High-<i>M</i>r glycoprotein profiles in human milk serum and fat-globule membrane

Shimizu, Masatoshi; Yamauchi, Kiyoshi; Miyauchi, Yuu; Sakurai, T; Tokugawa, Kazuhisa; McIlhinney, R. A. Jeffrey

doi:10.1042/bj2330725

Cited by 42 publications

(22 citation statements)

References 24 publications

(27 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The second milk mucin, variously called component A and MUCX, has a higher apparent M r , is more heavily glycosylated, and has not been well characterized (21,28). Based on the studies described here and comparative amino acid compositions (28,29), ASGP-1 is a likely candidate for component A/MUCX. Component A was originally described as being associated with the human milk fat globule membrane (28).…”

Section: Analysis Of Asgp-2 Transcripts By Rt-pcr-mentioning

confidence: 99%

“…The best characterized is MUC1, the polymorphic epithelial mucin (4,5,(25)(26)(27). The second milk mucin, variously called component A and MUCX, has a higher apparent M r , is more heavily glycosylated, and has not been well characterized (21,28). Based on the studies described here and comparative amino acid compositions (28,29), ASGP-1 is a likely candidate for component A/MUCX.…”

Section: Analysis Of Asgp-2 Transcripts By Rt-pcr-mentioning

confidence: 99%

“…Based on the studies described here and comparative amino acid compositions (28,29), ASGP-1 is a likely candidate for component A/MUCX. Component A was originally described as being associated with the human milk fat globule membrane (28). However, no milk mucins are found in the fat globule membranes of the rat (30).…”

Section: Analysis Of Asgp-2 Transcripts By Rt-pcr-mentioning

confidence: 99%

See 2 more Smart Citations

Sialomucin Complex, a Heterodimeric Glycoprotein Complex

Rossi¹,

McNeer²,

Price‐Schiavi³

et al. 1996

Journal of Biological Chemistry

109

View full text Add to dashboard Cite

Ascites 13762 rat mammary adenocarcinoma cells express abundantly on their cell surfaces a heterodimeric glycoprotein complex composed of a sialomucin ascites sialoglycoprotein (ASGP)-1 and a transmembrane subunit ASGP-2. The latter, which contains two epidermal growth factor-like domains, binds the receptor tyrosine kinase p185 neu , suggesting that the complex is bifunctional as well as heterodimeric. Immunoblot analyses using monoclonal antibodies prepared against the complex demonstrate high levels of expression in rat lactating mammary gland and colon. Immunolocalization studies with anti-ASGP-2 indicate that ASGP-2 is present in these two tissues in the apical regions of secretory epithelial cells. Both mammary gland and colon contain a soluble, secretable form of ASGP-2, which is not found in the ascites cells; milk and mammary gland also have the membrane form. Immunoblot analyses using a COOH-terminal-specific polyclonal antibody indicate that the soluble form of ASGP-2 is missing its COOHterminal domains. Both the soluble and membrane forms of ASGP-2 are similar to the membrane-associated form from the 13762 adenocarcinoma with respect to M r , antigenicity, and association with ASGP-1. The presence of ASGP-1 in milk suggests that it is a candidate for the uncharacterized high M r milk mucin, MUCX. ASGP-2 expression is up-regulated in mammary gland during pregnancy, because it is undetectable in virgin and early pregnant rats but abundant in the gland from late pregnant and lactating animals. However, compared with the lactating mammary gland, the 13762 ascites cells overexpress ASGP-2 by more than 100-fold, which may contribute to their malignancy. These combined results indicate that sialomucin complex is a unique secreted product in the mammary gland and colon, whose behavior is different from that in the mammary ascites tumors, and which may play important roles in mammary and intestinal physiology.

show abstract

Section: Analysis Of Asgp-2 Transcripts By Rt-pcr-mentioning

confidence: 99%

Section: Analysis Of Asgp-2 Transcripts By Rt-pcr-mentioning

confidence: 99%

Section: Analysis Of Asgp-2 Transcripts By Rt-pcr-mentioning

confidence: 99%

See 1 more Smart Citation

Sialomucin Complex, a Heterodimeric Glycoprotein Complex

Rossi¹,

McNeer²,

Price‐Schiavi³

et al. 1996

Journal of Biological Chemistry

109

View full text Add to dashboard Cite

show abstract

“…In 1982 Shimizu and Yamauchi S ) originally reported the presence of one HMGP (HMGP-C) in human milk. More recently, Shimizu et al 6 ) reported the occurrence of the other HMGP (HMGP-A and HMGP-B) with a much larger molecular size and containing more carbohydrate (80% (w/w».…”

mentioning

confidence: 99%

Reactivity of the High-M_rMucin-like Glycoproteins in Human Milk with Monoclonal Antibodies HMFG-1 and HMFG-2

Kanamaru

Nagaoka

Kuzuya

et al. 1993

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

“…That notwithstanding, the major human milk mucins have been identified, initially as mucin 1 and a higher-molecular-weight electrophoresis band, 18,19 designated mucin X. 20,21 Recently our laboratory purified mucin 4 from human milk and identified it ( Fig.…”

mentioning

confidence: 99%

Human Milk Glycoproteins Protect Infants Against Human Pathogens

Liu

Newburg

2013

Breastfeeding Medicine

139

104

View full text Add to dashboard Cite

Breastfeeding protects the neonate against pathogen infection. Major mechanisms of protection include human milk glycoconjugates functioning as soluble receptor mimetics that inhibit pathogen binding to the mucosal cell surface, prebiotic stimulation of gut colonization by favorable microbiota, immunomodulation, and as a substrate for bacterial fermentation products in the gut. Human milk proteins are predominantly glycosylated, and some biological functions of these human milk glycoproteins (HMGPs) have been reported. HMGPs range in size from 14 kDa to 2,000 kDa and include mucins, secretory immunoglobulin A, bile salt-stimulated lipase, lactoferrin, butyrophilin, lactadherin, leptin, and adiponectin. This review summarizes known biological roles of HMGPs that may contribute to the ability of human milk to protect neonates from disease.

show abstract

High-Mr glycoprotein profiles in human milk serum and fat-globule membrane

Cited by 42 publications

References 24 publications

Sialomucin Complex, a Heterodimeric Glycoprotein Complex

Sialomucin Complex, a Heterodimeric Glycoprotein Complex

Reactivity of the High-M_rMucin-like Glycoproteins in Human Milk with Monoclonal Antibodies HMFG-1 and HMFG-2

Human Milk Glycoproteins Protect Infants Against Human Pathogens

Contact Info

Product

Resources

About

High-Mr glycoprotein profiles in human milk serum and fat-globule membrane

Cited by 42 publications

References 24 publications

Sialomucin Complex, a Heterodimeric Glycoprotein Complex

Sialomucin Complex, a Heterodimeric Glycoprotein Complex

Reactivity of the High-MrMucin-like Glycoproteins in Human Milk with Monoclonal Antibodies HMFG-1 and HMFG-2

Human Milk Glycoproteins Protect Infants Against Human Pathogens

Contact Info

Product

Resources

About

Reactivity of the High-M_rMucin-like Glycoproteins in Human Milk with Monoclonal Antibodies HMFG-1 and HMFG-2