Hormone glycosylation required for lutropin receptor recognition in sheep testis

Sairam, M.R.; Bhargavi, G. N.; Yarney, T.A.

doi:10.1016/0014-5793(90)80528-q

Cited by 3 publications

(1 citation statement)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For proteins other than TGF‐β ligands (e.g. hormones), it has been shown that glycosylation can ameliorate the receptor binding [14]; however, this is the first report in which glycosylation of a TGF‐β superfamily ligand is essential for the versatility in receptor binding.…”

mentioning

confidence: 99%

Type I receptor binding of bone morphogenetic protein 6 is dependent on N‐glycosylation of the ligand

Saremba¹,

Nickel²,

Seher³

et al. 2007

The FEBS Journal

View full text Add to dashboard Cite

Bone morphogenetic protein (BMP)-6, BMP-5, BMP-7 and BMP-8 constitute a subgroup of the transforming growth factor (TGF)-b superfamily proteins. Besides the ability of BMP-6 to induce bone formation at ectopic and orthotopic sites, BMP-6 transcripts have been localized in numerous studies to developing organs and tissues, such as the heart, the brain, and hypertrophic cartilage, throughout the developing skeletal system, and also to adult tissues, such as brain and uterus [1][2][3][4][5]. BMP-6 and its closest relative, BMP-7, show overlapping expression patterns as well as overlapping functions. For example, in the developing heart, BMP-6 and BMP-7 are required for cushion formation and septation [5]. In the brain, BMP-6 and Bone morphogenetic proteins (BMPs), together with transforming growth factor (TGF)-b and activins ⁄ inhibins, constitute the TGF-b superfamily of ligands. This superfamily is formed by more than 30 structurally related secreted proteins. The crystal structure of human BMP-6 was determined to a resolution of 2.1 Å ; the overall structure is similar to that of other TGF-b superfamily ligands, e.g. BMP-7. The asymmetric unit contains the full dimeric BMP-6, indicating possible asymmetry between the two monomeric subunits. Indeed, the conformation of several loops differs between both monomers. In particular, the prehelix loop, which plays a crucial role in the type I receptor interactions of BMP-2, adopts two rather different conformations in BMP-6, indicating possible dynamic flexibility of the prehelix loop in its unbound conformation. Flexibility of this loop segment has been discussed as an important feature required for promiscuous binding of different type I receptors to BMPs. Further studies investigating the interaction of BMP-6 with different ectodomains of type I receptors revealed that N-glycosylation at Asn73 of BMP-6 in the wrist epitope is crucial for recognition by the activin receptor type I. In the absence of the carbohydrate moiety, activin receptor type I-mediated signaling of BMP-6 is totally diminished. Thus, flexibility within the binding epitope of BMP-6 and an unusual recognition motif, i.e. an N-glycosylation motif, possibly play an important role in type I receptor specificity of BMP-6.

show abstract

mentioning

confidence: 99%

Type I receptor binding of bone morphogenetic protein 6 is dependent on N‐glycosylation of the ligand

Saremba¹,

Nickel²,

Seher³

et al. 2007

The FEBS Journal

View full text Add to dashboard Cite

show abstract

Chapter 11 The Glycoprotein Hormone Family: Structure and Function of the Carbohydrate Chains

Bielińska

Boime

1995

New Comprehensive Biochemistry

View full text Add to dashboard Cite

Influence of carbohydrates on the antigenic structure of gonadotropins: distinction of agonists and antagonists

Sairam¹,

Linggen²,

Sairam³

et al. 1990

Biochem. Cell Biol.

View full text Add to dashboard Cite

The biological properties of glycosylated (native) and deglycosylated gonadotropins are different. The immunological characteristics of antibodies prepared against deglycosylated lutropin and human chorionic gonadotropin were investigated. Distinct antibodies of rabbit polyclonal antisera against deglycosylated lutropin and deglycosylated chorionic gonadotropin were separated by affinity chromatography on divinylsulfonyl-Sepharose-immobilized hormone or antagonist columns, respectively, in successive runs. Antibodies that could discriminate between agonist and antagonistic forms of the hormones could thus be obtained. In radioimmunoassays using 125I-labeled antagonists and respective antagonist antibodies, only the deglycosylated hormones or their deglycosylated alpha-subunits showed preferential reaction. Based on recombinations using different deglycosylated subunits, it was concluded that the loss of antennary sugars in the alpha-subunits was mainly responsible for the changes that led to the formation of antagonist-specific antibodies. Only the agonist-specific antibody could neutralize hormone action. Thus, the type and extent of glycosylation appears to influence the antigenic structure of these secreted glycoproteins.

show abstract

Hormone glycosylation required for lutropin receptor recognition in sheep testis

Cited by 3 publications

References 17 publications

Type I receptor binding of bone morphogenetic protein 6 is dependent on N‐glycosylation of the ligand

Type I receptor binding of bone morphogenetic protein 6 is dependent on N‐glycosylation of the ligand

Chapter 11 The Glycoprotein Hormone Family: Structure and Function of the Carbohydrate Chains

Influence of carbohydrates on the antigenic structure of gonadotropins: distinction of agonists and antagonists

Contact Info

Product

Resources

About