| http://purl.uniprot.org/citations/27561202 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27561202 | http://www.w3.org/2000/01/rdf-schema#comment | "The hormone - specific FSHβ subunit of the human FSH heterodimer consists of N-linked glycans at Asn7 and Asn24 residues that are co-translationally attached early during subunit biosynthesis. Differences in the number of N-glycans (none, one or two) on the human FSHβ subunit contribute to macroheterogeneity in the FSH heterodimer. The resulting FSH glycoforms are termed hypo-glycosylated (FSH21/18, missing either an Asn24 or Asn7 N-glycan chain on the β - subunit, respectively) or fully glycosylated (FSH24, possessing of both Asn7 and Asn24 N-linked glycans on the β - subunit) FSH. The recombinant versions of human FSH glycoforms (FSH21/18 and FSH24) have been purified and biochemically characterized. In vitro functional studies have indicated that FSH21/18 exhibits faster FSH-receptor binding kinetics and is much more active than FSH24 in every assay tested to date. However, the in vivo bioactivity of the hypo-glycosylated FSH glycoform has never been tested. Here, we evaluated the in vivo bioactivities of FSH glycoforms in Fshb null mice using a pharmacological rescue approach. In Fshb null female mice, both hypo- and fully-glycosylated FSH elicited an ovarian weight gain response by 48 h and induced ovarian genes in a dose- and time-dependent manner. Quantification by real time qPCR assays indicated that hypo-glycosylated FSH21/18 was bioactive in vivo and induced FSH-responsive ovarian genes similar to fully-glycosylated FSH24. Western blot analyses followed by densitometry of key signaling components downstream of the FSH-receptor confirmed that the hypo-glycosylated FSH21/18 elicited a response similar to that by fully-glycosylated FSH24 in ovaries of Fshb null mice. When injected into Fshb null males, hypo-glycosylated FSH21/18 was more active than the fully-glycosylated FSH24 in inducing FSH-responsive genes and Sertoli cell proliferation. Thus, our data establish that recombinant hypo-glycosylated human FSH21/18 glycoform elicits bioactivity in vivo similar to the fully-glycosylated FSH. Our studies may have clinical implications particularly in formulating FSH-based ovarian follicle induction protocols using a combination of different human FSH glycoforms."xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.mce.2016.08.031"xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/author | "Wang H."xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/author | "Shuai B."xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/author | "May J."xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/author | "Kumar T.R."xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/author | "Bousfield G.R."xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/author | "May J.V."xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/author | "Butnev V."xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/name | "Mol Cell Endocrinol"xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/pages | "224-236"xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/title | "Evaluation of in vivo bioactivities of recombinant hypo- (FSHpisup>21/18pi/sup>) and fully- (FSHpisup>24pi/sup>) glycosylated human FSH glycoforms in Fshb null mice."xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://purl.uniprot.org/core/volume | "437"xsd:string |
| http://purl.uniprot.org/citations/27561202 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27561202 |
| http://purl.uniprot.org/citations/27561202 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/27561202 |
| http://purl.uniprot.org/uniprot/#_A0A0D9SGA7-mappedCitation-27561202 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/27561202 |
| http://purl.uniprot.org/uniprot/#_A0A087WYZ4-mappedCitation-27561202 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/27561202 |
| http://purl.uniprot.org/uniprot/#_A0A0F7RQE8-mappedCitation-27561202 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/27561202 |
| http://purl.uniprot.org/uniprot/#_A0A0F7RQR1-mappedCitation-27561202 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/27561202 |
| http://purl.uniprot.org/uniprot/#_C0KRQ8-mappedCitation-27561202 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/27561202 |
| http://purl.uniprot.org/uniprot/#_Q60687-mappedCitation-27561202 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/27561202 |
| http://purl.uniprot.org/uniprot/#_Q27RP3-mappedCitation-27561202 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/27561202 |
| http://purl.uniprot.org/uniprot/#_P01215-mappedCitation-27561202 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/27561202 |