol esters, phospholipids, glycosphingolipids, and proteins associated with the droplet surface.In writing this chapter we have emphasized Wndings since the previous edition of this book was published in 1994. Much of the new information gained in this area concerns the proteins of the MFGM. Since the previous edition, there have been few additional studies on intracellular aspects of milk lipid globule formation and on the composition of the MFGM. For those interested in earlier literature and coverage of historical aspects of research on milk lipid globules, the comprehensive review by Brunner (1974) and later reviews (Anderson and Cawston, 1975;Patton and Keenan, 1975;

show abstract

Establishment and characterization of bovine mammary epithelial cell lines

Gibson

Vega

Baumrucker

et al. 1991

In Vitro Cell Dev Biol - Animal

View full text Add to dashboard Cite

One bovine mammary epithelial cell clone, designated PS-BME-Cl, and two bovine mammary epithelial cell lines, designated PS-BME-L6 and PS-BME-L7, were derived from mammary tissue of a pregnant (270 day) Holstein cow. The cells exhibit the distinctive morphologic characteristics of mammary epithelial cells and express the milk fat globule membrane protein, PAS-III. They form domes when cultured on plastic substrata and acinilike aggregates when cultured on a collagen matrix. These cells are capable of synthesizing and secreting alpha-lactalbumin and alpha-s1-casein when cultured on a collagen matrix in the presence of insulin, cortisol, and prolactin. The cells have a near-normal diploid number and do not grow in suspension culture. When transplanted to the cleared mammary fat pads of female athymic nude mice, the cells readily proliferate forming noninvasive palpable spherical cellular masses within 8 wk after inoculation. The cells may become a useful tool to study the regulation of ruminant mammary epithelial cell growth and differentiation.

show abstract

Expression of a 95–100 kDa glycoprotein on the apical surfaces of bovine mammary epithelial cells during lactation

Cited by 6 publications

References 0 publications

Isolation and characterization of MUC15, a novel cell membrane‐associated mucin

Isolation and characterization of MUC15, a novel cell membrane‐associated mucin

Intracellular Origin of Milk Fat Globules and the Nature of the Milk Fat Globule Membrane

Establishment and characterization of bovine mammary epithelial cell lines

Contact Info

Product

Resources

About